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Conserved domains on  [gi|166797876|gb|ABY89499|]
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iturin A synthetase B [Bacillus subtilis]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1004279)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12316 super family cl36106
peptide synthase; Provisional
1314-5332 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2707.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1314 EAENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKK 1393
Cdd:PRK12316   45 SSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRG-ADDSLAQVPLDRP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1394 IGFQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYF 1473
Cdd:PRK12316  124 LEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1474 ALLQQKQPEQSSI-TPYSQYIEWLGR-QDAKEAA---AYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTS 1548
Cdd:PRK12316  204 AYATGAEPGLPALpIQYADYALWQRSwLEAGEQErqlEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1549 KMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGipNVETMIGLFINTIPVRFRCEAGTTFAELMKEA 1628
Cdd:PRK12316  284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA--EVEGLIGFFVNTQVLRSVFDGRTRVATLLAGV 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1629 QERAVASQKFETHPlYDIQARTTQKQDLITHLMIFE----NYPVDQYMESIGRQNGTSITISNVQmEEQTNYDFNL-TVI 1703
Cdd:PRK12316  362 KDTVLGAQAHQDLP-FERLVEALKVERSLSHSPLFQvmynHQPLVADIEALDTVAGLEFGQLEWK-SRTTQFDLTLdTYE 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1704 PGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLFEE 1782
Cdd:PRK12316  440 KGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPlQRGVHRLFEE 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1783 QSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDR 1862
Cdd:PRK12316  520 QVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAER 599
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 IRYMLDDSQAGIVLMQRDVRKQLAY-EGVTVL-LDDESSYHQDGSDLAPISDVS--HLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:PRK12316  600 LAYMLEDSGVQLLLSQSHLGRKLPLaAGVQVLdLDRPAAWLEGYSEENPGTELNpeNLAYVIYTSGSTGKPKGAGNRHRA 679
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 LTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVY---DGEDKTALLESIVRDpRVDIIKLTPAHLQ 2015
Cdd:PRK12316  680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINRE-GVDTLHFVPSMLQ 758
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 -VLKEMNIADQTAVRRMIVGGENLSTrlarSIHEQFEGRI---EICNEYGPTETVVG-CMIYRYDAAKDrreSVPIGTAA 2090
Cdd:PRK12316  759 aFLQDEDVASCTSLRRIVCSGEALPA----DAQEQVFAKLpqaGLYNLYGPTEAAIDvTHWTCVEEGGD---SVPIGRPI 831
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2091 ANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQ 2170
Cdd:PRK12316  832 ANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 911
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2171 VKIRGYRIELGEIEAALLQEEVIKEAVVTAREDvhgfKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEM 2248
Cdd:PRK12316  912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGYVVleSEGGDWREALKAHLAASLPEYMVPAQWLALERL 987
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2249 PLTSNGKINKKGLPAPDFELQdRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQGYKM 2328
Cdd:PRK12316  988 PLTPNGKLDRKALPAPEASVA-QQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQL 1066
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2329 EIKDLFQYATIAELSPHIKQNLRIA-DQGEVKGKVSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLA 2407
Cdd:PRK12316 1067 SPRDLFQHQTIRSLALVAKAGQATAaDQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLV 1146
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2408 EHHDALRMTFRTTENGC-EAQNEEIAQSGLYRLEVMNLKEdpdpgrtIEAKADEIQSSMHLSDGPLMKAGLFQCADGDH- 2485
Cdd:PRK12316 1147 AHHDALRLRFREEDGGWqQAYAAPQAGEVLWQRQAASEEE-------LLALCEEAQRSLDLEQGPLLRALLVDMADGSQr 1219
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2486 LLIAIHHLIIDGISWRILLEDIVSGYKQAengrVIQLPQKTDSFQLWAKRLSEYAQSETikQEQEYWTKIEQTEVKPLPK 2565
Cdd:PRK12316 1220 LLLVIHHLVVDGVSWRILLEDLQRAYADL----DADLPARTSSYQAWARRLHEHAGARA--EELDYWQAQLEDAPHELPC 1293
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2566 DFHETHTTAKDSETAAVEWTKEETELLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDISR 2645
Cdd:PRK12316 1294 ENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSR 1373
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2646 TVGWFTSLYPVVLHaqPGKEISDYIKTTKEGLRQIPHKGIGYGIARYLSGG-----MPSKLNPEISFNYLGQFDQDLQRH 2720
Cdd:PRK12316 1374 TVGWFTSLFPVRLT--PAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEeaaarLAALPQPRITFNYLGQFDRQFDEA 1451
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2721 GVqLSSYSCGSDSSGHQERPYV--LNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHCVHKEQSELTP 2798
Cdd:PRK12316 1452 AL-FVPATESAGAAQDPCAPLAnwLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTP 1530
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2799 SDILLKGISIDELDQLLIQlphAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGeLKIDWFKASLERLFETY 2878
Cdd:PRK12316 1531 SDFPLAGLSQAQLDALPLP---AGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRH 1606
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2879 AVLRTRFY--SGWnDTPLQIVYKTQtpQIHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHL 2956
Cdd:PRK12316 1607 EILRSGFLwqDGL-EQPLQVIHKQV--ELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHL 1683
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2957 IWSFHHIVMDGWCLSLITKEVFDHYSalqeGREPePLSAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKgETTLLHKIAQ 3036
Cdd:PRK12316 1684 IYTNHHILMDGWSNAQLLGEVLQRYA----GQPV-AAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALE-EPTRLAQAAR 1757
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3037 HEQKEYAYANLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFIN 3116
Cdd:PRK12316 1758 TEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFIN 1837
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3117 TIPVRIRCDEDSTFADTMQMVQQNALASQSYDTYPLYEIQAQTEQK-QNLIDHIMIFENYPIGQQAEETGHHGteLNITN 3195
Cdd:PRK12316 1838 TLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGgEALFDSLLVFENYPVAEALKQGAPAG--LVFGR 1915
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3196 FHMQEHSHYDLNVVVIPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSN 3275
Cdd:PRK12316 1916 VSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRT 1995
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3276 DMHYPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLK 3355
Cdd:PRK12316 1996 PEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLK 2075
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3356 AGGAYLPIDPDSPSERIRYILNDSSISVLLYCGKLQDDIGFSG--TCIDL---MEEHFYHEKDSSLALSYQSsqLAYAIY 3430
Cdd:PRK12316 2076 AGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAgvARLPLdrdAEWADYPDTAPAVQLAGEN--LAYVIY 2153
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3431 TSGTTGKPKGTLIEHRQVI-HLIEGLSRQVYSAYDAELNiamLAPYYFDASVQQMYASLLSGHTLFIVPKEIvSDGAALC 3509
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVaHCQAAGERYELSPADCELQ---FMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLY 2229
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3510 RYYRQHSIDITDGTPAHLKLLIAAGDLQGVT--LQHLLIGGEALSKTTVNKLKQLFGehgaAPGITNVYGPTETCVDASL 3587
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQLAEHAERDGRPpaVRVYCFGGEAVPAASLRLAWEALR----PVYLFNGYGPTEAVVTPLL 2305
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3588 FNIeCSSDAWARSqnYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRM 3666
Cdd:PRK12316 2306 WKC-RPQDPCGAA--YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERL 2382
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3667 YRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYyLCGYFAAD--KTIQISE 3744
Cdd:PRK12316 2383 YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQ-LVAYVVPDdaAEDLLAE 2461
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3745 LRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKKRDSGiEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHF 3824
Cdd:PRK12316 2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ-AYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHF 2540
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3825 FEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLARTITKTELTGYAAIPAIEKRPYYPVSSAQKRLYILNHLEG 3904
Cdd:PRK12316 2541 FELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEP 2620
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3905 GELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEA--EWYQGEEDDADLY--IRQF 3980
Cdd:PRK12316 2621 ESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIvlEDCAGVADAAIRQrvAEEI 2700
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3981 IRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGE------TLPPLRIQYKDYAVWQTGEA 4054
Cdd:PRK12316 2701 QRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGArrgeqpTLPPLPLQYADYAAWQRAWM 2780
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4055 RLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKY 4134
Cdd:PRK12316 2781 DSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRY 2860
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4135 SGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIARDLSR 4214
Cdd:PRK12316 2861 SGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSH 2940
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4215 NPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSI 4294
Cdd:PRK12316 2941 SPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGM 3020
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4295 IKQPEAELARLNMMTKEEERDIQQLFNDTAvAEKRIPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVL 4374
Cdd:PRK12316 3021 VENPQRSVDELAMLDAEERGQLLEAWNATA-AEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRL 3099
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4375 QDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTcAGHAIPPLFEGEVLLLDD 4454
Cdd:PRK12316 3100 IERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-QSHLRLPLAQGVQVLDLD 3178
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4455 PLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSA 4533
Cdd:PRK12316 3179 RGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVgDRVLQFTTFSFDVFVEELFWP 3258
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4534 LSSGGILFIIGNEAKRDIRQLNDFVRTHGIQ-TAFLPTAFLKLLASEKhyfEPFAECVDHIIAAGEQLIATRMLRDMLar 4612
Cdd:PRK12316 3259 LMSGARVVLAGPEDWRDPALLVELINSEGVDvLHAYPSMLQAFLEEED---AHRCTSLKRIVCGGEALPADLQQQVFA-- 3333
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4613 hQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLE 4692
Cdd:PRK12316 3334 -GLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAE 3412
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4693 TFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTdgQSDLYAY 4770
Cdd:PRK12316 3413 RFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHpwVREAVVLAVDGR--QLVAYVV 3490
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4771 FTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQTgTDYVAPRTNMEEQLICIWQDVL 4850
Cdd:PRK12316 3491 PEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQ-QDYVAPVNELERRLAAIWADVL 3569
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4851 KVKEIGVKDNFFDLGGHSLRGMTLIAKIhKQFSKNISLREVFQCPTVGEMAQAiaeAETNGpdyipkAKAKDVYPVSSVQ 4930
Cdd:PRK12316 3570 KLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLARV---ARVGG------GVAVDQGPVSGET 3639
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4931 KMVYLTTQIIGGELP----YNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVemVREEAV-QVIKSQVEFSME-RYE 5004
Cdd:PRK12316 3640 LLLPIQQQFFEEPVPerhhWNQSLLLKPREALDAAALEAALQALVEHHDALRLRF--VEDAGGwTAEHLPVELGGAlLWR 3717
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5005 ATADEVEECFR---AFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLY------DGKELAP 5075
Cdd:PRK12316 3718 AELDDAEELERlgeEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllqgEAPRLPA 3797
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5076 LRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFhEELPSfELPKDFARPPVRSFDGKRHNFTLDKTVT-QGIKQLEELTGS 5154
Cdd:PRK12316 3798 KTSSFKAWAERLQEHARGEALKAELAYWQEQL-QGVSS-ELPCDHPQGALQNRHAASVQTRLDRELTrRLLQQAPAAYRT 3875
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5155 TAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPH----ADLEPIIGMFVNTLAIRTAPMAEktFLDYITETKEtMLKAFE 5230
Cdd:PRK12316 3876 QVNDLLLTALARVVCRWTGEASALVQLEGHGREDlfadIDLSRTVGWFTSLFPVRLSPVED--LGASIKAIKE-QLRAIP 3952
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5231 HQEYPFeELVEKLG---VKRDLSRNPLFDTMF--VLQNTEQTDIE----VDSLAVRPYEQTETAAKFD-LQLNFLIDQDE 5300
Cdd:PRK12316 3953 NKGIGF-GLLRYLGdeeSRRTLAGLPVPRITFnyLGQFDGSFDEEmalfVPAGESAGAEQSPDAPLDNwLSLNGRVYGGE 4031
                        4090      4100      4110
                  ....*....|....*....|....*....|..
gi 166797876 5301 IQGSFDYCTKLFKKKTIAVLAKDYVMILSAIM 5332
Cdd:PRK12316 4032 LSLDWTFSREMFEEATIQRLADDYAAELTALV 4063
PRK12467 super family cl36129
peptide synthase; Provisional
7-2343 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1819.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    7 QETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDR 86
Cdd:PRK12467 1304 QLAYWKAQLGGEQPVLELP----TDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQ 1379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   87 TSLILGIPTVSKQKAGQSA-----VNNIVLlKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMP 161
Cdd:PRK12467 1380 DDIRVGVPIANRNRAETEGligffVNTQVL-RAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSP 1458
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  162 LIHtvVSLN---------------EIHSLQCKEDTAtdtlfHFDLENN------GIHLKLFYNGNLYDERYINQIVSHLD 220
Cdd:PRK12467 1459 LFQ--VMFNhqrddhqaqaqlpglSVESLSWESQTA-----QFDLTLDtyesseGLQASLTYATDLFEASTIERLAGHWL 1531
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  221 QLLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASR 300
Cdd:PRK12467 1532 NLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANR 1611
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  301 LARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSLAF-DG- 378
Cdd:PRK12467 1612 LAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLpDGl 1691
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  379 PVIDLNDEASYHADCSLLSP--VAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFD 456
Cdd:PRK12467 1692 RSLVLDQEDDWLEGYSDSNPavNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFD 1771
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  457 AFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNR-EDFIHVQHVVVGGEQLETDTV 535
Cdd:PRK12467 1772 VSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQvEHPLSLRRVVCGGEALEVEAL 1851
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  536 EKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ----ITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARG 611
Cdd:PRK12467 1852 RPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEgrdsVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARG 1931
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  612 YLNRPELTEEKFV-EHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVARE 690
Cdd:PRK12467 1932 YLNRPALTAERFVaDPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  691 DAdGAKQLYAYYV----------GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADEnTRAEN 760
Cdd:PRK12467 2012 GA-NGKQLVAYVVptdpglvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDA-SELQQ 2089
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  761 EYIAPRNTIEELLASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQfVAPVSR- 839
Cdd:PRK12467 2090 AYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAA-VAQEGDg 2168
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  840 --VADQGEVNGGTKLTPIQHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGY--APR 915
Cdd:PRK12467 2169 tvSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWsaMHR 2248
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  916 ITGTDESELFHLEVMNYKGETdpaQAIADKAneiQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLED 994
Cdd:PRK12467 2249 APEQERRPLLWQVVVADKEEL---EALCEQA---QRSLDLEEGPLLRAVLATLPDGSQrLLLVIHHLVVDGVSWRILLED 2322
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  995 FASGYEQAERRQTIQLPQKTDSFPFWADQLSKYAAETDMEEEIAYW-TELSSIkPQPLPKDTISEGSLLRDSEEVTIQWT 1073
Cdd:PRK12467 2323 LQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWqAQLQGA-STELPCDHPQGGLQRRHAASVTTHLD 2401
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1074 KEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPDADISRTIGWFTSQYPVvlRMEAGKN 1153
Cdd:PRK12467 2402 SEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPV--KLSPTAS 2479
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1154 LSQRIKIVKEGLRRIPDKGMNYSIIKYIsGHPEA-DSLQL--KPEISFNYLGQFDQ--DLKHQALrISPfsTGLSMNENQ 1228
Cdd:PRK12467 2480 LATSIKTIKEQLRAVPNKGLGFGVLRYL-GSEAArQTLQAlpVPRITFNYLGQFDGsfDAEKQAL-FVP--SGEFSGAEQ 2555
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1229 ERTAVLD----LNGMIAEGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHCVSRQQTSLTPSDILLKDISIDELEQ 1304
Cdd:PRK12467 2556 SEEAPLGnwlsINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDR 2635
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1305 LleqTRELGEAENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGdLEIDSFSKSLDGLSQKYDIFRTNF-YRGWKDQ 1383
Cdd:PRK12467 2636 L---PVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlWDGELEE 2711
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1384 PLQIIFKTKKIGFQFNDLREMKESQKEamIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPL 1463
Cdd:PRK12467 2712 PLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQ 2789
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1464 ITKEIFENYFAllqqkQPEQSSITPYSQYIEWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAE-DGRYVPEKVTCDI 1542
Cdd:PRK12467 2790 LLGEVLQRYFG-----QPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPaEAVAGHGAHYLHL 2864
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1543 SSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFA 1622
Cdd:PRK12467 2865 DATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVS 2944
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1623 ELMKEAQERAVASQKFETHPLYDIQARTTQ-KQDLITHLMIFENYPVDqymESIGRQNGTSITISNVQMEEQTNYDFNLT 1701
Cdd:PRK12467 2945 DWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPIS---EALKQGAPSGLRFGAVSSREQTNYPLTLA 3021
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1702 VIPGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLF 1780
Cdd:PRK12467 3022 VGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPsERLVHQLI 3101
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1781 EEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQ 1860
Cdd:PRK12467 3102 EAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPR 3181
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1861 DRIRYMLDDSQAGIVLMQRDVRKQLAYEGV--TVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:PRK12467 3182 ERLAYMIEDSGVKLLLTQAHLLEQLPAPAGdtALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGA 3261
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 LTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKT-ALLESIVRDPRVDIIKLTPAHLQVL 2017
Cdd:PRK12467 3262 LANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDpEELWQAIHAHRISIACFPPAYLQQF 3341
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2018 KEM-NIADQTAVRRMIVGGEnlstRLARSIHEQFEGRIE---ICNEYGPTETVVGCMIYRYDA-AKDRRESVPIGTAAAN 2092
Cdd:PRK12467 3342 AEDaGGADCASLDIYVFGGE----AVPPAAFEQVKRKLKprgLTNGYGPTEAVVTVTLWKCGGdAVCEAPYAPIGRPVAG 3417
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2093 TSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFE-PGAKMYKTGDLAKWLADGNIEYAGRIDEQV 2171
Cdd:PRK12467 3418 RSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQV 3497
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2172 KIRGYRIELGEIEAALLQEEVIKEAVVTAReDVHGFKQLCAYYVSG--GQTTAARLRKQLSQTLASYMVPAYFIELDEMP 2249
Cdd:PRK12467 3498 KIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAdpQGDWRETLRDHLAASLPDYMVPAQLLVLAAMP 3576
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2250 LTSNGKINKKGLPAPDFELQDraEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQ-GYKM 2328
Cdd:PRK12467 3577 LGPNGKVDRKALPDPDAKGSR--EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKL 3654
                        2410
                  ....*....|....*
gi 166797876 2329 EIKDLFQYATIAELS 2343
Cdd:PRK12467 3655 SLRDLMSAPTIAELA 3669
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
1314-5332 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2707.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1314 EAENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKK 1393
Cdd:PRK12316   45 SSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRG-ADDSLAQVPLDRP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1394 IGFQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYF 1473
Cdd:PRK12316  124 LEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1474 ALLQQKQPEQSSI-TPYSQYIEWLGR-QDAKEAA---AYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTS 1548
Cdd:PRK12316  204 AYATGAEPGLPALpIQYADYALWQRSwLEAGEQErqlEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1549 KMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGipNVETMIGLFINTIPVRFRCEAGTTFAELMKEA 1628
Cdd:PRK12316  284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA--EVEGLIGFFVNTQVLRSVFDGRTRVATLLAGV 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1629 QERAVASQKFETHPlYDIQARTTQKQDLITHLMIFE----NYPVDQYMESIGRQNGTSITISNVQmEEQTNYDFNL-TVI 1703
Cdd:PRK12316  362 KDTVLGAQAHQDLP-FERLVEALKVERSLSHSPLFQvmynHQPLVADIEALDTVAGLEFGQLEWK-SRTTQFDLTLdTYE 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1704 PGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLFEE 1782
Cdd:PRK12316  440 KGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPlQRGVHRLFEE 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1783 QSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDR 1862
Cdd:PRK12316  520 QVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAER 599
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 IRYMLDDSQAGIVLMQRDVRKQLAY-EGVTVL-LDDESSYHQDGSDLAPISDVS--HLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:PRK12316  600 LAYMLEDSGVQLLLSQSHLGRKLPLaAGVQVLdLDRPAAWLEGYSEENPGTELNpeNLAYVIYTSGSTGKPKGAGNRHRA 679
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 LTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVY---DGEDKTALLESIVRDpRVDIIKLTPAHLQ 2015
Cdd:PRK12316  680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINRE-GVDTLHFVPSMLQ 758
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 -VLKEMNIADQTAVRRMIVGGENLSTrlarSIHEQFEGRI---EICNEYGPTETVVG-CMIYRYDAAKDrreSVPIGTAA 2090
Cdd:PRK12316  759 aFLQDEDVASCTSLRRIVCSGEALPA----DAQEQVFAKLpqaGLYNLYGPTEAAIDvTHWTCVEEGGD---SVPIGRPI 831
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2091 ANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQ 2170
Cdd:PRK12316  832 ANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 911
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2171 VKIRGYRIELGEIEAALLQEEVIKEAVVTAREDvhgfKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEM 2248
Cdd:PRK12316  912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGYVVleSEGGDWREALKAHLAASLPEYMVPAQWLALERL 987
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2249 PLTSNGKINKKGLPAPDFELQdRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQGYKM 2328
Cdd:PRK12316  988 PLTPNGKLDRKALPAPEASVA-QQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQL 1066
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2329 EIKDLFQYATIAELSPHIKQNLRIA-DQGEVKGKVSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLA 2407
Cdd:PRK12316 1067 SPRDLFQHQTIRSLALVAKAGQATAaDQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLV 1146
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2408 EHHDALRMTFRTTENGC-EAQNEEIAQSGLYRLEVMNLKEdpdpgrtIEAKADEIQSSMHLSDGPLMKAGLFQCADGDH- 2485
Cdd:PRK12316 1147 AHHDALRLRFREEDGGWqQAYAAPQAGEVLWQRQAASEEE-------LLALCEEAQRSLDLEQGPLLRALLVDMADGSQr 1219
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2486 LLIAIHHLIIDGISWRILLEDIVSGYKQAengrVIQLPQKTDSFQLWAKRLSEYAQSETikQEQEYWTKIEQTEVKPLPK 2565
Cdd:PRK12316 1220 LLLVIHHLVVDGVSWRILLEDLQRAYADL----DADLPARTSSYQAWARRLHEHAGARA--EELDYWQAQLEDAPHELPC 1293
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2566 DFHETHTTAKDSETAAVEWTKEETELLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDISR 2645
Cdd:PRK12316 1294 ENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSR 1373
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2646 TVGWFTSLYPVVLHaqPGKEISDYIKTTKEGLRQIPHKGIGYGIARYLSGG-----MPSKLNPEISFNYLGQFDQDLQRH 2720
Cdd:PRK12316 1374 TVGWFTSLFPVRLT--PAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEeaaarLAALPQPRITFNYLGQFDRQFDEA 1451
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2721 GVqLSSYSCGSDSSGHQERPYV--LNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHCVHKEQSELTP 2798
Cdd:PRK12316 1452 AL-FVPATESAGAAQDPCAPLAnwLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTP 1530
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2799 SDILLKGISIDELDQLLIQlphAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGeLKIDWFKASLERLFETY 2878
Cdd:PRK12316 1531 SDFPLAGLSQAQLDALPLP---AGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRH 1606
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2879 AVLRTRFY--SGWnDTPLQIVYKTQtpQIHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHL 2956
Cdd:PRK12316 1607 EILRSGFLwqDGL-EQPLQVIHKQV--ELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHL 1683
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2957 IWSFHHIVMDGWCLSLITKEVFDHYSalqeGREPePLSAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKgETTLLHKIAQ 3036
Cdd:PRK12316 1684 IYTNHHILMDGWSNAQLLGEVLQRYA----GQPV-AAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALE-EPTRLAQAAR 1757
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3037 HEQKEYAYANLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFIN 3116
Cdd:PRK12316 1758 TEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFIN 1837
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3117 TIPVRIRCDEDSTFADTMQMVQQNALASQSYDTYPLYEIQAQTEQK-QNLIDHIMIFENYPIGQQAEETGHHGteLNITN 3195
Cdd:PRK12316 1838 TLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGgEALFDSLLVFENYPVAEALKQGAPAG--LVFGR 1915
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3196 FHMQEHSHYDLNVVVIPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSN 3275
Cdd:PRK12316 1916 VSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRT 1995
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3276 DMHYPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLK 3355
Cdd:PRK12316 1996 PEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLK 2075
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3356 AGGAYLPIDPDSPSERIRYILNDSSISVLLYCGKLQDDIGFSG--TCIDL---MEEHFYHEKDSSLALSYQSsqLAYAIY 3430
Cdd:PRK12316 2076 AGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAgvARLPLdrdAEWADYPDTAPAVQLAGEN--LAYVIY 2153
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3431 TSGTTGKPKGTLIEHRQVI-HLIEGLSRQVYSAYDAELNiamLAPYYFDASVQQMYASLLSGHTLFIVPKEIvSDGAALC 3509
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVaHCQAAGERYELSPADCELQ---FMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLY 2229
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3510 RYYRQHSIDITDGTPAHLKLLIAAGDLQGVT--LQHLLIGGEALSKTTVNKLKQLFGehgaAPGITNVYGPTETCVDASL 3587
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQLAEHAERDGRPpaVRVYCFGGEAVPAASLRLAWEALR----PVYLFNGYGPTEAVVTPLL 2305
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3588 FNIeCSSDAWARSqnYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRM 3666
Cdd:PRK12316 2306 WKC-RPQDPCGAA--YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERL 2382
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3667 YRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYyLCGYFAAD--KTIQISE 3744
Cdd:PRK12316 2383 YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQ-LVAYVVPDdaAEDLLAE 2461
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3745 LRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKKRDSGiEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHF 3824
Cdd:PRK12316 2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ-AYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHF 2540
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3825 FEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLARTITKTELTGYAAIPAIEKRPYYPVSSAQKRLYILNHLEG 3904
Cdd:PRK12316 2541 FELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEP 2620
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3905 GELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEA--EWYQGEEDDADLY--IRQF 3980
Cdd:PRK12316 2621 ESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIvlEDCAGVADAAIRQrvAEEI 2700
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3981 IRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGE------TLPPLRIQYKDYAVWQTGEA 4054
Cdd:PRK12316 2701 QRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGArrgeqpTLPPLPLQYADYAAWQRAWM 2780
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4055 RLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKY 4134
Cdd:PRK12316 2781 DSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRY 2860
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4135 SGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIARDLSR 4214
Cdd:PRK12316 2861 SGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSH 2940
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4215 NPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSI 4294
Cdd:PRK12316 2941 SPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGM 3020
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4295 IKQPEAELARLNMMTKEEERDIQQLFNDTAvAEKRIPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVL 4374
Cdd:PRK12316 3021 VENPQRSVDELAMLDAEERGQLLEAWNATA-AEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRL 3099
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4375 QDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTcAGHAIPPLFEGEVLLLDD 4454
Cdd:PRK12316 3100 IERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-QSHLRLPLAQGVQVLDLD 3178
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4455 PLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSA 4533
Cdd:PRK12316 3179 RGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVgDRVLQFTTFSFDVFVEELFWP 3258
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4534 LSSGGILFIIGNEAKRDIRQLNDFVRTHGIQ-TAFLPTAFLKLLASEKhyfEPFAECVDHIIAAGEQLIATRMLRDMLar 4612
Cdd:PRK12316 3259 LMSGARVVLAGPEDWRDPALLVELINSEGVDvLHAYPSMLQAFLEEED---AHRCTSLKRIVCGGEALPADLQQQVFA-- 3333
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4613 hQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLE 4692
Cdd:PRK12316 3334 -GLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAE 3412
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4693 TFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTdgQSDLYAY 4770
Cdd:PRK12316 3413 RFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHpwVREAVVLAVDGR--QLVAYVV 3490
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4771 FTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQTgTDYVAPRTNMEEQLICIWQDVL 4850
Cdd:PRK12316 3491 PEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQ-QDYVAPVNELERRLAAIWADVL 3569
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4851 KVKEIGVKDNFFDLGGHSLRGMTLIAKIhKQFSKNISLREVFQCPTVGEMAQAiaeAETNGpdyipkAKAKDVYPVSSVQ 4930
Cdd:PRK12316 3570 KLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLARV---ARVGG------GVAVDQGPVSGET 3639
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4931 KMVYLTTQIIGGELP----YNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVemVREEAV-QVIKSQVEFSME-RYE 5004
Cdd:PRK12316 3640 LLLPIQQQFFEEPVPerhhWNQSLLLKPREALDAAALEAALQALVEHHDALRLRF--VEDAGGwTAEHLPVELGGAlLWR 3717
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5005 ATADEVEECFR---AFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLY------DGKELAP 5075
Cdd:PRK12316 3718 AELDDAEELERlgeEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllqgEAPRLPA 3797
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5076 LRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFhEELPSfELPKDFARPPVRSFDGKRHNFTLDKTVT-QGIKQLEELTGS 5154
Cdd:PRK12316 3798 KTSSFKAWAERLQEHARGEALKAELAYWQEQL-QGVSS-ELPCDHPQGALQNRHAASVQTRLDRELTrRLLQQAPAAYRT 3875
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5155 TAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPH----ADLEPIIGMFVNTLAIRTAPMAEktFLDYITETKEtMLKAFE 5230
Cdd:PRK12316 3876 QVNDLLLTALARVVCRWTGEASALVQLEGHGREDlfadIDLSRTVGWFTSLFPVRLSPVED--LGASIKAIKE-QLRAIP 3952
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5231 HQEYPFeELVEKLG---VKRDLSRNPLFDTMF--VLQNTEQTDIE----VDSLAVRPYEQTETAAKFD-LQLNFLIDQDE 5300
Cdd:PRK12316 3953 NKGIGF-GLLRYLGdeeSRRTLAGLPVPRITFnyLGQFDGSFDEEmalfVPAGESAGAEQSPDAPLDNwLSLNGRVYGGE 4031
                        4090      4100      4110
                  ....*....|....*....|....*....|..
gi 166797876 5301 IQGSFDYCTKLFKKKTIAVLAKDYVMILSAIM 5332
Cdd:PRK12316 4032 LSLDWTFSREMFEEATIQRLADDYAAELTALV 4063
PRK12467 PRK12467
peptide synthase; Provisional
7-2343 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1819.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    7 QETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDR 86
Cdd:PRK12467 1304 QLAYWKAQLGGEQPVLELP----TDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQ 1379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   87 TSLILGIPTVSKQKAGQSA-----VNNIVLlKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMP 161
Cdd:PRK12467 1380 DDIRVGVPIANRNRAETEGligffVNTQVL-RAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSP 1458
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  162 LIHtvVSLN---------------EIHSLQCKEDTAtdtlfHFDLENN------GIHLKLFYNGNLYDERYINQIVSHLD 220
Cdd:PRK12467 1459 LFQ--VMFNhqrddhqaqaqlpglSVESLSWESQTA-----QFDLTLDtyesseGLQASLTYATDLFEASTIERLAGHWL 1531
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  221 QLLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASR 300
Cdd:PRK12467 1532 NLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANR 1611
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  301 LARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSLAF-DG- 378
Cdd:PRK12467 1612 LAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLpDGl 1691
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  379 PVIDLNDEASYHADCSLLSP--VAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFD 456
Cdd:PRK12467 1692 RSLVLDQEDDWLEGYSDSNPavNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFD 1771
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  457 AFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNR-EDFIHVQHVVVGGEQLETDTV 535
Cdd:PRK12467 1772 VSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQvEHPLSLRRVVCGGEALEVEAL 1851
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  536 EKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ----ITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARG 611
Cdd:PRK12467 1852 RPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEgrdsVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARG 1931
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  612 YLNRPELTEEKFV-EHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVARE 690
Cdd:PRK12467 1932 YLNRPALTAERFVaDPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  691 DAdGAKQLYAYYV----------GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADEnTRAEN 760
Cdd:PRK12467 2012 GA-NGKQLVAYVVptdpglvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDA-SELQQ 2089
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  761 EYIAPRNTIEELLASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQfVAPVSR- 839
Cdd:PRK12467 2090 AYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAA-VAQEGDg 2168
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  840 --VADQGEVNGGTKLTPIQHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGY--APR 915
Cdd:PRK12467 2169 tvSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWsaMHR 2248
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  916 ITGTDESELFHLEVMNYKGETdpaQAIADKAneiQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLED 994
Cdd:PRK12467 2249 APEQERRPLLWQVVVADKEEL---EALCEQA---QRSLDLEEGPLLRAVLATLPDGSQrLLLVIHHLVVDGVSWRILLED 2322
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  995 FASGYEQAERRQTIQLPQKTDSFPFWADQLSKYAAETDMEEEIAYW-TELSSIkPQPLPKDTISEGSLLRDSEEVTIQWT 1073
Cdd:PRK12467 2323 LQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWqAQLQGA-STELPCDHPQGGLQRRHAASVTTHLD 2401
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1074 KEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPDADISRTIGWFTSQYPVvlRMEAGKN 1153
Cdd:PRK12467 2402 SEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPV--KLSPTAS 2479
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1154 LSQRIKIVKEGLRRIPDKGMNYSIIKYIsGHPEA-DSLQL--KPEISFNYLGQFDQ--DLKHQALrISPfsTGLSMNENQ 1228
Cdd:PRK12467 2480 LATSIKTIKEQLRAVPNKGLGFGVLRYL-GSEAArQTLQAlpVPRITFNYLGQFDGsfDAEKQAL-FVP--SGEFSGAEQ 2555
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1229 ERTAVLD----LNGMIAEGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHCVSRQQTSLTPSDILLKDISIDELEQ 1304
Cdd:PRK12467 2556 SEEAPLGnwlsINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDR 2635
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1305 LleqTRELGEAENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGdLEIDSFSKSLDGLSQKYDIFRTNF-YRGWKDQ 1383
Cdd:PRK12467 2636 L---PVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlWDGELEE 2711
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1384 PLQIIFKTKKIGFQFNDLREMKESQKEamIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPL 1463
Cdd:PRK12467 2712 PLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQ 2789
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1464 ITKEIFENYFAllqqkQPEQSSITPYSQYIEWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAE-DGRYVPEKVTCDI 1542
Cdd:PRK12467 2790 LLGEVLQRYFG-----QPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPaEAVAGHGAHYLHL 2864
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1543 SSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFA 1622
Cdd:PRK12467 2865 DATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVS 2944
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1623 ELMKEAQERAVASQKFETHPLYDIQARTTQ-KQDLITHLMIFENYPVDqymESIGRQNGTSITISNVQMEEQTNYDFNLT 1701
Cdd:PRK12467 2945 DWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPIS---EALKQGAPSGLRFGAVSSREQTNYPLTLA 3021
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1702 VIPGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLF 1780
Cdd:PRK12467 3022 VGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPsERLVHQLI 3101
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1781 EEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQ 1860
Cdd:PRK12467 3102 EAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPR 3181
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1861 DRIRYMLDDSQAGIVLMQRDVRKQLAYEGV--TVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:PRK12467 3182 ERLAYMIEDSGVKLLLTQAHLLEQLPAPAGdtALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGA 3261
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 LTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKT-ALLESIVRDPRVDIIKLTPAHLQVL 2017
Cdd:PRK12467 3262 LANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDpEELWQAIHAHRISIACFPPAYLQQF 3341
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2018 KEM-NIADQTAVRRMIVGGEnlstRLARSIHEQFEGRIE---ICNEYGPTETVVGCMIYRYDA-AKDRRESVPIGTAAAN 2092
Cdd:PRK12467 3342 AEDaGGADCASLDIYVFGGE----AVPPAAFEQVKRKLKprgLTNGYGPTEAVVTVTLWKCGGdAVCEAPYAPIGRPVAG 3417
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2093 TSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFE-PGAKMYKTGDLAKWLADGNIEYAGRIDEQV 2171
Cdd:PRK12467 3418 RSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQV 3497
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2172 KIRGYRIELGEIEAALLQEEVIKEAVVTAReDVHGFKQLCAYYVSG--GQTTAARLRKQLSQTLASYMVPAYFIELDEMP 2249
Cdd:PRK12467 3498 KIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAdpQGDWRETLRDHLAASLPDYMVPAQLLVLAAMP 3576
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2250 LTSNGKINKKGLPAPDFELQDraEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQ-GYKM 2328
Cdd:PRK12467 3577 LGPNGKVDRKALPDPDAKGSR--EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKL 3654
                        2410
                  ....*....|....*
gi 166797876 2329 EIKDLFQYATIAELS 2343
Cdd:PRK12467 3655 SLRDLMSAPTIAELA 3669
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3876-5169 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1045.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3876 AAIPAIEKRPYYPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYV 3955
Cdd:COG1020     7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3956 LDHAAFEAEWY--------QGEEDDADLYIRQFIRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEF 4027
Cdd:COG1020    87 QPVVAAPLPVVvllvdleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4028 IRIY------EGETLPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLD 4101
Cdd:COG1020   167 LRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4102 KQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYL 4181
Cdd:COG1020   247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4182 SEVKENALKAYEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEG 4261
Cdd:COG1020   327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETG 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4262 AGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDIQQLFNDTAVAEKRiPTTIHQLFEQQ 4341
Cdd:COG1020   407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPA-DATLHELFEAQ 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRR 4421
Cdd:COG1020   486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4422 AFMLKDSGADVLLTCAGHAIP-PLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNL 4500
Cdd:COG1020   566 AYMLEDAGARLVLTQSALAARlPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4501 LAYEQDHTQLR-FDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASe 4579
Cdd:COG1020   646 LAWMQRRYGLGpGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD- 724
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4580 kHYFEPFAEcVDHIIAAGEQLiATRMLRDMLARH-QVTLHNHYGPSETHV-VTMYTVDP-DTDQELQPIGKPISNTEIFI 4656
Cdd:COG1020   725 -AAPEALPS-LRLVLVGGEAL-PPELVRRWRARLpGARLVNLYGPTETTVdSTYYEVTPpDADGGSVPIGRPIANTRVYV 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4657 LNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYD-SNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGY 4735
Cdd:COG1020   802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGF 881
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:COG1020   882 RIELGEIEAALLQHpgVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNG 961
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4814 NRRALPMPEAGLQTGTDYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQ 4893
Cdd:COG1020   962 KLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFL 1041
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4894 CPTVGEMAQAIAEAETNGPDYIPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQG 4973
Cdd:COG1020  1042 AAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLAL 1121
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4974 HEPLRTVVEMVREEAVQVIKSQVEF----------SMERYEATADEVEECFRAFVRPFDLSQAPLLRAGLIELEQDLHIF 5043
Cdd:COG1020  1122 LAALRARRAVRQEGPRLRLLVALAAalalaallalLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLL 1201
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5044 MFDMHHIITDGASMNIFVEKLIQLYDGKELAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARP 5123
Cdd:COG1020  1202 LLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLP 1281
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876 5124 PVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFSAYSILLA 5169
Cdd:COG1020  1282 ALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2-1104 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 825.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    2 SVFKTQETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLY 81
Cdd:COG1020   202 EELARQLAYWRQQLAGLPPLLELP----TDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLA 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   82 KYTDRTSLILGIPTvskqkAG--QSAVN-------NIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLS 152
Cdd:COG1020   278 RYSGQDDVVVGTPV-----AGrpRPELEglvgffvNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQ 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  153 VQYNDEHMPLIHTVVSLN-------EIHSLQCKEDTATDTLFHFDL------ENNGIHLKLFYNGNLYDERYINQIVSHL 219
Cdd:COG1020   353 PERDLSRNPLFQVMFVLQnapadelELPGLTLEPLELDSGTAKFDLtltvveTGDGLRLTLEYNTDLFDAATIERMAGHL 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  220 DQLLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKAS 299
Cdd:COG1020   433 VTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARAN 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  300 RLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSL-AFDG 378
Cdd:COG1020   513 RLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGV 592
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  379 PVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAF 458
Cdd:COG1020   593 PVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS 672
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  459 ILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMnREDFIHVQHVVVGGEQLETDTVEKL 538
Cdd:COG1020   673 VWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAA-PEALPSLRLVLVGGEALPPELVRRW 751
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  539 HSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ---ITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNR 615
Cdd:COG1020   752 RARLPGARLVNLYGPTETTVDSTYYEVTPPDADggsVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNR 831
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  616 PELTEEKFVEH-LHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADG 694
Cdd:COG1020   832 PELTAERFVADpFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPG 911
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  695 AKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADENTRAenEYIAPRNTIEEL 772
Cdd:COG1020   912 DKRLVAYVVPEAgaAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--AAAAPPAEEEEE 989
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  773 LASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQFVAPVSRVADQGEVNGGTKL 852
Cdd:COG1020   990 EAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAP 1069
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  853 TPIQHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGTDESELFH--LEVM 930
Cdd:COG1020  1070 LPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVAlaAALA 1149
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  931 NYKGETDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDHLLIAIHHLLIDGVSWRILLEDFASG----YEQAERRQ 1006
Cdd:COG1020  1150 LAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLllllLLLAAAAA 1229
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1007 TIQLPQKTDSFPFWADQLSKYAAETDMEEEIAYWTELSSIKPQPLPKDTISEGSLLRDSEEVTIQWTKEETEQLLKQANR 1086
Cdd:COG1020  1230 ALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLAL 1309
                        1130
                  ....*....|....*...
gi 166797876 1087 AYNTDINDLLLTSLGLAV 1104
Cdd:COG1020  1310 ALALLLLLLLLLALLLLA 1327
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1778-2265 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 776.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHG 1937
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1938 GLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKT--ALLESIVRDPRVDIIKLTPAHLQ 2015
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLdgQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 VLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCMIYRYDAAKDRRESVPIGTAAANTSI 2095
Cdd:cd17655   241 LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2096 YVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRG 2175
Cdd:cd17655   321 YILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2176 YRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGK 2255
Cdd:cd17655   401 YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGK 480
                         490
                  ....*....|
gi 166797876 2256 INKKGLPAPD 2265
Cdd:cd17655   481 VDRKALPEPD 490
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
267-753 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 661.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  267 QLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPE 346
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  347 YPKERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHG 426
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  427 GIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLK 506
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  507 tMIEQMNREDFIHVQHVVVGGEQLETDTVEKL-HSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ---ITIGSPVANHQ 582
Cdd:cd17655   241 -LLDAADDSEGLSLKHLIVGGEALSTELAKKIiELFGTNPTITNAYGPTETTVDASIYQYEPETDQqvsVPIGKPLGNTR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  583 AYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIR 662
Cdd:cd17655   320 IYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  663 GYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNG 742
Cdd:cd17655   400 GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNG 479
                         490
                  ....*....|.
gi 166797876  743 KIDLKALPAAD 753
Cdd:cd17655   480 KVDRKALPEPD 490
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1801-2198 1.74e-170

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 532.23  E-value: 1.74e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1801 TYGELNKRANRLARTLRA-KGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQR 1879
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1880 DVRKQLAYEGVTVLLDD--ESSYHQDGSDLAPISDVS---HLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGE 1954
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDplELAALDDAPAPPPPDAPSgpdDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1955 KANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIVRDPRVDIIKLTPAHLQVLKEMNIADQTAVRRM 2031
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeerDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2032 IVGGENLSTRLARSIHEQFeGRIEICNEYGPTETVVGCMIYRYDAAKDRRES-VPIGTAAANTSIYVLDENMKPAPIGVP 2110
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARG-PGARLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVLDDDLRPVPVGVV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2111 GEIYISGAGVARGYLNRPELTAEKFVDDPF--EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALL 2188
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
                          410
                   ....*....|
gi 166797876  2189 QEEVIKEAVV 2198
Cdd:TIGR01733  400 RHPGVREAVV 409
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
290-686 1.10e-159

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 501.41  E-value: 1.10e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   290 TYRELNEKASRLARTLR-NCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   369 HLKNSLAFDGPVIDLND--EASYHADCSLLSPV---AGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSP 443
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDplELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   444 ADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQER-ITHFSTSPRLLKTMIEQMnREDFIHVQH 522
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAAL-PPALASLRL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   523 VVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ----ITIGSPVANHQAYILGAHHQIQPIGIP 598
Cdd:TIGR01733  240 VILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPrespVPIGRPLANTRLYVLDDDLRPVPVGVV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   599 GELYVGGAGVARGYLNRPELTEEKFVEHLHVP--GQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMF 676
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
                          410
                   ....*....|
gi 166797876   677 NLENVREAAV 686
Cdd:TIGR01733  400 RHPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
3887-4316 1.72e-134

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 430.99  E-value: 1.72e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKM-ADGEPVQYVLDHAAFEAEW 3965
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3966 YQG---EEDDADLYIRQFIR-----PFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYE----G 4033
Cdd:pfam00668   85 IDIsdlSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqllkG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4034 ETLPPLRIQ-YKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLA 4112
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4113 SQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAY 4192
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4193 EHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNT-----EQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFT 4267
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgqdsQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTIK 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 166797876  4268 LEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDI 4316
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
AMP-binding pfam00501
AMP-binding enzyme;
269-662 4.24e-112

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 365.10  E-value: 4.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   269 FEEQAERTPENAAV-KFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEY 347
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   348 PKERLQYLLHDADADVLLVQHHLKNS-----------------LAFDGPV--IDLNDEASYHADCSLLSPVAGHSHLAYV 408
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgklevvklvlvLDRDPVLkeEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   409 IYTSGTTGKPKGVMVEHGGIVNSLQWKKAF----FKHSPADRVLVLYPYVFDA-FILNFFGPLISGATLHLLPNEENKET 483
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   484 FAIQNAIKQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRiRINNEYGPTENSVVST 561
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAgaPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   562 FHPVQSADEQI--TIGSPVANHQAYILGAHH-QIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTG 638
Cdd:pfam00501  320 TPLPLDEDLRSlgSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
                          410       420
                   ....*....|....*....|....
gi 166797876   639 DLARWLPDGRIEYLGRIDHQVKIR 662
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2278-2350 2.20e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 48.79  E-value: 2.20e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876   2278 RTKAEEILVSAWESVLGAENVSILD---NFFDLGGDSIKSIQVSSRLNQQ-GYKMEIKDLFQYATIAELSPHIKQNL 2350
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAAEL 86
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
746-835 6.45e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 47.24  E-value: 6.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    746 LKALPAADentraeneyiaPRNTIEELLASIWQEVLGAERIGILD---NFFDFGGDSIKSIQVSSRLYQA-GYKVDMKHL 821
Cdd:smart00823    1 LAALPPAE-----------RRRLLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAAtGLRLPATLV 69
                            90
                    ....*....|....
gi 166797876    822 FKHPSIAELSQFVA 835
Cdd:smart00823   70 FDHPTPAALAEHLA 83
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
1314-5332 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2707.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1314 EAENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKK 1393
Cdd:PRK12316   45 SSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRG-ADDSLAQVPLDRP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1394 IGFQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYF 1473
Cdd:PRK12316  124 LEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1474 ALLQQKQPEQSSI-TPYSQYIEWLGR-QDAKEAA---AYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTS 1548
Cdd:PRK12316  204 AYATGAEPGLPALpIQYADYALWQRSwLEAGEQErqlEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1549 KMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGipNVETMIGLFINTIPVRFRCEAGTTFAELMKEA 1628
Cdd:PRK12316  284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA--EVEGLIGFFVNTQVLRSVFDGRTRVATLLAGV 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1629 QERAVASQKFETHPlYDIQARTTQKQDLITHLMIFE----NYPVDQYMESIGRQNGTSITISNVQmEEQTNYDFNL-TVI 1703
Cdd:PRK12316  362 KDTVLGAQAHQDLP-FERLVEALKVERSLSHSPLFQvmynHQPLVADIEALDTVAGLEFGQLEWK-SRTTQFDLTLdTYE 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1704 PGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLFEE 1782
Cdd:PRK12316  440 KGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPlQRGVHRLFEE 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1783 QSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDR 1862
Cdd:PRK12316  520 QVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAER 599
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 IRYMLDDSQAGIVLMQRDVRKQLAY-EGVTVL-LDDESSYHQDGSDLAPISDVS--HLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:PRK12316  600 LAYMLEDSGVQLLLSQSHLGRKLPLaAGVQVLdLDRPAAWLEGYSEENPGTELNpeNLAYVIYTSGSTGKPKGAGNRHRA 679
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 LTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVY---DGEDKTALLESIVRDpRVDIIKLTPAHLQ 2015
Cdd:PRK12316  680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINRE-GVDTLHFVPSMLQ 758
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 -VLKEMNIADQTAVRRMIVGGENLSTrlarSIHEQFEGRI---EICNEYGPTETVVG-CMIYRYDAAKDrreSVPIGTAA 2090
Cdd:PRK12316  759 aFLQDEDVASCTSLRRIVCSGEALPA----DAQEQVFAKLpqaGLYNLYGPTEAAIDvTHWTCVEEGGD---SVPIGRPI 831
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2091 ANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQ 2170
Cdd:PRK12316  832 ANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 911
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2171 VKIRGYRIELGEIEAALLQEEVIKEAVVTAREDvhgfKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEM 2248
Cdd:PRK12316  912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGYVVleSEGGDWREALKAHLAASLPEYMVPAQWLALERL 987
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2249 PLTSNGKINKKGLPAPDFELQdRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQGYKM 2328
Cdd:PRK12316  988 PLTPNGKLDRKALPAPEASVA-QQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQL 1066
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2329 EIKDLFQYATIAELSPHIKQNLRIA-DQGEVKGKVSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLA 2407
Cdd:PRK12316 1067 SPRDLFQHQTIRSLALVAKAGQATAaDQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLV 1146
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2408 EHHDALRMTFRTTENGC-EAQNEEIAQSGLYRLEVMNLKEdpdpgrtIEAKADEIQSSMHLSDGPLMKAGLFQCADGDH- 2485
Cdd:PRK12316 1147 AHHDALRLRFREEDGGWqQAYAAPQAGEVLWQRQAASEEE-------LLALCEEAQRSLDLEQGPLLRALLVDMADGSQr 1219
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2486 LLIAIHHLIIDGISWRILLEDIVSGYKQAengrVIQLPQKTDSFQLWAKRLSEYAQSETikQEQEYWTKIEQTEVKPLPK 2565
Cdd:PRK12316 1220 LLLVIHHLVVDGVSWRILLEDLQRAYADL----DADLPARTSSYQAWARRLHEHAGARA--EELDYWQAQLEDAPHELPC 1293
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2566 DFHETHTTAKDSETAAVEWTKEETELLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDISR 2645
Cdd:PRK12316 1294 ENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSR 1373
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2646 TVGWFTSLYPVVLHaqPGKEISDYIKTTKEGLRQIPHKGIGYGIARYLSGG-----MPSKLNPEISFNYLGQFDQDLQRH 2720
Cdd:PRK12316 1374 TVGWFTSLFPVRLT--PAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEeaaarLAALPQPRITFNYLGQFDRQFDEA 1451
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2721 GVqLSSYSCGSDSSGHQERPYV--LNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHCVHKEQSELTP 2798
Cdd:PRK12316 1452 AL-FVPATESAGAAQDPCAPLAnwLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTP 1530
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2799 SDILLKGISIDELDQLLIQlphAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGeLKIDWFKASLERLFETY 2878
Cdd:PRK12316 1531 SDFPLAGLSQAQLDALPLP---AGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRH 1606
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2879 AVLRTRFY--SGWnDTPLQIVYKTQtpQIHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHL 2956
Cdd:PRK12316 1607 EILRSGFLwqDGL-EQPLQVIHKQV--ELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHL 1683
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2957 IWSFHHIVMDGWCLSLITKEVFDHYSalqeGREPePLSAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKgETTLLHKIAQ 3036
Cdd:PRK12316 1684 IYTNHHILMDGWSNAQLLGEVLQRYA----GQPV-AAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALE-EPTRLAQAAR 1757
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3037 HEQKEYAYANLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFIN 3116
Cdd:PRK12316 1758 TEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFIN 1837
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3117 TIPVRIRCDEDSTFADTMQMVQQNALASQSYDTYPLYEIQAQTEQK-QNLIDHIMIFENYPIGQQAEETGHHGteLNITN 3195
Cdd:PRK12316 1838 TLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGgEALFDSLLVFENYPVAEALKQGAPAG--LVFGR 1915
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3196 FHMQEHSHYDLNVVVIPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSN 3275
Cdd:PRK12316 1916 VSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRT 1995
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3276 DMHYPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLK 3355
Cdd:PRK12316 1996 PEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLK 2075
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3356 AGGAYLPIDPDSPSERIRYILNDSSISVLLYCGKLQDDIGFSG--TCIDL---MEEHFYHEKDSSLALSYQSsqLAYAIY 3430
Cdd:PRK12316 2076 AGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAgvARLPLdrdAEWADYPDTAPAVQLAGEN--LAYVIY 2153
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3431 TSGTTGKPKGTLIEHRQVI-HLIEGLSRQVYSAYDAELNiamLAPYYFDASVQQMYASLLSGHTLFIVPKEIvSDGAALC 3509
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVaHCQAAGERYELSPADCELQ---FMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLY 2229
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3510 RYYRQHSIDITDGTPAHLKLLIAAGDLQGVT--LQHLLIGGEALSKTTVNKLKQLFGehgaAPGITNVYGPTETCVDASL 3587
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQLAEHAERDGRPpaVRVYCFGGEAVPAASLRLAWEALR----PVYLFNGYGPTEAVVTPLL 2305
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3588 FNIeCSSDAWARSqnYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRM 3666
Cdd:PRK12316 2306 WKC-RPQDPCGAA--YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERL 2382
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3667 YRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYyLCGYFAAD--KTIQISE 3744
Cdd:PRK12316 2383 YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQ-LVAYVVPDdaAEDLLAE 2461
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3745 LRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKKRDSGiEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHF 3824
Cdd:PRK12316 2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ-AYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHF 2540
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3825 FEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLARTITKTELTGYAAIPAIEKRPYYPVSSAQKRLYILNHLEG 3904
Cdd:PRK12316 2541 FELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEP 2620
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3905 GELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEA--EWYQGEEDDADLY--IRQF 3980
Cdd:PRK12316 2621 ESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIvlEDCAGVADAAIRQrvAEEI 2700
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3981 IRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGE------TLPPLRIQYKDYAVWQTGEA 4054
Cdd:PRK12316 2701 QRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGArrgeqpTLPPLPLQYADYAAWQRAWM 2780
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4055 RLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKY 4134
Cdd:PRK12316 2781 DSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRY 2860
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4135 SGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIARDLSR 4214
Cdd:PRK12316 2861 SGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSH 2940
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4215 NPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSI 4294
Cdd:PRK12316 2941 SPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGM 3020
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4295 IKQPEAELARLNMMTKEEERDIQQLFNDTAvAEKRIPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVL 4374
Cdd:PRK12316 3021 VENPQRSVDELAMLDAEERGQLLEAWNATA-AEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRL 3099
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4375 QDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTcAGHAIPPLFEGEVLLLDD 4454
Cdd:PRK12316 3100 IERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-QSHLRLPLAQGVQVLDLD 3178
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4455 PLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSA 4533
Cdd:PRK12316 3179 RGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVgDRVLQFTTFSFDVFVEELFWP 3258
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4534 LSSGGILFIIGNEAKRDIRQLNDFVRTHGIQ-TAFLPTAFLKLLASEKhyfEPFAECVDHIIAAGEQLIATRMLRDMLar 4612
Cdd:PRK12316 3259 LMSGARVVLAGPEDWRDPALLVELINSEGVDvLHAYPSMLQAFLEEED---AHRCTSLKRIVCGGEALPADLQQQVFA-- 3333
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4613 hQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLE 4692
Cdd:PRK12316 3334 -GLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAE 3412
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4693 TFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTdgQSDLYAY 4770
Cdd:PRK12316 3413 RFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHpwVREAVVLAVDGR--QLVAYVV 3490
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4771 FTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQTgTDYVAPRTNMEEQLICIWQDVL 4850
Cdd:PRK12316 3491 PEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQ-QDYVAPVNELERRLAAIWADVL 3569
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4851 KVKEIGVKDNFFDLGGHSLRGMTLIAKIhKQFSKNISLREVFQCPTVGEMAQAiaeAETNGpdyipkAKAKDVYPVSSVQ 4930
Cdd:PRK12316 3570 KLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLARV---ARVGG------GVAVDQGPVSGET 3639
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4931 KMVYLTTQIIGGELP----YNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVemVREEAV-QVIKSQVEFSME-RYE 5004
Cdd:PRK12316 3640 LLLPIQQQFFEEPVPerhhWNQSLLLKPREALDAAALEAALQALVEHHDALRLRF--VEDAGGwTAEHLPVELGGAlLWR 3717
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5005 ATADEVEECFR---AFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLY------DGKELAP 5075
Cdd:PRK12316 3718 AELDDAEELERlgeEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllqgEAPRLPA 3797
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5076 LRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFhEELPSfELPKDFARPPVRSFDGKRHNFTLDKTVT-QGIKQLEELTGS 5154
Cdd:PRK12316 3798 KTSSFKAWAERLQEHARGEALKAELAYWQEQL-QGVSS-ELPCDHPQGALQNRHAASVQTRLDRELTrRLLQQAPAAYRT 3875
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5155 TAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPH----ADLEPIIGMFVNTLAIRTAPMAEktFLDYITETKEtMLKAFE 5230
Cdd:PRK12316 3876 QVNDLLLTALARVVCRWTGEASALVQLEGHGREDlfadIDLSRTVGWFTSLFPVRLSPVED--LGASIKAIKE-QLRAIP 3952
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5231 HQEYPFeELVEKLG---VKRDLSRNPLFDTMF--VLQNTEQTDIE----VDSLAVRPYEQTETAAKFD-LQLNFLIDQDE 5300
Cdd:PRK12316 3953 NKGIGF-GLLRYLGdeeSRRTLAGLPVPRITFnyLGQFDGSFDEEmalfVPAGESAGAEQSPDAPLDNwLSLNGRVYGGE 4031
                        4090      4100      4110
                  ....*....|....*....|....*....|..
gi 166797876 5301 IQGSFDYCTKLFKKKTIAVLAKDYVMILSAIM 5332
Cdd:PRK12316 4032 LSLDWTFSREMFEEATIQRLADDYAAELTALV 4063
PRK12467 PRK12467
peptide synthase; Provisional
1320-4050 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1971.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFyRGWKDQPLQIIFKTKKIGF--Q 1397
Cdd:PRK12467 1118 PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTF-VQEDGRTRQVIHPVGSLTLeeP 1196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1398 FNDLREMKESQKEAMIQKYARedkmRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQ 1477
Cdd:PRK12467 1197 LLLAADKDEAQLKVYVEAEAR----QPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQ 1272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPEQSSI-TPYSQYIEWlGRQ--DAKEAA---AYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMK 1551
Cdd:PRK12467 1273 GQSLQLPALpIQYADYAVW-QRQwmDAGERArqlAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLR 1351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1552 RTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGipNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQER 1631
Cdd:PRK12467 1352 ALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA--ETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQA 1429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1632 AVASQKFETHPlYDIQARTTQKQDLITHLMIFENYPVDQYMESIGRQNGTSITISNVQMEEQT-NYDFNLTVIPGDE-MN 1709
Cdd:PRK12467 1430 ALEAQAHQDLP-FEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGLSVESLSWESQTaQFDLTLDTYESSEgLQ 1508
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1710 ISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLFEEQSQRTP 1788
Cdd:PRK12467 1509 ASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPlARLVHQLIEDQAAATP 1588
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1789 DQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLD 1868
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIE 1668
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1869 DSQAGIVLMQRDVRKQLAY-EGV-TVLLDDESSYHQDGSDLAPIS--DVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIW 1944
Cdd:PRK12467 1669 DSGIELLLTQSHLQARLPLpDGLrSLVLDQEDDWLEGYSDSNPAVnlAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLC 1748
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1945 WAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIVRDpRVDIIKLTPAHLQVLKEMN 2021
Cdd:PRK12467 1749 ATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGahrDPEQLIQLIERQ-QVTTLHFVPSMLQQLLQMD 1827
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2022 --IADQTAVRRMIVGGENLSTRLARSIHEQFeGRIEICNEYGPTETVVGCMIYRYDAAKDR-RESVPIGTAAANTSIYVL 2098
Cdd:PRK12467 1828 eqVEHPLSLRRVVCGGEALEVEALRPWLERL-PDTGLFNLYGPTETAVDVTHWTCRRKDLEgRDSVPIGQPIANLSTYIL 1906
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2099 DENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYR 2177
Cdd:PRK12467 1907 DASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFR 1986
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2178 IELGEIEAALLQEEVIKEAVVTAREDVHGfKQLCAYYVSGG----------QTTAARLRKQLSQTLASYMVPAYFIELDE 2247
Cdd:PRK12467 1987 IELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDpglvdddeaqVALRAILKNHLKASLPEYMVPAHLVFLAR 2065
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2248 MPLTSNGKINKKGLPAPDFELQDRAeYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQGYK 2327
Cdd:PRK12467 2066 MPLTPNGKLDRKALPAPDASELQQA-YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIR 2144
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2328 MEIKDLFQYATIAELS--PHIKQNLRIADQGEVKGKVSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQK 2405
Cdd:PRK12467 2145 FTPKDLFQHQTVQSLAavAQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQA 2224
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2406 LAEHHDALRMTFRTTENGCEAQN---EEIAQSGLYRLEVMNLKEdpdpgrtIEAKADEIQSSMHLSDGPLMKAGLFQCAD 2482
Cdd:PRK12467 2225 LLVHHDALRLGFVQEDGGWSAMHrapEQERRPLLWQVVVADKEE-------LEALCEQAQRSLDLEEGPLLRAVLATLPD 2297
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2483 GDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTKIEQTEVK 2561
Cdd:PRK12467 2298 GSQrLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGAST 2377
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2562 PLPKDFHETHTTAKDSETAAVEWTKEETELLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDI 2641
Cdd:PRK12467 2378 ELPCDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEI 2457
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2642 DISRTVGWFTSLYPVVLhaQPGKEISDYIKTTKEGLRQIPHKGIGYGIARYLSG--------GMPSklnPEISFNYLGQF 2713
Cdd:PRK12467 2458 DLTRTVGWFTSLYPVKL--SPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSeaarqtlqALPV---PRITFNYLGQF 2532
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2714 DQDLQRHGVQLSSYSCGSDSSGHQERPYV---LNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHCVH 2790
Cdd:PRK12467 2533 DGSFDAEKQALFVPSGEFSGAEQSEEAPLgnwLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCS 2612
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2791 KEQSELTPSDILLKGISIDELDQLLIQlphAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGeLKIDWFKAS 2870
Cdd:PRK12467 2613 NDQRGVTPSDFPLAGLSQEQLDRLPVA---VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTA 2688
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2871 LERLFETYAVLRTRFYSGWN-DTPLQIVYKTQTPQIHFADLRDieEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRM 2949
Cdd:PRK12467 2689 WQAVIDRHEILRSGFLWDGElEEPLQVVYKQARLPFSRLDWRD--RADLEQALDALAAADRQQGFDLLSAPLLRLTLVRT 2766
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2950 EDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSAlqegrEPEPLSAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKGETT 3029
Cdd:PRK12467 2767 GEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG-----QPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTR 2841
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3030 LLHKI-AQHEQKEYAYANLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVE 3108
Cdd:PRK12467 2842 LARALyPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAE 2921
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3109 QMIGLFINTIPVRIRCDEDSTFADTMQMVQQNALASQSYDTYPLYEIQAQTEQ-KQNLIDHIMIFENYPIGQQAEETGHH 3187
Cdd:PRK12467 2922 QQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGAPS 3001
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3188 GteLNITNFHMQEHSHYDLNVVVIPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEY 3267
Cdd:PRK12467 3002 G--LRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQ 3079
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3268 LLSRFQSNDMHYPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMV 3347
Cdd:PRK12467 3080 VLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMI 3159
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3348 VGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYCGKLQDDIGF--SGTCIDLMEEHFYHEKDSSLALSYQSSQL 3425
Cdd:PRK12467 3160 VALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPApaGDTALTLDRLDLNGYSENNPSTRVMGENL 3239
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3426 AYAIYTSGTTGKPKGTLIEHRQVIHLIEgLSRQVY--SAYDAELniaMLAPYYFDASVQQMYASLLSGHTLFIVPKEiVS 3503
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALANHLC-WIAEAYelDANDRVL---LFMSFSFDGAQERFLWTLICGGCLVVRDND-LW 3314
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3504 DGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQ-GVTLQHLLIGGEALSkttVNKLKQLFgEHGAAPGITNVYGPTETC 3582
Cdd:PRK12467 3315 DPEELWQAIHAHRISIACFPPAYLQQFAEDAGGAdCASLDIYVFGGEAVP---PAAFEQVK-RKLKPRGLTNGYGPTEAV 3390
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3583 VDASLFniECSSDAWARSQnYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-V 3661
Cdd:PRK12467 3391 VTVTLW--KCGGDAVCEAP-YAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsG 3467
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3662 PEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEyYLCGYFAADKTIQ 3741
Cdd:PRK12467 3468 SGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGK-QLVAYVVPADPQG 3546
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3742 --ISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKKrDSGiEYVPPQTSAEIQLTAIWEDVLGLEQVG 3819
Cdd:PRK12467 3547 dwRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK-GSR-EYVAPRSEVEQQLAAIWADVLGVEQVG 3624
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3820 IRDHFFEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLArtitkteltgyaaipaiekrpyypvssaqkrlyil 3899
Cdd:PRK12467 3625 VTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA----------------------------------- 3669
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3900 NHLEGGELSYNMLglmtvegkLDRDKLQQAFRTLILRHESLRTGFkmaDGEPVQYVLDHaafeaewyqgeeddadlyirq 3979
Cdd:PRK12467 3670 GYSPLGDVPVNLL--------LDLNRLETGFPALFCRHEGLGTVF---DYEPLAVILEG--------------------- 3717
                        2730      2740      2750      2760      2770      2780      2790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 3980 firpfhldeppllrvglielqpDRGILMFDMHHIISDGtsmsvlikefiriYEGETLPPLRIQYKDYAVWQ 4050
Cdd:PRK12467 3718 ----------------------DRHVLGLTCRHLLDDG-------------WQDTSLQAMAVQYADYILWQ 3753
PRK12316 PRK12316
peptide synthase; Provisional
7-2785 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1925.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    7 QETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDR 86
Cdd:PRK12316  239 QLEYWRAQLGEEHPVLELP----TDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQ 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   87 TSLILGIPTVSKQKAGQSA-----VNNIVLlKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMP 161
Cdd:PRK12316  315 TDIRVGVPIANRNRAEVEGligffVNTQVL-RSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSP 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  162 LIHTVVSLNEIHSLQCKEDTATDTLF----------HFDL------ENNGIHLKLFYNGNLYDERYINQIVSHLDQLLSV 225
Cdd:PRK12316  394 LFQVMYNHQPLVADIEALDTVAGLEFgqlewksrttQFDLtldtyeKGGRLHAALTYATDLFEARTVERMARHWQNLLRG 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  226 ILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTL 305
Cdd:PRK12316  474 MVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHAL 553
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  306 RNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSLAFDG--PVIDL 383
Cdd:PRK12316  554 IERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAgvQVLDL 633
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  384 NDEASYHADCSLLSPV--AGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILN 461
Cdd:PRK12316  634 DRPAAWLEGYSEENPGteLNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE 713
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  462 FFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSL 541
Cdd:PRK12316  714 FFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAK 793
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  542 QPRIRINNEYGPTENSV-VSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTE 620
Cdd:PRK12316  794 LPQAGLYNLYGPTEAAIdVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTA 873
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  621 EKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAredADGaKQLYA 700
Cdd:PRK12316  874 ERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDG-KQLVG 949
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  701 YYVgePSLTAAQFREELS----RELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADEnTRAENEYIAPRNTIEELLASI 776
Cdd:PRK12316  950 YVV--LESEGGDWREALKahlaASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEA-SVAQQGYVAPRNALERTLAAI 1026
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  777 WQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQFV-APVSRVADQGEVNGGTKLTPI 855
Cdd:PRK12316 1027 WQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPV 1106
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  856 QHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGTDESELFhlevmnYKGE 935
Cdd:PRK12316 1107 QRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVL------WQRQ 1180
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  936 TDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRqtiqLPQKT 1014
Cdd:PRK12316 1181 AASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQrLLLVIHHLVVDGVSWRILLEDLQRAYADLDAD----LPART 1256
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1015 DSFPFWADQLSKYAAEtdMEEEIAYWTELSSIKPQPLPKDTISEGSLLRDSEEVTIQWTKEETEQLLKQANRAYNTDIND 1094
Cdd:PRK12316 1257 SSYQAWARRLHEHAGA--RAEELDYWQAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVND 1334
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1095 LLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPDADISRTIGWFTSQYPVvlRMEAGKNLSQRIKIVKEGLRRIPDKGMN 1174
Cdd:PRK12316 1335 LLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFPV--RLTPAADLGESIKAIKEQLRAVPDKGIG 1412
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1175 YSIIKYISGHPEADSLQL--KPEISFNYLGQFDQDLKHQALRI-SPFSTGLSMNENQERTAVLDLNGMIAEGTLSLTLSY 1251
Cdd:PRK12316 1413 YGLLRYLAGEEAAARLAAlpQPRITFNYLGQFDRQFDEAALFVpATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSF 1492
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1252 SSKQYERSTMAQFARGLKESLQEVIAHCVSRQQTSLTPSDILLKDISIDELEQLleqTRELGEAENIYPLTPMQKGMLFH 1331
Cdd:PRK12316 1493 SREMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPLAGLSQAQLDAL---PLPAGEIADIYPLSPMQQGMLFH 1569
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1332 SLFDPNSGAYFQQTMFDLHGdLEIDSFSKSLDGLSQKYDIFRTNFYrgWKD---QPLQIIFKTKKIGFQFNDLRemKESQ 1408
Cdd:PRK12316 1570 SLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFL--WQDgleQPLQVIHKQVELPFAELDWR--GRED 1644
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1409 KEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFAllqqkQPEQSSITP 1488
Cdd:PRK12316 1645 LGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-----QPVAAPGGR 1719
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1489 YSQYIEWLGRQDAKEAAAYWDQYLEGYEEQTGLpKDHHAAEDGR--YVPEKVTCDisSDLTSKMKRTAGKHHVTLNTLLQ 1566
Cdd:PRK12316 1720 YRDYIAWLQRQDAAASEAFWKEQLAALEEPTRL-AQAARTEDGQvgYGDHQQLLD--PAQTRALAEFARAQKVTLNTLVQ 1796
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1567 TAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERAVASQKFETHPLYDI 1646
Cdd:PRK12316 1797 AAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDI 1876
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1647 QARTTQK-QDLITHLMIFENYPVDQYMESIGRQngtSITISNVQMEEQTNYDFNLTVIPGDEMNISFEYNANVYERASIE 1725
Cdd:PRK12316 1877 QRWAGQGgEALFDSLLVFENYPVAEALKQGAPA---GLVFGRVSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIE 1953
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1726 RVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFPQTP-VHQLFEEQSQRTPDQAAVIDKDRQLTYGE 1804
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPgVHQRIAEQAARAPEAIAVVFGDQHLSYAE 2033
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1805 LNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQ 1884
Cdd:PRK12316 2034 LDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLER 2113
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1885 LAY-EGVTVLLDDESSYHQDGSDLAPISDVS--HLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANFPLY 1961
Cdd:PRK12316 2114 LPLpAGVARLPLDRDAEWADYPDTAPAVQLAgeNLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQF 2193
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1962 SSISFDLTVTSIFTPLVTGNAIIVYDGEDKTA--LLESIVRDPrVDIIKLTPAHLQVLKEMNIAD--QTAVRRMIVGGEN 2037
Cdd:PRK12316 2194 MSFSFDGAHEQWFHPLLNGARVLIRDDELWDPeqLYDEMERHG-VTILDFPPVYLQQLAEHAERDgrPPAVRVYCFGGEA 2272
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2038 LSTRLARSIHEQFEGrIEICNEYGPTETVVGCMIYRYDAAK-DRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYIS 2116
Cdd:PRK12316 2273 VPAASLRLAWEALRP-VYLFNGYGPTEAVVTPLLWKCRPQDpCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLG 2351
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2117 GAGVARGYLNRPELTAEKFVDDPFE-PGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKE 2195
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE 2431
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2196 AVVTAREDVHGfKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFELQDRAe 2273
Cdd:PRK12316 2432 AVVVAQDGASG-KQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQA- 2509
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2274 YKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQ-GYKMEIKDLFQYATIAELSPHIK--QNL 2350
Cdd:PRK12316 2510 YVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLEsgQTS 2589
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2351 RIADQGEVKGK----VSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTEngcEA 2426
Cdd:PRK12316 2590 RAPVLQKVTRVqplpLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVG---EQ 2666
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2427 QNEEIAQSGLYRLEVMNLKEDPDpGRTIEAKADEIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLE 2505
Cdd:PRK12316 2667 TRQVILPNMSLRIVLEDCAGVAD-AAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHvLVITQHHIVSDGWSMQVMVD 2745
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2506 DIVSGYKQAENGRVIQLPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTKIEQTE--VKPLPKDFHETHTTAKDSETAAVE 2583
Cdd:PRK12316 2746 ELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEqpVLELPLDRPRPALQSHRGARLDVA 2825
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2584 WTKEETELLLKQANRAYHTeINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQiiqdIDISRTVGWFTSLYPVVLHAQPG 2663
Cdd:PRK12316 2826 LDVALSRELLALARREGVT-LFMLLLASFQVLLHRYSGQSDIRVGVPIANRNR----AETERLIGFFVNTQVLRAQVDAQ 2900
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2664 KEISDYIKTTKE-GLRQIPHKGIGYgiarylsGGMPSKLNPEISFNYLGQFD-----QDLQRHGVQLSSYSCGSDSSGHQ 2737
Cdd:PRK12316 2901 LAFRDLLGQVKEqALGAQAHQDLPF-------EQLVEALQPERSLSHSPLFQvmynhQSGERAAAQLPGLHIESFAWDGA 2973
                        2810      2820      2830      2840
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 2738 ERPYVLNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTII 2785
Cdd:PRK12316 2974 ATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMV 3021
PRK12316 PRK12316
peptide synthase; Provisional
1320-3864 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1883.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFyRGWKDQPLQIIFKTKKIGFQFN 1399
Cdd:PRK12316 2604 PLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRF-VEVGEQTRQVILPNMSLRIVLE 2682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1400 DLREMKESQKEAMIQKYARedkmRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQK 1479
Cdd:PRK12316 2683 DCAGVADAAIRQRVAEEIQ----RPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGE 2758
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1480 QPEQSSIT-PYSQYIEWLGR-QDAKEAAA---YWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKRTA 1554
Cdd:PRK12316 2759 QPTLPPLPlQYADYAAWQRAwMDSGEGARqldYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALA 2838
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1555 GKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRpaGIPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERAVA 1634
Cdd:PRK12316 2839 RREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALG 2916
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1635 SQKFETHPLYDIqARTTQKQDLITHLMIFENYPVDQYMESIGRQNGTSITISNVQMEEQTNYDFNL-TVIPGDEMNISFE 1713
Cdd:PRK12316 2917 AQAHQDLPFEQL-VEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALdTWESAEGLGASLT 2995
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1714 YNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLFEEQSQRTPDQAA 1792
Cdd:PRK12316 2996 YATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPlERGVHRLFEEQVERTPDAVA 3075
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1793 VIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQA 1872
Cdd:PRK12316 3076 LAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGA 3155
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1873 GIVLMQRDVRKQLAyEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVK 1952
Cdd:PRK12316 3156 QLLLSQSHLRLPLA-QGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL 3234
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1953 GEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE--DKTALLESIVRDPRVDIIKLTPAHLQ-VLKEMNIADQTAVR 2029
Cdd:PRK12316 3235 GVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEdwRDPALLVELINSEGVDVLHAYPSMLQaFLEEEDAHRCTSLK 3314
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2030 RMIVGGENLSTRLARSIHEQfegrIEICNEYGPTETVVGCMIYRydAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGV 2109
Cdd:PRK12316 3315 RIVCGGEALPADLQQQVFAG----LPLYNLYGPTEATITVTHWQ--CVEEGKDAVPIGRPIANRACYILDGSLEPVPVGA 3388
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2110 PGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQ 2189
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLE 3468
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2190 EEVIKEAVVTAREDvhgfKQLCAYYVSGGQTTAAR--LRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFE 2267
Cdd:PRK12316 3469 HPWVREAVVLAVDG----RQLVAYVVPEDEAGDLReaLKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAA 3544
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2268 LQDRAeYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQGYKMEIKDLFQYATIAELSPHIK 2347
Cdd:PRK12316 3545 LLQQD-YVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVAR 3623
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2348 QNLRIA-DQGEVKGKVSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEA 2426
Cdd:PRK12316 3624 VGGGVAvDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTA 3703
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2427 QNEEIAQSG--LYRLEVMNLKEdpdpgrtIEAKADEIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRIL 2503
Cdd:PRK12316 3704 EHLPVELGGalLWRAELDDAEE-------LERLGEEAQRSLDLADGPLLRALLATLADGSQrLLLVIHHLVVDGVSWRIL 3776
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2504 LEDIVSGYKQAENGRVIQLPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTKIEQTEVKPLPKDFHETHTTAKDSETAAVE 2583
Cdd:PRK12316 3777 LEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELPCDHPQGALQNRHAASVQTR 3856
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2584 WTKEETELLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDISRTVGWFTSLYPVVLhaQPG 2663
Cdd:PRK12316 3857 LDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRL--SPV 3934
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2664 KEISDYIKTTKEGLRQIPHKGIGYGIARYLS--------GGMPSklnPEISFNYLGQFDQDLQRHGVQLSSYSCGSDSSG 2735
Cdd:PRK12316 3935 EDLGASIKAIKEQLRAIPNKGIGFGLLRYLGdeesrrtlAGLPV---PRITFNYLGQFDGSFDEEMALFVPAGESAGAEQ 4011
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2736 HQERPY--VLNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHCVHKEQSELTPSDILLKGISIDELDQ 2813
Cdd:PRK12316 4012 SPDAPLdnWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQARLDA 4091
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2814 LliQLPhAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGeLKIDWFKASLERLFETYAVLRTRF-YSGWNDT 2892
Cdd:PRK12316 4092 L--PLP-LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGR 4167
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2893 PLQIVYKTQTPQIHFADLRDIEEhlREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSL 2972
Cdd:PRK12316 4168 PLQVVHKQVSLPFAELDWRGRAD--LQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQ 4245
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2973 ITKEVFDHYSalqeGREPEPlSAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKGETTLLHKIAQHEQKEYA-YANLICRF 3051
Cdd:PRK12316 4246 LLGEVLERYS----GRPPAQ-PGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANgYGEHVREL 4320
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3052 DHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRCDEDSTFA 3131
Cdd:PRK12316 4321 DATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVV 4400
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3132 DTMQMVQQNALASQSYDTYPLYEIQAQTEQK-QNLIDHIMIFENYPIGQQAEETGHHGteLNITNFHMQEHSHYDLNVVV 3210
Cdd:PRK12316 4401 EWLQQVQRQNLALREHEHTPLYEIQRWAGQGgEALFDSLLVFENYPVSEALQQGAPGG--LRFGEVTNHEQTNYPLTLAV 4478
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3211 IPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSNDMHYPREKTIHELFE 3290
Cdd:PRK12316 4479 GLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVA 4558
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3291 EQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSE 3370
Cdd:PRK12316 4559 ERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE 4638
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3371 RIRYILNDSSISVLLYCGKLQDDI----GFSGTCIDLMEE-HFYHEKDSSLALSYQSsqLAYAIYTSGTTGKPKGTLIEH 3445
Cdd:PRK12316 4639 RLAYMMEDSGAALLLTQSHLLQRLpipdGLASLALDRDEDwEGFPAHDPAVRLHPDN--LAYVIYTSGSTGRPKGVAVSH 4716
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3446 RQVI-HLIEGLSRQVYSAYDAELniaMLAPYYFDASVQQMYASLLSGHTLFIVPKEIvSDGAALCRYYRQHSIDITDGTP 3524
Cdd:PRK12316 4717 GSLVnHLHATGERYELTPDDRVL---QFMSFSFDGSHEGLYHPLINGASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPP 4792
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3525 AHLKLLI--AAGDLQGVTLQHLLIGGEALSkttVNKLKQLFGehGAAP-GITNVYGPTETCVDASLFNiecSSDAWARSQ 3601
Cdd:PRK12316 4793 VYLQQLAehAERDGEPPSLRVYCFGGEAVA---QASYDLAWR--ALKPvYLFNGYGPTETTVTVLLWK---ARDGDACGA 4864
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3602 NYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRMYRTGDLARLLPDGN 3680
Cdd:PRK12316 4865 AYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGV 4944
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3681 IEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEyYLCGYFA------ADKTIQISELRKR----MA 3750
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGK-QLVGYVVpqdpalADADEAQAELRDElkaaLR 5023
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3751 RHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPvkkrDSGI---EYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHFFEI 3827
Cdd:PRK12316 5024 ERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP----DASLlqqAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFEL 5099
                        2570      2580      2590
                  ....*....|....*....|....*....|....*..
gi 166797876 3828 GGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLA 3864
Cdd:PRK12316 5100 GGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFV 5136
PRK12467 PRK12467
peptide synthase; Provisional
7-2343 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1819.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    7 QETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDR 86
Cdd:PRK12467 1304 QLAYWKAQLGGEQPVLELP----TDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQ 1379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   87 TSLILGIPTVSKQKAGQSA-----VNNIVLlKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMP 161
Cdd:PRK12467 1380 DDIRVGVPIANRNRAETEGligffVNTQVL-RAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSP 1458
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  162 LIHtvVSLN---------------EIHSLQCKEDTAtdtlfHFDLENN------GIHLKLFYNGNLYDERYINQIVSHLD 220
Cdd:PRK12467 1459 LFQ--VMFNhqrddhqaqaqlpglSVESLSWESQTA-----QFDLTLDtyesseGLQASLTYATDLFEASTIERLAGHWL 1531
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  221 QLLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASR 300
Cdd:PRK12467 1532 NLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANR 1611
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  301 LARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSLAF-DG- 378
Cdd:PRK12467 1612 LAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLpDGl 1691
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  379 PVIDLNDEASYHADCSLLSP--VAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFD 456
Cdd:PRK12467 1692 RSLVLDQEDDWLEGYSDSNPavNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFD 1771
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  457 AFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNR-EDFIHVQHVVVGGEQLETDTV 535
Cdd:PRK12467 1772 VSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQvEHPLSLRRVVCGGEALEVEAL 1851
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  536 EKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ----ITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARG 611
Cdd:PRK12467 1852 RPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEgrdsVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARG 1931
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  612 YLNRPELTEEKFV-EHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVARE 690
Cdd:PRK12467 1932 YLNRPALTAERFVaDPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  691 DAdGAKQLYAYYV----------GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADEnTRAEN 760
Cdd:PRK12467 2012 GA-NGKQLVAYVVptdpglvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDA-SELQQ 2089
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  761 EYIAPRNTIEELLASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQfVAPVSR- 839
Cdd:PRK12467 2090 AYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAA-VAQEGDg 2168
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  840 --VADQGEVNGGTKLTPIQHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGY--APR 915
Cdd:PRK12467 2169 tvSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWsaMHR 2248
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  916 ITGTDESELFHLEVMNYKGETdpaQAIADKAneiQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLED 994
Cdd:PRK12467 2249 APEQERRPLLWQVVVADKEEL---EALCEQA---QRSLDLEEGPLLRAVLATLPDGSQrLLLVIHHLVVDGVSWRILLED 2322
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  995 FASGYEQAERRQTIQLPQKTDSFPFWADQLSKYAAETDMEEEIAYW-TELSSIkPQPLPKDTISEGSLLRDSEEVTIQWT 1073
Cdd:PRK12467 2323 LQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWqAQLQGA-STELPCDHPQGGLQRRHAASVTTHLD 2401
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1074 KEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPDADISRTIGWFTSQYPVvlRMEAGKN 1153
Cdd:PRK12467 2402 SEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPV--KLSPTAS 2479
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1154 LSQRIKIVKEGLRRIPDKGMNYSIIKYIsGHPEA-DSLQL--KPEISFNYLGQFDQ--DLKHQALrISPfsTGLSMNENQ 1228
Cdd:PRK12467 2480 LATSIKTIKEQLRAVPNKGLGFGVLRYL-GSEAArQTLQAlpVPRITFNYLGQFDGsfDAEKQAL-FVP--SGEFSGAEQ 2555
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1229 ERTAVLD----LNGMIAEGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHCVSRQQTSLTPSDILLKDISIDELEQ 1304
Cdd:PRK12467 2556 SEEAPLGnwlsINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDR 2635
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1305 LleqTRELGEAENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGdLEIDSFSKSLDGLSQKYDIFRTNF-YRGWKDQ 1383
Cdd:PRK12467 2636 L---PVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlWDGELEE 2711
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1384 PLQIIFKTKKIGFQFNDLREMKESQKEamIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPL 1463
Cdd:PRK12467 2712 PLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQ 2789
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1464 ITKEIFENYFAllqqkQPEQSSITPYSQYIEWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAE-DGRYVPEKVTCDI 1542
Cdd:PRK12467 2790 LLGEVLQRYFG-----QPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPaEAVAGHGAHYLHL 2864
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1543 SSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFA 1622
Cdd:PRK12467 2865 DATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVS 2944
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1623 ELMKEAQERAVASQKFETHPLYDIQARTTQ-KQDLITHLMIFENYPVDqymESIGRQNGTSITISNVQMEEQTNYDFNLT 1701
Cdd:PRK12467 2945 DWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPIS---EALKQGAPSGLRFGAVSSREQTNYPLTLA 3021
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1702 VIPGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTPVHQLF 1780
Cdd:PRK12467 3022 VGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPsERLVHQLI 3101
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1781 EEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQ 1860
Cdd:PRK12467 3102 EAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPR 3181
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1861 DRIRYMLDDSQAGIVLMQRDVRKQLAYEGV--TVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:PRK12467 3182 ERLAYMIEDSGVKLLLTQAHLLEQLPAPAGdtALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGA 3261
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 LTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKT-ALLESIVRDPRVDIIKLTPAHLQVL 2017
Cdd:PRK12467 3262 LANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDpEELWQAIHAHRISIACFPPAYLQQF 3341
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2018 KEM-NIADQTAVRRMIVGGEnlstRLARSIHEQFEGRIE---ICNEYGPTETVVGCMIYRYDA-AKDRRESVPIGTAAAN 2092
Cdd:PRK12467 3342 AEDaGGADCASLDIYVFGGE----AVPPAAFEQVKRKLKprgLTNGYGPTEAVVTVTLWKCGGdAVCEAPYAPIGRPVAG 3417
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2093 TSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFE-PGAKMYKTGDLAKWLADGNIEYAGRIDEQV 2171
Cdd:PRK12467 3418 RSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQV 3497
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2172 KIRGYRIELGEIEAALLQEEVIKEAVVTAReDVHGFKQLCAYYVSG--GQTTAARLRKQLSQTLASYMVPAYFIELDEMP 2249
Cdd:PRK12467 3498 KIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAdpQGDWRETLRDHLAASLPDYMVPAQLLVLAAMP 3576
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2250 LTSNGKINKKGLPAPDFELQDraEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQ-GYKM 2328
Cdd:PRK12467 3577 LGPNGKVDRKALPDPDAKGSR--EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKL 3654
                        2410
                  ....*....|....*
gi 166797876 2329 EIKDLFQYATIAELS 2343
Cdd:PRK12467 3655 SLRDLMSAPTIAELA 3669
PRK12316 PRK12316
peptide synthase; Provisional
7-2357 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1748.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    7 QETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDR 86
Cdd:PRK12316 2788 QLDYWRERLGGEQPVLELP----LDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQ 2863
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   87 TSLILGIPTVSKQKAGQSAV----NNIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMPL 162
Cdd:PRK12316 2864 SDIRVGVPIANRNRAETERLigffVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPL 2943
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  163 IHTVVSLN-------EIHSLQCKEDTATDTLFHFDL------ENNGIHLKLFYNGNLYDERYINQIVSHLDQLLSVILFQ 229
Cdd:PRK12316 2944 FQVMYNHQsgeraaaQLPGLHIESFAWDGAATQFDLaldtweSAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVEN 3023
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  230 PQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCG 309
Cdd:PRK12316 3024 PQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERG 3103
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  310 VQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASY 389
Cdd:PRK12316 3104 VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDEN 3183
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  390 HADCSLLSPVAGhSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISG 469
Cdd:PRK12316 3184 YAEANPAIRTMP-ENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSG 3262
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  470 ATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPrirINN 549
Cdd:PRK12316 3263 ARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYN 3339
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  550 EYGPTENSVVSTFHPVQSADE-QITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLH 628
Cdd:PRK12316 3340 LYGPTEATITVTHWQCVEEGKdAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF 3419
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  629 VPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAredaDGAKQLYAYYVGEPSL 708
Cdd:PRK12316 3420 VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEA 3495
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  709 TAAQ--FREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADEnTRAENEYIAPRNTIEELLASIWQEVLGAERI 786
Cdd:PRK12316 3496 GDLReaLKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDA-ALLQQDYVAPVNELERRLAAIWADVLKLEQV 3574
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  787 GILDNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELsqfvAPVSRVA-----DQGEVNGGTKLTPIQHWFFE 861
Cdd:PRK12316 3575 GLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGL----ARVARVGggvavDQGPVSGETLLLPIQQQFFE 3650
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  862 QKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGTDESELFHLEvmnykGETDPAQA 941
Cdd:PRK12316 3651 EPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWR-----AELDDAEE 3725
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  942 IADKANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQLPQKTDSFPFW 1020
Cdd:PRK12316 3726 LERLGEEAQRSLDLADGPLLRALLATLADGSQrLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAW 3805
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1021 ADQLSKYAAETDMEEEIAYWTELSSIKPQPLPKDTISEGSLLRDSEEVTIQWTKEETEQLLKQANRAYNTDINDLLLTSL 1100
Cdd:PRK12316 3806 AERLQEHARGEALKAELAYWQEQLQGVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTAL 3885
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1101 GLAVHKWTGTEDIVVNLEGHGREPIIPDADISRTIGWFTSQYPVvlRMEAGKNLSQRIKIVKEGLRRIPDKGMNYSIIKY 1180
Cdd:PRK12316 3886 ARVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPV--RLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRY 3963
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1181 ISGHPEADSLQLKP--EISFNYLGQFDQDLKHQALRISPfsTGLSMNENQERTAVLD----LNGMIAEGTLSLTLSYSSK 1254
Cdd:PRK12316 3964 LGDEESRRTLAGLPvpRITFNYLGQFDGSFDEEMALFVP--AGESAGAEQSPDAPLDnwlsLNGRVYGGELSLDWTFSRE 4041
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1255 QYERSTMAQFARGLKESLQEVIAHCVSRQQTSLTPSDILLKDISIDELEQLleqTRELGEAENIYPLTPMQKGMLFHSLF 1334
Cdd:PRK12316 4042 MFEEATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQARLDAL---PLPLGEIEDIYPLSPMQQGMLFHSLY 4118
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1335 DPNSGAYFQQTMFDLHGdLEIDSFSKSLDGLSQKYDIFRTNF-YRGWKDQPLQIIFKTKKIGFQFNDLRemKESQKEAMI 1413
Cdd:PRK12316 4119 EQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGRPLQVVHKQVSLPFAELDWR--GRADLQAAL 4195
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1414 QKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYfallQQKQPEQSSITpYSQYI 1493
Cdd:PRK12316 4196 DALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY----SGRPPAQPGGR-YRDYI 4270
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1494 EWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAE--DGRYVPEKVTcDISSDLTSKMKRTAGKHHVTLNTLLQTAWAV 1571
Cdd:PRK12316 4271 AWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADlrSANGYGEHVR-ELDATATARLREFARTQRVTLNTLVQAAWLL 4349
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1572 LLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERAVASQKFETHPLYDIQARTT 1651
Cdd:PRK12316 4350 LLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAG 4429
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1652 QKQD-LITHLMIFENYPVDQYMEsigRQNGTSITISNVQMEEQTNYDFNLTVIPGDEMNISFEYNANVYERASIERVREH 1730
Cdd:PRK12316 4430 QGGEaLFDSLLVFENYPVSEALQ---QGAPGGLRFGEVTNHEQTNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARH 4506
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1731 FMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFPQTP-VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRA 1809
Cdd:PRK12316 4507 LTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRcVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRA 4586
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1810 NRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQL-AYE 1888
Cdd:PRK12316 4587 NRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpIPD 4666
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1889 GVTVLLDDESSYHQDGSDLAPIS--DVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISF 1966
Cdd:PRK12316 4667 GLASLALDRDEDWEGFPAHDPAVrlHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSF 4746
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1967 DLTVTSIFTPLVTGNAIIVYDGE--DKTALLESIVRDpRVDIIKLTPAHLQVLKE--MNIADQTAVRRMIVGGENLSTRL 2042
Cdd:PRK12316 4747 DGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEH-RVTVLVFPPVYLQQLAEhaERDGEPPSLRVYCFGGEAVAQAS 4825
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2043 ARSIHEQFEgRIEICNEYGPTETVVGCMIYR-YDAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVA 2121
Cdd:PRK12316 4826 YDLAWRALK-PVYLFNGYGPTETTVTVLLWKaRDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVA 4904
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2122 RGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTA 2200
Cdd:PRK12316 4905 RGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA 4984
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2201 REDVHGfKQLCAYYVSggQTTA------------ARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFEL 2268
Cdd:PRK12316 4985 QEGAVG-KQLVGYVVP--QDPAladadeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASL 5061
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2269 QDRAeYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQ-GYKMEIKDLFQYATIAELSphik 2347
Cdd:PRK12316 5062 LQQA-YVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLAAFV---- 5136
                        2410
                  ....*....|
gi 166797876 2348 QNLRIADQGE 2357
Cdd:PRK12316 5137 ELAAAAGSGD 5146
PRK05691 PRK05691
peptide synthase; Validated
1320-3867 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1679.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFyRGWKDQPLQIIFKTKKIGFQFN 1399
Cdd:PRK05691 1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTF-PSVDGVPVQQVAEDSGLRMDWQ 1808
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1400 DLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQK 1479
Cdd:PRK05691 1809 DFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDR 1888
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1480 qpeQSSITPYS-QYI-------EWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDH-------HAAEDGRYvpekvtcDISS 1544
Cdd:PRK05691 1889 ---ESPLEPLPvQYLdysvwqrQWLESGERQRQLDYWKAQLGNEHPLLELPADRprppvqsHRGELYRF-------DLSP 1958
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1545 DLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAEL 1624
Cdd:PRK05691 1959 ELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIR--PESEGLIGAFLNTQVLRCQLDGQMSVSEL 2036
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1625 MKEAQERAVASQKFETHPlYDIQARTTQKQDLITHlmifenYPVDQYMESIGR-QNGTSITISNVQME------EQTNYD 1697
Cdd:PRK05691 2037 LEQVRQTVIEGQSHQDLP-FDHLVEALQPPRSAAY------NPLFQVMCNVQRwEFQQSRQLAGMTVEylvndaRATKFD 2109
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1698 FNLTVIPGDE-MNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP-QTP 1775
Cdd:PRK05691 2110 LNLEVTDLDGrLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARlDQT 2189
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPID 1855
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1856 PEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAY--EGVT--VLLDDESSY-HQDGSDLAPISDVSHLAYVIYTSGSTGRPK 1930
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEALGElpAGVArwCLEDDAAALaAYSDAPLPFLSLPQHQAYLIYTSGSTGKPK 2349
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1931 GVLIEHGGLTNYIWWAKEVY-VKGEKANFPLYsSISFDLTVTSIFTPLVTGNAIIV-----YDGEDKTALlesiVRDPRV 2004
Cdd:PRK05691 2350 GVVVSHGEIAMHCQAVIERFgMRADDCELHFY-SINFDAASERLLVPLLCGARVVLraqgqWGAEEICQL----IREQQV 2424
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2005 DIIKLTPAHLQVLKEMNIA--DQTAVRRMIVGGENLSTRLARSIHEQFEGRIeICNEYGPTETVV---GCMIyrYDAAKD 2079
Cdd:PRK05691 2425 SILGFTPSYGSQLAQWLAGqgEQLPVRMCITGGEALTGEHLQRIRQAFAPQL-FFNAYGPTETVVmplACLA--PEQLEE 2501
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2080 RRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEP-GAKMYKTGDLAKWLAD 2158
Cdd:PRK05691 2502 GAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRAD 2581
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2159 GNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAReDVHGFKQLCAYYVS--GGQTTAAR------LRKQLS 2230
Cdd:PRK05691 2582 GLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSavAGQDDEAQaalreaLKAHLK 2660
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2231 QTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFElQDRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGD 2310
Cdd:PRK05691 2661 QQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPE-LNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGD 2739
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2311 SIKSIQVSSRLNQQGYKMEIKDLFQYATIAELSPHIKQNLRI-ADQGEVKGKVSLTPIQHWFFEQTTTDQHYYNQAVMLH 2389
Cdd:PRK05691 2740 SILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAqAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLE 2819
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2390 APEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQNEEIAQSG-LYRLEVMNLKEdpdpgrtIEAKADEIQSSMHLS 2468
Cdd:PRK05691 2820 PRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQElLWQVTVADFAE-------CAALFADAQRSLDLQ 2892
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2469 DGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLPQKTDSFQLWAKRLSEYAQSETIKQ 2547
Cdd:PRK05691 2893 QGPLLRALLVDGPQGQQrLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLRE 2972
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2548 EQEYWTKIEQTEVKPLPKDFHETHTTAKDSETAAVEWTKEETELLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPI 2627
Cdd:PRK05691 2973 ELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLV 3052
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2628 HLEGHGREQIIQDIDISRTVGWFTSLYPVVLHAQPGKEIS--DYIKTTKEGLRQIPHKGIGYGIARYLSGG-----MPSK 2700
Cdd:PRK05691 3053 QLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAPGDDAArgESIKAIKEQLRAVPHKGLGYGVLRYLADAavreaMAAL 3132
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2701 LNPEISFNYLGQFDQDLQRHGvqLSSYSCGSDSSGHQER---PYVLNINGMITDGRLKLTISYSSKQYAKETIMRLSETI 2777
Cdd:PRK05691 3133 PQAPITFNYLGQFDQSFASDA--LFRPLDEPAGPAHDPDaplPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAY 3210
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2778 QSRLRTIITHCVHKEQSELTPSDILLKGISIDELDQLLIQlphAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFD 2857
Cdd:PRK05691 3211 LAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVP---AAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYR 3287
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2858 LQGELKIDWFKASLERLFETYAVLRTRFysGWN--DTPLQIVYKTQTPQIHFADLRDIEEHLREDAIAAYQREDKAKGFD 2935
Cdd:PRK05691 3288 INSALDPERFAQAWQAVVARHEALRASF--SWNagETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFD 3365
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2936 LARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQEGREPEPLSAVPYSDYIEWLDRQDQGAAKR 3015
Cdd:PRK05691 3366 LLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQ 3445
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3016 YWSGYLEGYKGETT------LLHKIAQHEQKeYAYANLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSA 3089
Cdd:PRK05691 3446 WWQDNLRGFERPTPipsdrpFLREHAGDSGG-MVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDR 3524
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3090 DVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRC---DEDSTFADTMQMVQQNALASQSYDTYPLYEIQAQTE--QKQN 3164
Cdd:PRK05691 3525 DVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLpaaGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSElpKGQP 3604
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3165 LIDHIMIFENYPIGQQAEETGHHgteLNITNFHMQEHSHYDLNVVVIPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQ 3244
Cdd:PRK05691 3605 LFDSLFVFENAPVEVSVLDRAQS---LNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLL 3681
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3245 QVLRQPSVKIEDLELLTQQEKEYLLSRFQSNDMHYPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLART 3324
Cdd:PRK05691 3682 ALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHA 3761
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3325 LQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLyCGKLQDDIGfsgtcIDLM 3404
Cdd:PRK05691 3762 LRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLV-CSAACREQA-----RALL 3835
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3405 EEhfYHEKDSSLALSYQSSQ-----------------LAYAIYTSGTTGKPKGTLIEHRQVihLIEGLSRQVYSAYDAEL 3467
Cdd:PRK05691 3836 DE--LGCANRPRLLVWEEVQagevashnpgiysgpdnLAYVIYTSGSTGLPKGVMVEQRGM--LNNQLSKVPYLALSEAD 3911
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3468 NIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLIG 3547
Cdd:PRK05691 3912 VIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPT 3991
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3548 GEALSKTTVNKLKQLFgehgAAPGITNVYGPTETCVDASLFNIECSSDAWArsqnYVPIGKPLGRNRMYILDSKKRLQPK 3627
Cdd:PRK05691 3992 GEAMPPELARQWLQRY----PQIGLVNAYGPAECSDDVAFFRVDLASTRGS----YLPIGSPTDNNRLYLLDEALELVPL 4063
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3628 GVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESV 3706
Cdd:PRK05691 4064 GAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEAR 4143
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3707 MLNVPDIQEAAAAALKDADDEyYLCGYFAADKTIQ-----ISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK05691 4144 LHEQAEVREAAVAVQEGVNGK-HLVGYLVPHQTVLaqgalLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3782 PAPVKKRDSGIEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHFFEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIE 3861
Cdd:PRK05691 4223 PALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVE 4302

                  ....*.
gi 166797876 3862 QLARTI 3867
Cdd:PRK05691 4303 ELAEYI 4308
PRK12467 PRK12467
peptide synthase; Provisional
2829-5211 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1612.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVYKTQTPQIHFA 2908
Cdd:PRK12467   51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQD-EEGFRQVIDASLSLTIPLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2909 DLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQEGR 2988
Cdd:PRK12467  130 DLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGR 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2989 EPEpLSAVP--YSDYI----EWLDRQDQGAAKRYWSGYLegyKGETTLLHKIAQHE---QKEYAYANLICRFDHEQTKQL 3059
Cdd:PRK12467  210 EPS-LPALPiqYADYAiwqrSWLEAGERERQLAYWQEQL---GGEHTVLELPTDRPrpaVPSYRGARLRVDLPQALSAGL 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3060 QQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEipDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQ 3139
Cdd:PRK12467  286 KALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAEVDPQASFLELLQQVKR 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3140 NALASQSYDTYPlYEIQAQTEQKQNLIDHIMIFEnYPIGQQAEETGHHGTE------LNITNFHMQEHS-HYDLNVVVIP 3212
Cdd:PRK12467  364 TALGAQAHQDLP-FEQLVEALQPERSLSHSPLFQ-VMFNHQNTATGGRDREgaqlpgLTVEELSWARHTaQFDLALDTYE 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3213 GKQ-LAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSNDMHYPREkTIHELFEE 3291
Cdd:PRK12467  442 SAQgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPD-CVHQLIEA 520
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3292 QAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSER 3371
Cdd:PRK12467  521 QARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR 600
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3372 IRYILNDSSISVLLYCGKLQDDI----GFSGTCIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQ 3447
Cdd:PRK12467  601 LAYMLDDSGVRLLLTQSHLLAQLpvpaGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA 680
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3448 VIHLIEGLSRqvYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHL 3527
Cdd:PRK12467  681 LANYVCVIAE--RLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHL 758
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3528 KLLIAAGDLQGVTLQH-LLIGGEALSKTTVNKLKQLfgehGAAPGITNVYGPTETCVDASLFniECSSDAwaRSQNYVPI 3606
Cdd:PRK12467  759 QALLQASRVALPRPQRaLVCGGEALQVDLLARVRAL----GPGARLINHYGPTETTVGVSTY--ELSDEE--RDFGNVPI 830
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3607 GKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPE-DRMYRTGDLARLLPDGNIEYIG 3685
Cdd:PRK12467  831 GQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADgGRLYRTGDLARYRADGVIEYLG 910
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3686 RIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEY---YLCGYFAAD---KTIQISELRKRMARHLPGYMIP 3759
Cdd:PRK12467  911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQlvaYLVPAAVADgaeHQATRDELKAQLRQVLPDYMVP 990
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3760 AHFVQLDKMPLTPNGKLNRQLLPAPV--KKRDSgieYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHFFEIGGHSLRATAL 3837
Cdd:PRK12467  991 AHLLLLDSLPLTPNGKLDRKALPKPDasAVQAT---FVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQV 1067
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3838 IAKIQKQMHVQIPLRDVFRFPTIEQLARTITKTELTGYAAIPAIEKRPYYPVSSAQKRLYILNHLEGGELSYNMLGLMTV 3917
Cdd:PRK12467 1068 ISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRL 1147
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3918 EGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQY---VLDHAAFEAEWYQGEEDDADL--YIRQFIR-PFHLDEPPL 3991
Cdd:PRK12467 1148 KGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVihpVGSLTLEEPLLLAADKDEAQLkvYVEAEARqPFDLEQGPL 1227
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3992 LRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGE------TLPPLRIQYKDYAVWQTGEARLQQIQKQEAY 4065
Cdd:PRK12467 1228 LRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAY 1307
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4066 WLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSP 4145
Cdd:PRK12467 1308 WKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVP 1387
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4146 IAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQ 4225
Cdd:PRK12467 1388 IANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQ 1467
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4226 NT-EQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELAR 4304
Cdd:PRK12467 1468 RDdHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGE 1547
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4305 LNMMTKEEERDIQQLFNDTAvAEKRIPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQV 4384
Cdd:PRK12467 1548 LDLLDEAERRQILEGWNATH-TGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVL 1626
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4385 VAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCAgHAIP--PLFEG-EVLLLDDPLLY-QG 4460
Cdd:PRK12467 1627 VGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS-HLQArlPLPDGlRSLVLDQEDDWlEG 1705
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4461 RTD-NLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSALSSGG 4538
Cdd:PRK12467 1706 YSDsNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAaDVVLQFTSFAFDVSVWELFWPLINGA 1785
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4539 ILFIIGNEAKRDIRQLNDFVRTHGIQTA-FLPTAFLKLLASEKHYFEPFAecVDHIIAAGEQLiATRMLRDMLARHQVT- 4616
Cdd:PRK12467 1786 RLVIAPPGAHRDPEQLIQLIERQQVTTLhFVPSMLQQLLQMDEQVEHPLS--LRRVVCGGEAL-EVEALRPWLERLPDTg 1862
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4617 LHNHYGPSETHV-VTMYTVD--PDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLET 4693
Cdd:PRK12467 1863 LFNLYGPTETAVdVTHWTCRrkDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAER 1942
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4694 FVPHPYDS-NQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSdLYAY 4770
Cdd:PRK12467 1943 FVADPFGTvGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQggVREAVVIAQDGANGKQ-LVAY 2021
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4771 FT----------AEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGlQTGTDYVAPRTNMEE 4840
Cdd:PRK12467 2022 VVptdpglvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAS-ELQQAYVAPQSELEQ 2100
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4841 QLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKiHKQFSKNISLREVFQCPTVGEMAqAIAEaETNGPDYIPKAKA 4920
Cdd:PRK12467 2101 RLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLA-AVAQ-EGDGTVSIDQGPV 2177
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4921 KDVYPVSSVQKMVYltTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTV----------VEMVREEAVQ 4990
Cdd:PRK12467 2178 TGDLPLLPIQQMFF--ADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGfvqedggwsaMHRAPEQERR 2255
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4991 VIKSQVEFS-MERYEATADEVEecfrafvRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLI---- 5065
Cdd:PRK12467 2256 PLLWQVVVAdKEELEALCEQAQ-------RSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQtayr 2328
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5066 QLYDGKELApLRIQYKDFTEWKHQKEQRERIKSQEE---YWLGVFHEElpSFELPKDFARPPVRSFDGKRHNFTLDKTVT 5142
Cdd:PRK12467 2329 QLQGGQPVK-LPAKTSAFKAWAERLQTYAASAALADelgYWQAQLQGA--STELPCDHPQGGLQRRHAASVTTHLDSEWT 2405
                        2410      2420      2430      2440      2450      2460      2470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 5143 QGIKQleelTGSTAYM-----ILFSAYSILLAKYSGQDDIVVGTPIAGR----PHADLEPIIGMFVNTLAIRTAPMAE 5211
Cdd:PRK12467 2406 RRLLQ----EAPAAYRtqvndLLLTALARVIARWTGQASTLIQLEGHGRedlfDEIDLTRTVGWFTSLYPVKLSPTAS 2479
PRK05691 PRK05691
peptide synthase; Validated
49-2347 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1474.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   49 LSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDRTSLILGIPTVSKQKAGQS----AVNNIVLLKNTLSNESTFKT 124
Cdd:PRK05691 1956 LSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEgligAFLNTQVLRCQLDGQMSVSE 2035
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  125 VFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMPLIHTVVSLNEIHSLQCKE----------DTATDTLFHFDLENN 194
Cdd:PRK05691 2036 LLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRQlagmtveylvNDARATKFDLNLEVT 2115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  195 GIHLKL----FYNGNLYDERYINQIVSHLDQLLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFE 270
Cdd:PRK05691 2116 DLDGRLgcclTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFA 2195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  271 EQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKE 350
Cdd:PRK05691 2196 AQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLE 2275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  351 RLQYLLHDADADVLLVQHHL------------KNSLAFDGPVIdlndeASYHADCslLSPVAGHSHLAYVIYTSGTTGKP 418
Cdd:PRK05691 2276 RLHYMIEDSGIGLLLSDRALfealgelpagvaRWCLEDDAAAL-----AAYSDAP--LPFLSLPQHQAYLIYTSGSTGKP 2348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  419 KGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLhLLPNEENKETFAIQNAIKQERITHF 498
Cdd:PRK05691 2349 KGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARV-VLRAQGQWGAEEICQLIREQQVSIL 2427
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  499 STSP----RLLKTMIEQmnrEDFIHVQHVVVGGEQLETDTVEKLH-SLQPRIrINNEYGPTENSVVSTFHPVQSADEQ-- 571
Cdd:PRK05691 2428 GFTPsygsQLAQWLAGQ---GEQLPVRMCITGGEALTGEHLQRIRqAFAPQL-FFNAYGPTETVVMPLACLAPEQLEEga 2503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  572 --ITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFV-EHLHVPGQKMYKTGDLARWLPDGR 648
Cdd:PRK05691 2504 asVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVaDPFAADGGRLYRTGDLVRLRADGL 2583
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  649 IEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAReDADGAKQLYAYYVGE----PSLTAAQFRE----ELSRE 720
Cdd:PRK05691 2584 VEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAvagqDDEAQAALREalkaHLKQQ 2662
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  721 LPNYMIPSRFIPLERIPLTSNGKIDLKALPAADENtRAENEYIAPRNTIEELLASIWQEVLGAERIGILDNFFDFGGDSI 800
Cdd:PRK05691 2663 LPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPE-LNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSI 2741
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  801 KSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQFVAPVSRV-ADQGEVNGGTKLTPIQHWFFEQKMPHAHHYNQAVMLYSA 879
Cdd:PRK05691 2742 LSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAqAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPR 2821
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  880 EGFKEGPLRRTMERIASHHDALRMIFEKTPDGY-APRITGTDESELFHLEVmnykgeTDPAQAIADKAnEIQSSMVLDKG 958
Cdd:PRK05691 2822 QALDPALLEQALQALVEHHDALRLRFSQADGRWqAEYRAVTAQELLWQVTV------ADFAECAALFA-DAQRSLDLQQG 2894
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  959 PLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQLPQKTDSFPFWADQLSKYAAETDMEEEI 1037
Cdd:PRK05691 2895 PLLRALLVDGPQGQQrLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREEL 2974
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1038 AYW-TELSSIKPQpLPKDTISEGSLLRDSEEVTIQWTKEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVN 1116
Cdd:PRK05691 2975 GWWqAQLGGPRAE-LPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQ 3053
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1117 LEGHGREPIIPDADISRTIGWFTSQYPVVLRMEAGKNLSQ--RIKIVKEGLRRIPDKGMNYSIIKYISGHPEADSLQLKP 1194
Cdd:PRK05691 3054 LEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAPGDDAARgeSIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALP 3133
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1195 E--ISFNYLGQFDQDLKHQAL-RISPFSTGLSMNENQERTAVLDLNGMIAEGTLSLTLSYSSKQYERSTMAQFARGLKES 1271
Cdd:PRK05691 3134 QapITFNYLGQFDQSFASDALfRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAE 3213
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1272 LQEVIAHCVSRQQTSLTPSDILLKDISIDELEQLLEQTRELgeaENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHG 1351
Cdd:PRK05691 3214 LQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEI---EDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINS 3290
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1352 DLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPLQIIFKTKKIGFQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGA 1431
Cdd:PRK05691 3291 ALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQP 3370
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1432 LMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQKQPEQSSITPYSQYIEWLGRQDAKEAAAYWDQY 1511
Cdd:PRK05691 3371 PFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDN 3450
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1512 LEGYEEQTGLPKDH-----HAAEDGRYVPEKVTCDISSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGS 1586
Cdd:PRK05691 3451 LRGFERPTPIPSDRpflreHAGDSGGMVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGV 3530
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1587 VVSGRPAGIPNVETMIGLFINTIPVRFRC-EAG--TTFAELMKEAQERAVASQKFETHPLYDIQARTT--QKQDLITHLM 1661
Cdd:PRK05691 3531 TVAGRPVSMPQMQRTVGLFINSIALRVQLpAAGqrCSVRQWLQGLLDSNMELREYEYLPLVAIQECSElpKGQPLFDSLF 3610
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1662 IFENYPVDQYMESIGRQ-NGTSITisnvqmeEQTNYDFNLTVI--PGDEMNISFEYNANVYERASIERVREHFMQILHQV 1738
Cdd:PRK05691 3611 VFENAPVEVSVLDRAQSlNASSDS-------GRTHTNFPLTAVcyPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLAL 3683
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1739 VTDADIRVDQAELLTEGERRTLLQTLNDTAAPFP--QTPVhQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTL 1816
Cdd:PRK05691 3684 VQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPleQSYV-RLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHAL 3762
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1817 RAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQ-------LAYEG 1889
Cdd:PRK05691 3763 RAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQaralldeLGCAN 3842
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1890 VTVLLDDESSYHQDGSDLAP--ISDVSHLAYVIYTSGSTGRPKGVLIE-HGGLTNYIwwAKEVYVKGEKAN-FPLYSSIS 1965
Cdd:PRK05691 3843 RPRLLVWEEVQAGEVASHNPgiYSGPDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQL--SKVPYLALSEADvIAQTASQS 3920
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1966 FDLTVTSIF-TPLVTGNAIIVYD--GEDKTALLESiVRDPRVDIIKLTPAHLQVLKEMNIADQTAVRRMIVGGENLSTRL 2042
Cdd:PRK05691 3921 FDISVWQFLaAPLFGARVEIVPNaiAHDPQGLLAH-VQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPEL 3999
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2043 ARSIHEQFEgRIEICNEYGPTETVVGCMIYRYDAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVAR 2122
Cdd:PRK05691 4000 ARQWLQRYP-QIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGR 4078
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2123 GYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAR 2201
Cdd:PRK05691 4079 GYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ 4158
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2202 EDVHGfKQLCAYYVSgGQTTAA------RLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFELQDRAEYK 2275
Cdd:PRK05691 4159 EGVNG-KHLVGYLVP-HQTVLAqgalleRIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYL 4236
                        2330      2340      2350      2360      2370      2380      2390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 2276 APRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQGYK-MEIKDLFQYATIAELSPHIK 2347
Cdd:PRK05691 4237 APRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRnVPLRAMFECSTVEELAEYIE 4309
PRK05691 PRK05691
peptide synthase; Validated
2829-5332 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1293.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVYKTQTPQIHFA 2908
Cdd:PRK05691  677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYER-DGVALQRIDAQGEFALQRI 755
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2909 DLRDIEEHLREdAIAAYQREDKAKG-FDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQEG 2987
Cdd:PRK05691  756 DLSDLPEAERE-ARAAQIREEEARQpFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQG 834
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2988 REPE--PLsAVPYSDYIEWlDRQ--DQGAAKR---YWSGYLEGYKGETTLLHKIAQHEQKEYAYANLICRFDHEQTKQLQ 3060
Cdd:PRK05691  835 QTAElaPL-PLGYADYGAW-QRQwlAQGEAARqlaYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALR 912
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3061 QIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAeiPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQN 3140
Cdd:PRK05691  913 GLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQA 990
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3141 ALASQSYDTYPLYE-IQAQTEQKQNLIDHIMI---------FENYPiGQQAEETGHHGTElniTNFHMQEHSHYDLNvvv 3210
Cdd:PRK05691  991 TLGAQAHQDLPFEQlVEALPQAREQGLFQVMFnhqqrdlsaLRRLP-GLLAEELPWHSRE---AKFDLQLHSEEDRN--- 1063
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3211 ipgKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSNDMhyPREKTIHELFE 3290
Cdd:PRK05691 1064 ---GRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCA--PAQAWLPELLN 1138
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3291 EQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSE 3370
Cdd:PRK05691 1139 EQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAE 1218
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3371 RIRYILNDSSISVLLYCGKLQDDI-GFSGTC-IDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQv 3448
Cdd:PRK05691 1219 RLAYMLADSGVELLLTQSHLLERLpQAEGVSaIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA- 1297
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3449 ihLIEGLS-RQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHL 3527
Cdd:PRK05691 1298 --LAERLQwMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLL 1375
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3528 KLLIAAGDLQGVT-LQHLLIGGEALSKTTVNKLKQLFgehgaaPGIT--NVYGPTETCVDASLFniECSSDAWARSqnyv 3604
Cdd:PRK05691 1376 QLFIDEPLAAACTsLRRLFSGGEALPAELRNRVLQRL------PQVQlhNRYGPTETAINVTHW--QCQAEDGERS---- 1443
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 PIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPE-DRMYRTGDLARLLPDGNIEY 3683
Cdd:PRK05691 1444 PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDgARLYRTGDRARWNADGALEY 1523
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3684 IGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEyYLCGYFAADKT--IQISELRKRMARHLPGYMIPAH 3761
Cdd:PRK05691 1524 LGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGA-QLVGYYTGEAGqeAEAERLKAALAAELPEYMVPAQ 1602
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3762 FVQLDKMPLTPNGKLNRQLLPAPVKKRDsgiEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHFFEIGGHSLRATALIAKI 3841
Cdd:PRK05691 1603 LIRLDQMPLGPSGKLDRRALPEPVWQQR---EHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRT 1679
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3842 QKQMHVQIPLRDVFRFPTI----EQLARTITKTELTGYAAIPAIEKRPYYPVSSAQKRLYILNHLEGGELSYNMLGLMTV 3917
Cdd:PRK05691 1680 RQACDVELPLRALFEASELgafaEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARL 1759
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3918 EGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEWYQGEEDDAD--------LYIRQFIRPFHLDEP 3989
Cdd:PRK05691 1760 SGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADarqqrlqqLADSEAHQPFDLERG 1839
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3990 PLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEG------ETLPPLRIQYKDYAVWQTGEARLQQIQKQE 4063
Cdd:PRK05691 1840 PLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAflddreSPLEPLPVQYLDYSVWQRQWLESGERQRQL 1919
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4064 AYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVG 4143
Cdd:PRK05691 1920 DYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIG 1999
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4144 SPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIARDLSRNPLFDTMFV 4223
Cdd:PRK05691 2000 APVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCN 2079
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4224 LQNTE-QEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAEL 4302
Cdd:PRK05691 2080 VQRWEfQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRL 2159
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4303 ARLNMMTKEEERDIQQLFNDTAVaEKRIPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTD 4382
Cdd:PRK05691 2160 AELPLLAAAEQQQLLDSLAGEAG-EARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQ 2238
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4383 QVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLtcaGHAIppLFE--GEV--------LLL 4452
Cdd:PRK05691 2239 VRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL---SDRA--LFEalGELpagvarwcLED 2313
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4453 DDPLLYQGRTDNL-NLSCSENdLMYVIYTSGTTGQPKGVQLEHKTMTNllayeqdHTQLRFDRV--------LQFAAMSF 4523
Cdd:PRK05691 2314 DAAALAAYSDAPLpFLSLPQH-QAYLIYTSGSTGKPKGVVVSHGEIAM-------HCQAVIERFgmraddceLHFYSINF 2385
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4524 DVCYQEMFSALSSGG--ILFIIGNEAKRDIRQLndfVRTHGIQT-AFLPTAFLKL---LASEKHyFEPFAECvdhiIAAG 4597
Cdd:PRK05691 2386 DAASERLLVPLLCGArvVLRAQGQWGAEEICQL---IREQQVSIlGFTPSYGSQLaqwLAGQGE-QLPVRMC----ITGG 2457
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4598 EQLIATRMLRDMLARHQVTLHNHYGPSETHVVTMYTVDPDTDQELQ---PIGKPISNTEIFILNEAGTLQPVGIVGELCI 4674
Cdd:PRK05691 2458 EALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAasvPIGRVVGARVAYILDADLALVPQGATGELYV 2537
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4675 SGVSLARGYHNRESLTLETFVPHPYDSNQ-RMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQ 4751
Cdd:PRK05691 2538 GGAGLAQGYHDRPGLTAERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHpaVR 2617
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4752 EAVVLAKENTDGQ-------SDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAG 4824
Cdd:PRK05691 2618 EAVVLALDTPSGKqlagylvSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPE 2697
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4825 LQTgTDYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIhKQFSKNISLREVFQCPTVGEMAQAI 4904
Cdd:PRK05691 2698 LNR-QAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRA-RQLGIHFSPRDLFQHQTVQTLAAVA 2775
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4905 AEAETNGPDYIPKAKAKDVYPvssVQKMVYLTtqiiggELP----YNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTV 4980
Cdd:PRK05691 2776 THSEAAQAEQGPLQGASGLTP---IQHWFFDS------PVPqpqhWNQALLLEPRQALDPALLEQALQALVEHHDALRLR 2846
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4981 VEMV----REEAVQVIKSQVefsmeRYEATADEVEEC---FRAFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITD 5053
Cdd:PRK05691 2847 FSQAdgrwQAEYRAVTAQEL-----LWQVTVADFAECaalFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVD 2921
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5054 GASMNIFVEKLIQLY----DGKELaPLRIQYKDFTEWKHQKEQRERIKSQEEYwLGVFHEEL--PSFELPKDFARPPVRS 5127
Cdd:PRK05691 2922 GVSWRVLLEDLQALYrqlsAGAEP-ALPAKTSAFRDWAARLQAYAGSESLREE-LGWWQAQLggPRAELPCDRPQGGNLN 2999
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5128 FDGKRHNFTLDKTVTQGIKQleelTGSTAYM-----ILFSAYSILLAKYSGQDDIVVGTPIAGRPHA----DLEPIIGMF 5198
Cdd:PRK05691 3000 RHAQTVSVRLDAERTRQLLQ----QAPAAYRtqvndLLLTALARVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWF 3075
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5199 VNTLAIRTAP--MAEKTFLDYITETKEtMLKAFEHQEYPFeelveklGVKRDLSRNPLFDTMFVLQNTE-------QTDI 5269
Cdd:PRK05691 3076 TSAYPLRLTPapGDDAARGESIKAIKE-QLRAVPHKGLGY-------GVLRYLADAAVREAMAALPQAPitfnylgQFDQ 3147
                        2570      2580      2590      2600      2610      2620      2630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 5270 EVDSLAV-RPYEQTETAAKfDLQL---NFL-IDQD----EIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIM 5332
Cdd:PRK05691 3148 SFASDALfRPLDEPAGPAH-DPDAplpNELsVDGQvyggELVLRWTYSAERYDEQTIAELAEAYLAELQALI 3218
PRK12467 PRK12467
peptide synthase; Provisional
3888-5344 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1124.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEW-- 3965
Cdd:PRK12467   51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLdd 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3966 -YQGEEDDADLYIRQFI-----RPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGE----- 4034
Cdd:PRK12467  131 lANEQGRARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgre 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4035 -TLPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLAS 4113
Cdd:PRK12467  211 pSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQ 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4114 QTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYE 4193
Cdd:PRK12467  291 REGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQA 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4194 HQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQ-----EQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTL 4268
Cdd:PRK12467  371 HQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATggrdrEGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAF 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4269 EYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDIQQLFNdtAVAEKRIPTTIHQLFEQQAERNPDH 4348
Cdd:PRK12467  451 TYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWN--APATEYAPDCVHQLIEAQARQHPER 528
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4349 EAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDS 4428
Cdd:PRK12467  529 PALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDS 608
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4429 GADVLLT-CAGHAIPPLFEG-EVLLLDDPL-LYQGRTD-NLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYE 4504
Cdd:PRK12467  609 GVRLLLTqSHLLAQLPVPAGlRSLCLDEPAdLLCGYSGhNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVI 688
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4505 QDHTQLRFD-RVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASekhyf 4583
Cdd:PRK12467  689 AERLQLAADdSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ----- 763
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4584 epfAECVD------HIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHV-VTMYTV-DPDTDQELQPIGKPISNTEIF 4655
Cdd:PRK12467  764 ---ASRVAlprpqrALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVgVSTYELsDEERDFGNVPIGQPLANLGLY 840
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4656 ILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSN-QRMYKTGDLARYLPEGNIEYAGRRDHQVKIRG 4734
Cdd:PRK12467  841 ILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADgGRLYRTGDLARYRADGVIEYLGRMDHQVKIRG 920
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4735 YRVELGEVEAALLKH--VQEAVVLAKENtDGQSDLYAYFT-------AEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKL 4805
Cdd:PRK12467  921 FRIELGEIEARLLAQpgVREAVVLAQPG-DAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSL 999
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4806 PLTGNGKVNRRALPMPEAGLQTGTdYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKN 4885
Cdd:PRK12467 1000 PLTPNGKLDRKALPKPDASAVQAT-FVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQ 1078
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4886 ISLREVFQCPTVGEMAQAIAEAETNGPDYIPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLT 4965
Cdd:PRK12467 1079 VPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALER 1158
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4966 AFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMERYE-ATADEVEECFRAFV-----RPFDLSQAPLLRAGLIELEQD 5039
Cdd:PRK12467 1159 SFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLlLAADKDEAQLKVYVeaearQPFDLEQGPLLRVGLLRLAAD 1238
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5040 LHIFMFDMHHIITDGASMNIFVEKLIQLYDGK------ELAPLRIQYKDFTEWkhqkeQRERIKSQEE-----YWLGVFH 5108
Cdd:PRK12467 1239 EHVLVLTLHHIVSDGWSMQVLVDELVALYAAYsqgqslQLPALPIQYADYAVW-----QRQWMDAGERarqlaYWKAQLG 1313
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5109 EELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPH 5188
Cdd:PRK12467 1314 GEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNR 1393
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5189 ADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNT-EQT 5267
Cdd:PRK12467 1394 AETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDdHQA 1473
                        1450      1460      1470      1480      1490      1500      1510
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 5268 DIEVDSLAVRPYEQTETAAKFDLQLNFLIDQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQL 5344
Cdd:PRK12467 1474 QAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDL 1550
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3876-5169 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1045.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3876 AAIPAIEKRPYYPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYV 3955
Cdd:COG1020     7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3956 LDHAAFEAEWY--------QGEEDDADLYIRQFIRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEF 4027
Cdd:COG1020    87 QPVVAAPLPVVvllvdleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4028 IRIY------EGETLPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLD 4101
Cdd:COG1020   167 LRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4102 KQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYL 4181
Cdd:COG1020   247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4182 SEVKENALKAYEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEG 4261
Cdd:COG1020   327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETG 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4262 AGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDIQQLFNDTAVAEKRiPTTIHQLFEQQ 4341
Cdd:COG1020   407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPA-DATLHELFEAQ 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRR 4421
Cdd:COG1020   486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4422 AFMLKDSGADVLLTCAGHAIP-PLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNL 4500
Cdd:COG1020   566 AYMLEDAGARLVLTQSALAARlPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4501 LAYEQDHTQLR-FDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASe 4579
Cdd:COG1020   646 LAWMQRRYGLGpGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD- 724
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4580 kHYFEPFAEcVDHIIAAGEQLiATRMLRDMLARH-QVTLHNHYGPSETHV-VTMYTVDP-DTDQELQPIGKPISNTEIFI 4656
Cdd:COG1020   725 -AAPEALPS-LRLVLVGGEAL-PPELVRRWRARLpGARLVNLYGPTETTVdSTYYEVTPpDADGGSVPIGRPIANTRVYV 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4657 LNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYD-SNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGY 4735
Cdd:COG1020   802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGF 881
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:COG1020   882 RIELGEIEAALLQHpgVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNG 961
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4814 NRRALPMPEAGLQTGTDYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQ 4893
Cdd:COG1020   962 KLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFL 1041
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4894 CPTVGEMAQAIAEAETNGPDYIPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQG 4973
Cdd:COG1020  1042 AAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLAL 1121
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4974 HEPLRTVVEMVREEAVQVIKSQVEF----------SMERYEATADEVEECFRAFVRPFDLSQAPLLRAGLIELEQDLHIF 5043
Cdd:COG1020  1122 LAALRARRAVRQEGPRLRLLVALAAalalaallalLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLL 1201
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5044 MFDMHHIITDGASMNIFVEKLIQLYDGKELAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARP 5123
Cdd:COG1020  1202 LLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLP 1281
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876 5124 PVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFSAYSILLA 5169
Cdd:COG1020  1282 ALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
PRK05691 PRK05691
peptide synthase; Validated
3284-5336 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 995.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVF------EGKQFTYEELNRRANQLARTLQAKGVQADQLVgIMTERSLEMVVGILGVLKAG 3357
Cdd:PRK05691   10 TLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3358 GAYLPIDPDSPS-----ERIRYILNDSSISVLLYCGKLQDDIGFSGT----------CIDLMeehfyhekDSSLALSYQS 3422
Cdd:PRK05691   89 VIAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRDSLLQMEElaaanapellCVDTL--------DPALAEAWQE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3423 SQL-----AYAIYTSGTTGKPKGTLIEHRQVIhLIEGLSRQvysAYDAELN----IAMLAPYYFDAS-VQQMYASLLSGh 3492
Cdd:PRK05691  161 PALqpddiAFLQYTSGSTALPKGVQVSHGNLV-ANEQLIRH---GFGIDLNpddvIVSWLPLYHDMGlIGGLLQPIFSG- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3493 tlfiVPKEIVSDGAALCRYYR------QHSIDITDGTPAHLKLL---IAAGDLQGVTLQHLLI---GGEALSKTTVNklk 3560
Cdd:PRK05691  236 ----VPCVLMSPAYFLERPLRwleaisEYGGTISGGPDFAYRLCserVSESALERLDLSRWRVaysGSEPIRQDSLE--- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3561 qLFGEHGAAPGIT-NVYGPTETCVDASLF-----------NIECSSDAWARSQNYVPIGKPL---GRNR----MYILDSK 3621
Cdd:PRK05691  309 -RFAEKFAACGFDpDSFFASYGLAEATLFvsggrrgqgipALELDAEALARNRAEPGTGSVLmscGRSQpghaVLIVDPQ 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3622 kRLQ--PKGVQGELYIAGDGVGRGYLNLPELTdekfvADPFVPED--RMYRTGDLArLLPDGNIEYIGRIDHQVKIQGFR 3697
Cdd:PRK05691  388 -SLEvlGDNRVGEIWASGPSIAHGYWRNPEAS-----AKTFVEHDgrTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHN 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3698 IELGEIESVMLNVPDIQEAAAAALkdaddeyylcgyFAAD----KTIQIS-ELRKRMARHLPGYMI-------------- 3758
Cdd:PRK05691  461 LYPQDIEKTVEREVEVVRKGRVAA------------FAVNhqgeEGIGIAaEISRSVQKILPPQALiksirqavaeacqe 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3759 -PAHFVQLD--KMPLTPNGKLNRQ---------------LLPAPvkkrDSGIEYVPPQTSAEIQ--LTAIWEDVLGLEQV 3818
Cdd:PRK05691  529 aPSVVLLLNpgALPKTSSGKLQRSacrlrladgsldsyaLFPAL----QAVEAAQTAASGDELQarIAAIWCEQLKVEQV 604
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3819 GIRDHFFEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLARTITKTELTG---YAAIPAIEKRPYYPVSSAQKR 3895
Cdd:PRK05691  605 AADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGgaaQAAIARLPRGQALPQSLAQNR 684
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3896 LYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAF-------------- 3961
Cdd:PRK05691  685 LWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFalqridlsdlpeae 764
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3962 -EAEWYQGEEDDADLyirqfirPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIY----EGET- 4035
Cdd:PRK05691  765 rEARAAQIREEEARQ-------PFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYaaacQGQTa 837
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4036 -LPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQ 4114
Cdd:PRK05691  838 eLAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQA 917
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4115 TESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEH 4194
Cdd:PRK05691  918 HQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAH 997
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4195 QDYPFEVLIDQLNIARDlsrNPLFDTMFvlqNTEQEQLE----INDVTFKPYPNGHTMAKFDLTLTAVEEGAG-IQFTLE 4269
Cdd:PRK05691  998 QDLPFEQLVEALPQARE---QGLFQVMF---NHQQRDLSalrrLPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFD 1071
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4270 YLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEErdiQQLFNDTAVAEKRIPTTIHQLFEQQAERNPDHE 4349
Cdd:PRK05691 1072 YAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAER---AQLAQWGQAPCAPAQAWLPELLNEQARQTPERI 1148
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4350 AVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSG 4429
Cdd:PRK05691 1149 ALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4430 ADVLLTcAGHAIPPLFEGE---VLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQD 4506
Cdd:PRK05691 1229 VELLLT-QSHLLERLPQAEgvsAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQA 1307
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4507 HTQLRFDRVL-QFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASekhyfEP 4585
Cdd:PRK05691 1308 TYALDDSDVLmQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID-----EP 1382
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4586 F-AEC--VDHIIAAGEQLIATrmLRDMLARH--QVTLHNHYGPSETHV-VTMYTVDPDtDQELQPIGKPISNTEIFILNE 4659
Cdd:PRK05691 1383 LaAACtsLRRLFSGGEALPAE--LRNRVLQRlpQVQLHNRYGPTETAInVTHWQCQAE-DGERSPIGRPLGNVLCRVLDA 1459
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4660 AGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPY-DSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVE 4738
Cdd:PRK05691 1460 ELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVE 1539
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4739 LGEVEAALLKH--VQEAVVLAKENTDGQSdLYAYFTAE--QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVN 4814
Cdd:PRK05691 1540 PEEIQARLLAQpgVAQAAVLVREGAAGAQ-LVGYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLD 1618
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4815 RRALPMPeaGLQTGtDYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQC 4894
Cdd:PRK05691 1619 RRALPEP--VWQQR-EHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEA 1695
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4895 PTVGEMAQAIA----EAETNGPDYIPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRL 4970
Cdd:PRK05691 1696 SELGAFAEQVAriqaAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQAL 1775
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4971 MQGHEPLRTVVEMVREEAVQVIKSQVEFSMERYEATADEVEE--------CFRAFVRPFDLSQAPLLRAGLIELEQDLHI 5042
Cdd:PRK05691 1776 ILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADArqqrlqqlADSEAHQPFDLERGPLLRACLVKAAEREHY 1855
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5043 FMFDMHHIITDGASMNIFVEKLIQLY----DGKE--LAPLRIQYKDFTEWKHQ-KEQRERiKSQEEYWLGVFHEELPSFE 5115
Cdd:PRK05691 1856 FVLTLHHIVTEGWAMDIFARELGALYeaflDDREspLEPLPVQYLDYSVWQRQwLESGER-QRQLDYWKAQLGNEHPLLE 1934
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5116 LPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPII 5195
Cdd:PRK05691 1935 LPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLI 2014
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5196 GMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTE-QTDIEVDSL 5274
Cdd:PRK05691 2015 GAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLAGM 2094
                        2170      2180      2190      2200      2210      2220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 5275 AVRPYEQTETAAKFDLQLNfLIDQDEIQG-SFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPS 5336
Cdd:PRK05691 2095 TVEYLVNDARATKFDLNLE-VTDLDGRLGcCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQ 2156
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1302-2622 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 954.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1302 LEQLLEQTRELGEAENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWk 1381
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1382 DQPLQIIFKTKKIGFQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCL 1461
Cdd:COG1020    80 GRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1462 PLITKEIFENYFALLQ-QKQPEQSSITPYSQY----IEWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPE 1536
Cdd:COG1020   160 GLLLAELLRLYLAAYAgAPLPLPPLPIQYADYalwqREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1537 KVTCDISSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCE 1616
Cdd:COG1020   240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1617 AGTTFAELMKEAQERAVASQKFETHPLYDIQ-----ARTTQKQDLITHLMIFENYPVDQymesigrQNGTSITISNVQME 1691
Cdd:COG1020   318 GDPSFAELLARVRETLLAAYAHQDLPFERLVeelqpERDLSRNPLFQVMFVLQNAPADE-------LELPGLTLEPLELD 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1692 EQT-NYDFNLTVIP-GDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAA 1769
Cdd:COG1020   391 SGTaKFDLTLTVVEtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAA 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1770 PFPQ-TPVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSG 1848
Cdd:COG1020   471 PYPAdATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1849 GAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVL-LDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTG 1927
Cdd:COG1020   551 AAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTG 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1928 RPKGVLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIVRDpRV 2004
Cdd:COG1020   631 RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEarrDPAALAELLARH-RV 709
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2005 DIIKLTPAHLQVLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRiEICNEYGPTETVVGCMIYRYDAAKDRRESV 2084
Cdd:COG1020   710 TVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGA-RLVNLYGPTETTVDSTYYEVTPPDADGGSV 788
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2085 PIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEY 2163
Cdd:COG1020   789 PIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEF 868
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2164 AGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVS--GGQTTAARLRKQLSQTLASYMVPAY 2241
Cdd:COG1020   869 LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPeaGAAAAAALLRLALALLLPPYMVPAA 948
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2242 FIELDEMPLTSNGKINKKGLPAPDFelQDRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRL 2321
Cdd:COG1020   949 VVLLLPLPLTGNGKLDRLALPAPAA--AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARA 1026
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2322 NQQGYKMEIKDLFQYATIAELSPHIKQNLRIADQGEVKGKVSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQ 2401
Cdd:COG1020  1027 ARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLL 1106
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2402 TLQKLAEHHDALRMTFRTTENGCEAQNEEIAQSGL--YRLEVMNLKEDPDPGRTIEAKADEIQSSMHLSDGPLMKAGLFQ 2479
Cdd:COG1020  1107 LLLALLLLLALLLALLAALRARRAVRQEGPRLRLLvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLL 1186
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2480 CADGDHLLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTKIEQTE 2559
Cdd:COG1020  1187 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALAL 1266
                        1290      1300      1310      1320      1330      1340
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 2560 VKPLPKDFHETHTTAKDSETAAVEWTKEETELLLKQANRAYHTEINDLLLTSLGLSISHWSGL 2622
Cdd:COG1020  1267 LALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2811-4131 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 920.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2811 LDQLLIQLPHAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWn 2890
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2891 DTPLQIVYKTQTPQIHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCL 2970
Cdd:COG1020    80 GRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2971 SLITKEVFDHYSALQEGRE-PEPLSAVPYSDYIEWLDRQDQG----AAKRYWSGYLEGYKGETTLLHKIAQHEQKEYAYA 3045
Cdd:COG1020   160 GLLLAELLRLYLAAYAGAPlPLPPLPIQYADYALWQREWLQGeelaRQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3046 NLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAeiPDVEQMIGLFINTIPVRIRCD 3125
Cdd:COG1020   240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3126 EDSTFADTMQMVQQNALASQSYDTYPLYEIQAQTEQKQN-----LIDHIMIFENYPIGQQaEETGHHGTELNITNfhmqE 3200
Cdd:COG1020   318 GDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDlsrnpLFQVMFVLQNAPADEL-ELPGLTLEPLELDS----G 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3201 HSHYDLNVVVIP-GKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSNDMHY 3279
Cdd:COG1020   393 TAKFDLTLTVVEtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPY 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3280 PREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA 3359
Cdd:COG1020   473 PADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3360 YLPIDPDSPSERIRYILNDSSISVLLYCGKLQDDI-GFSGTCIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKP 3438
Cdd:COG1020   553 YVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRP 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3439 KGTLIEHRQVIHLIEGLSRQVysAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSID 3518
Cdd:COG1020   633 KGVMVEHRALVNLLAWMQRRY--GLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVT 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3519 ITDGTPAHLKLLIAAGDLQGVTLQHLLIGGEALSKTTVNKLKQLFgehgaaPGIT--NVYGPTETCVDASLFNIEcSSDA 3596
Cdd:COG1020   711 VLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARL------PGARlvNLYGPTETTVDSTYYEVT-PPDA 783
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3597 WARSqnyVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRMYRTGDLARL 3675
Cdd:COG1020   784 DGGS---VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARW 860
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3676 LPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS--ELRKRMARHL 3753
Cdd:COG1020   861 LPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaaLLRLALALLL 940
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3754 PGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVkkRDSGIEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHFFEIGGHSLR 3833
Cdd:COG1020   941 PPYMVPAAVVLLLPLPLTGNGKLDRLALPAPA--AAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLL 1018
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3834 ATALIAKIQKQMHVQIPLRDVFRFPTIEQLARTITKTELTGYAAIPAIEKRPYYPVSSAQKRLYILNHLEGGELSYNMLG 3913
Cdd:COG1020  1019 LLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLAL 1098
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3914 LMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEWYQGEEDDADLY------IRQFIRPFHLD 3987
Cdd:COG1020  1099 LLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAaaaaelLAAAALLLLLA 1178
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3988 EPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGET------LPPLRIQYKDYAVWQTGEARLQQIQK 4061
Cdd:COG1020  1179 LLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAaaaallALALLLALLALAALLALAALAALAAA 1258
                        1290      1300      1310      1320      1330      1340      1350
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4062 QEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLL 4131
Cdd:COG1020  1259 LLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
PRK12316 PRK12316
peptide synthase; Provisional
3852-5344 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 868.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3852 RDVFRFPTIEQLART-----------------------------ITKTELTGYAaIPAIEKRPYYPVSSAQKRL--YILN 3900
Cdd:PRK12316 1494 REMFAEATVQRLADDyarelqaliehccdernrgvtpsdfplagLSQAQLDALP-LPAGEIADIYPLSPMQQGMlfHSLY 1572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3901 HLEGGELSYNMLglMTVEGkLDRDKLQQAFRTLILRHESLRTGFKMADG--EPVQYVLDHAAF---EAEWYQGEEDDADL 3975
Cdd:PRK12316 1573 EQEAGDYINQLR--VDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVELpfaELDWRGREDLGQAL 1649
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3976 -----YIRQfiRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGETLPPLRIQYKDYAVWq 4050
Cdd:PRK12316 1650 dalaqAERQ--KGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAW- 1726
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4051 tgearLQQIQKQ--EAYWLE-LYSGDVPVLHlpADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASY 4127
Cdd:PRK12316 1727 -----LQRQDAAasEAFWKEqLAALEEPTRL--AQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAW 1799
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4128 TLLLSKYSGQEDIIVGSPIAGRPhADLEPI---IGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFevlid 4204
Cdd:PRK12316 1800 LLLLQRYTGQETVAFGATVAGRP-AELPGIeqqIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPL----- 1873
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4205 qLNIAR--DLSRNPLFDTMFVLQN---TEQ-EQLEINDVTFKPYPNgHTMAKFDLTLtAVEEGAGIQFTLEYLTALFKPE 4278
Cdd:PRK12316 1874 -YDIQRwaGQGGEALFDSLLVFENypvAEAlKQGAPAGLVFGRVSN-HEQTNYPLTL-AVTLGETLSLQYSYDRGHFDAA 1950
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4279 TIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDIQQLFNDTAVAEKRIPTtIHQLFEQQAERNPDHEAVMFGNQTL 4358
Cdd:PRK12316 1951 AIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPG-VHQRIAEQAARAPEAIAVVFGDQHL 2029
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4359 TYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCAG 4438
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH 2109
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4439 HA--IPPLFEGEVLLLDDPLLYQGRTD-NLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLR-FDR 4514
Cdd:PRK12316 2110 LLerLPLPAGVARLPLDRDAEWADYPDtAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSpADC 2189
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4515 VLQFAAMSFDVCYQEMFSALSSGGILfIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEKHYfEPFAECVDHII 4594
Cdd:PRK12316 2190 ELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAER-DGRPPAVRVYC 2267
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4595 AAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVV-TMYTVDPD--TDQELQPIGKPISNTEIFILNEAGTLQPVGIVGE 4671
Cdd:PRK12316 2268 FGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTpLLWKCRPQdpCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGE 2347
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4672 LCISGVSLARGYHNRESLTLETFVPHPYD-SNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH- 4749
Cdd:PRK12316 2348 LYLGGEGLARGYLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHp 2427
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4750 -VQEAVVLAKENTDGQSdLYAYFTAE--QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGlQ 4826
Cdd:PRK12316 2428 aVREAVVVAQDGASGKQ-LVAYVVPDdaAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS-Q 2505
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4827 TGTDYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQCPTVGEMAQAIAE 4906
Cdd:PRK12316 2506 LRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLES 2585
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4907 AETNGPDYIPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVRE 4986
Cdd:PRK12316 2586 GQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGE 2665
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4987 EAVQVIKSQVEFSMERYEaTADEVEECFRAFV-----RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFV 5061
Cdd:PRK12316 2666 QTRQVILPNMSLRIVLED-CAGVADAAIRQRVaeeiqRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMV 2744
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5062 EKLIQLYDGKE------LAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNF 5135
Cdd:PRK12316 2745 DELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDV 2824
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5136 TLDKTVTQGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFL 5215
Cdd:PRK12316 2825 ALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFR 2904
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5216 DYITETKETMLKAFEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQTDIEVDSLAVRPYEQTETAAKFDLQLNFL 5295
Cdd:PRK12316 2905 DLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTW 2984
                        1530      1540      1550      1560
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876 5296 IDQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQL 5344
Cdd:PRK12316 2985 ESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAM 3033
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2-1104 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 825.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    2 SVFKTQETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLY 81
Cdd:COG1020   202 EELARQLAYWRQQLAGLPPLLELP----TDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLA 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   82 KYTDRTSLILGIPTvskqkAG--QSAVN-------NIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLS 152
Cdd:COG1020   278 RYSGQDDVVVGTPV-----AGrpRPELEglvgffvNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQ 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  153 VQYNDEHMPLIHTVVSLN-------EIHSLQCKEDTATDTLFHFDL------ENNGIHLKLFYNGNLYDERYINQIVSHL 219
Cdd:COG1020   353 PERDLSRNPLFQVMFVLQnapadelELPGLTLEPLELDSGTAKFDLtltvveTGDGLRLTLEYNTDLFDAATIERMAGHL 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  220 DQLLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKAS 299
Cdd:COG1020   433 VTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARAN 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  300 RLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSL-AFDG 378
Cdd:COG1020   513 RLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGV 592
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  379 PVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAF 458
Cdd:COG1020   593 PVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS 672
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  459 ILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMnREDFIHVQHVVVGGEQLETDTVEKL 538
Cdd:COG1020   673 VWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAA-PEALPSLRLVLVGGEALPPELVRRW 751
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  539 HSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ---ITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNR 615
Cdd:COG1020   752 RARLPGARLVNLYGPTETTVDSTYYEVTPPDADggsVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNR 831
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  616 PELTEEKFVEH-LHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADG 694
Cdd:COG1020   832 PELTAERFVADpFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPG 911
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  695 AKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADENTRAenEYIAPRNTIEEL 772
Cdd:COG1020   912 DKRLVAYVVPEAgaAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--AAAAPPAEEEEE 989
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  773 LASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQFVAPVSRVADQGEVNGGTKL 852
Cdd:COG1020   990 EAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAP 1069
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  853 TPIQHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGTDESELFH--LEVM 930
Cdd:COG1020  1070 LPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVAlaAALA 1149
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  931 NYKGETDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDHLLIAIHHLLIDGVSWRILLEDFASG----YEQAERRQ 1006
Cdd:COG1020  1150 LAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLllllLLLAAAAA 1229
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1007 TIQLPQKTDSFPFWADQLSKYAAETDMEEEIAYWTELSSIKPQPLPKDTISEGSLLRDSEEVTIQWTKEETEQLLKQANR 1086
Cdd:COG1020  1230 ALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLAL 1309
                        1130
                  ....*....|....*...
gi 166797876 1087 AYNTDINDLLLTSLGLAV 1104
Cdd:COG1020  1310 ALALLLLLLLLLALLLLA 1327
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1778-2265 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 776.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHG 1937
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1938 GLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKT--ALLESIVRDPRVDIIKLTPAHLQ 2015
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLdgQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 VLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCMIYRYDAAKDRRESVPIGTAAANTSI 2095
Cdd:cd17655   241 LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2096 YVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRG 2175
Cdd:cd17655   321 YILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2176 YRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGK 2255
Cdd:cd17655   401 YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGK 480
                         490
                  ....*....|
gi 166797876 2256 INKKGLPAPD 2265
Cdd:cd17655   481 VDRKALPEPD 490
PRK12467 PRK12467
peptide synthase; Provisional
1308-2625 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 764.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1308 QTRELGEAeniYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFyRGWKDQPLQI 1387
Cdd:PRK12467   42 QVRSAFER---IPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRF-VQDEEGFRQV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1388 IFKTKKIGFQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKE 1467
Cdd:PRK12467  118 IDASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEE 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1468 IFENYFALLQQKQPEQSSI-TPYSQYIEWlGRQ--DAKEAA---AYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCD 1541
Cdd:PRK12467  198 LVQLYSAYSQGREPSLPALpIQYADYAIW-QRSwlEAGERErqlAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVD 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1542 ISSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPagipNVET--MIGLFINTIPVRFRCEAGT 1619
Cdd:PRK12467  277 LPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRN----RVETerLIGFFVNTQVLKAEVDPQA 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1620 TFAELMKEAQERAVASQKFETHPLYDIqARTTQKQDLITHLMIFENYPVDQYMESIGRQNG----TSITISNVQMEEQT- 1694
Cdd:PRK12467  353 SFLELLQQVKRTALGAQAHQDLPFEQL-VEALQPERSLSHSPLFQVMFNHQNTATGGRDREgaqlPGLTVEELSWARHTa 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1695 NYDFNL-TVIPGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQTLNDTAAPFPQ 1773
Cdd:PRK12467  432 QFDLALdTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAP 511
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1774 TPVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVP 1853
Cdd:PRK12467  512 DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVP 591
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1854 IDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAY-EGVTVLLDDESS---YHQDGSDLAPISDVSHLAYVIYTSGSTGRP 1929
Cdd:PRK12467  592 LDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVpAGLRSLCLDEPAdllCGYSGHNPEVALDPDNLAYVIYTSGSTGQP 671
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1930 KGVLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIV------YDGEDKTALLEsivrDPR 2003
Cdd:PRK12467  672 KGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLlppdcaRDAEAFAALMA----DQG 747
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2004 VDIIKLTPAHLQVLKEMNIADQ-TAVRRMIVGGENLSTRLARSIHEQFEGrIEICNEYGPTETVVGCMIYRYDAAKDRRE 2082
Cdd:PRK12467  748 VTVLKIVPSHLQALLQASRVALpRPQRALVCGGEALQVDLLARVRALGPG-ARLINHYGPTETTVGVSTYELSDEERDFG 826
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2083 SVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEP-GAKMYKTGDLAKWLADGNI 2161
Cdd:PRK12467  827 NVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVI 906
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2162 EYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGfKQLCAYYV-----SGGQTTAAR--LRKQLSQTLA 2234
Cdd:PRK12467  907 EYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAG-LQLVAYLVpaavaDGAEHQATRdeLKAQLRQVLP 985
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2235 SYMVPAYFIELDEMPLTSNGKINKKGLPAPDfELQDRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKS 2314
Cdd:PRK12467  986 DYMVPAHLLLLDSLPLTPNGKLDRKALPKPD-ASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLA 1064
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2315 IQVSSRLNQQ-GYKMEIKDLFQYATIAElsphIKQNLRIADQGEVKG----------KVSLTPIQHWFFEQTTTDQHYYN 2383
Cdd:PRK12467 1065 TQVISRVRQRlGIQVPLRTLFEHQTLAG----FAQAVAAQQQGAQPAlpdvdrdqplPLSYAQERQWFLWQLEPGSAAYH 1140
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2384 --QAVMLHAPegFQETQLRQTLQKLAEHHDALRMTFRTTEngcEAQNEEIAQSGLYRLEVMNLKEDPDPGRTIEAKAD-E 2460
Cdd:PRK12467 1141 ipQALRLKGP--LDIEALERSFDALVARHESLRTTFVQED---GRTRQVIHPVGSLTLEEPLLLAADKDEAQLKVYVEaE 1215
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2461 IQSSMHLSDGPLMKAGLFQCADGDHLLI-AIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLP----QKTDsFQLWAKR 2535
Cdd:PRK12467 1216 ARQPFDLEQGPLLRVGLLRLAADEHVLVlTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPalpiQYAD-YAVWQRQ 1294
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2536 LSEYAQSEtikQEQEYWTKI---EQTeVKPLPKDFHETHTTAKDSETAAVEWTKEETElLLKQANRAYHTEINDLLLTSL 2612
Cdd:PRK12467 1295 WMDAGERA---RQLAYWKAQlggEQP-VLELPTDRPRPAVQSHRGARLAFELPPALAE-GLRALARREGVTLFMLLLASF 1369
                        1370
                  ....*....|...
gi 166797876 2613 GLSISHWSGLEQI 2625
Cdd:PRK12467 1370 QTLLHRYSGQDDI 1382
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3287-3784 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 764.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3287 ELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPD 3366
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3367 SPSERIRYILNDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHR 3446
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3447 QVIHLIEGLSRQVYSayDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAH 3526
Cdd:cd17655   161 GVVNLVEWANKVIYQ--GEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3527 LKLLIAAGDLQGVTLQHLLIGGEALSKTTVNKLKQLFGEhgaAPGITNVYGPTETCVDASLFNIECSSDawarSQNYVPI 3606
Cdd:cd17655   239 LKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGT---NPTITNAYGPTETTVDASIYQYEPETD----QQVSVPI 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3607 GKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGR 3686
Cdd:cd17655   312 GKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3687 IDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLD 3766
Cdd:cd17655   392 IDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLD 471
                         490
                  ....*....|....*...
gi 166797876 3767 KMPLTPNGKLNRQLLPAP 3784
Cdd:cd17655   472 EIPLTPNGKVDRKALPEP 489
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
4346-4819 0e+00

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 756.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGADVLLTCAGHAIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQ 4505
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4506 DHTQ-LRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEKHYFE 4584
Cdd:cd17656   162 EKTNiNFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFIN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4585 PFAECVDHIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTMYTVDP-DTDQELQPIGKPISNTEIFILNEAGTL 4663
Cdd:cd17656   242 RFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPeAEIPELPPIGKPISNTWIYILDQEQQL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4664 QPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVE 4743
Cdd:cd17656   322 QPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIE 401
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4744 AALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALP 4819
Cdd:cd17656   402 AQLLNHpgVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
PRK12316 PRK12316
peptide synthase; Provisional
2815-4171 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 734.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2815 LIQLPHAGEVENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWNDTPL 2894
Cdd:PRK12316   37 LFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2895 QIvyKTQTP-QIHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLI 2973
Cdd:PRK12316  117 QV--PLDRPlEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2974 TKEVFDHYSALQEGREPEpLSAVP--YSDYI----EWLDRQDQGAAKRYWSGYLegyKGETTLLHKIAQHEQ---KEYAY 3044
Cdd:PRK12316  195 IEEFSRFYSAYATGAEPG-LPALPiqYADYAlwqrSWLEAGEQERQLEYWRAQL---GEEHPVLELPTDHPRpavPSYRG 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3045 ANLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEipDVEQMIGLFINTIPVRIRC 3124
Cdd:PRK12316  271 SRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA--EVEGLIGFFVNTQVLRSVF 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3125 DEDSTFADTMQMVQQNALASQSYDTYPlYEIQAQTEQKQNLIDHIMIFE---NYP--IGQQAEETGHHGTELNITNFHMQ 3199
Cdd:PRK12316  349 DGRTRVATLLAGVKDTVLGAQAHQDLP-FERLVEALKVERSLSHSPLFQvmyNHQplVADIEALDTVAGLEFGQLEWKSR 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3200 EhSHYDLNV-VVIPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSRFQSNDMH 3278
Cdd:PRK12316  428 T-TQFDLTLdTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAE 506
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3279 YPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGG 3358
Cdd:PRK12316  507 YPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG 586
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3359 AYLPIDPDSPSERIRYILNDSSISVLLYCGKLQD----DIGFSGTCIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGT 3434
Cdd:PRK12316  587 AYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRklplAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGS 666
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3435 TGKPKGTLIEHRQVIHLIEgLSRQVYSaYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQ 3514
Cdd:PRK12316  667 TGKPKGAGNRHRALSNRLC-WMQQAYG-LGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINR 744
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3515 HSIDITDGTPAHLKLLIAAGDLQGVT-LQHLLIGGEALSKTTVnklKQLFGEHGAApGITNVYGPTETCVDASLFNieCS 3593
Cdd:PRK12316  745 EGVDTLHFVPSMLQAFLQDEDVASCTsLRRIVCSGEALPADAQ---EQVFAKLPQA-GLYNLYGPTEAAIDVTHWT--CV 818
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3594 SDAwARSqnyVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLA 3673
Cdd:PRK12316  819 EEG-GDS---VPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLA 894
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3674 RLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADdeyyLCGYFAADKT--IQISELRKRMAR 3751
Cdd:PRK12316  895 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQ----LVGYVVLESEggDWREALKAHLAA 970
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3752 HLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPvKKRDSGIEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHFFEIGGHS 3831
Cdd:PRK12316  971 SLPEYMVPAQWLALERLPLTPNGKLDRKALPAP-EASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDS 1049
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3832 LRATALIAKiQKQMHVQIPLRDVFRFPTIEQLARTITKTELTGYAAIPAIEKRPYYPVssaQKRLYIL-----NHlegge 3906
Cdd:PRK12316 1050 IVSIQVVSR-ARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPV---QRWFFEQaipqrQH----- 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3907 lsYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEWYQGEEDDADL--YIRQFIRPF 3984
Cdd:PRK12316 1121 --WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELlaLCEEAQRSL 1198
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3985 HLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGET--LPPLRIQYKDYAVWQTGEArlQQIQKQ 4062
Cdd:PRK12316 1199 DLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDadLPARTSSYQAWARRLHEHA--GARAEE 1276
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4063 EAYWLElYSGDVPVlHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQTEST-LYMVLLASYTLLLSKYSGQEDII 4141
Cdd:PRK12316 1277 LDYWQA-QLEDAPH-ELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTqVNDLLLTALARVTCRWSGQASVL 1354
                        1370      1380      1390
                  ....*....|....*....|....*....|....
gi 166797876 4142 VGSPIAGRPH----ADLEPIIGMFVNTLAMRNYP 4171
Cdd:PRK12316 1355 VQLEGHGREDlfedIDLSRTVGWFTSLFPVRLTP 1388
PRK12316 PRK12316
peptide synthase; Provisional
3878-4907 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 706.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3878 IPAIEKRPYYPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGkLDRDKLQQAFRTLILRHESLRTGF--KMADGEPVQYV 3955
Cdd:PRK12316 4094 LPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvwQGELGRPLQVV 4172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3956 LDHAAF---EAEWYQGEEDDADL---YIRQFIRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIR 4029
Cdd:PRK12316 4173 HKQVSLpfaELDWRGRADLQAALdalAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLE 4252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4030 IYEGETLPPLRIQYKDYAVWqtgeARLQQIQKQEAYWLE-LYSGDVPVlHLPADYIRPSARDFAGATMHF-TLDKQKSDG 4107
Cdd:PRK12316 4253 RYSGRPPAQPGGRYRDYIAW----LQRQDAAASEAFWREqLAALDEPT-RLAQAIARADLRSANGYGEHVrELDATATAR 4327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4108 LKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPhADL---EPIIGMFVNTLAMRNYPEKGKTFSQYLSEV 4184
Cdd:PRK12316 4328 LREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRP-AELpgiEGQIGLFINTLPVIATPRAQQSVVEWLQQV 4406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4185 KENALKAYEHQDYPFEvlidQLNIARDLSRNPLFDTMFVLQNTE----QEQLEINDVTFKPYPNgHTMAKFDLTLtAVEE 4260
Cdd:PRK12316 4407 QRQNLALREHEHTPLY----EIQRWAGQGGEALFDSLLVFENYPvseaLQQGAPGGLRFGEVTN-HEQTNYPLTL-AVGL 4480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4261 GAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDIQQLFNDTavaEKRIPTT--IHQLF 4338
Cdd:PRK12316 4481 GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRT---DAGYPATrcVHQLV 4557
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4339 EQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPE 4418
Cdd:PRK12316 4558 AERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPR 4637
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4419 KRRAFMLKDSGADVLLTcAGHAIP--PLFEG-EVLLLDDPLLYQGRTDN--LNLSCSENdLMYVIYTSGTTGQPKGVQLE 4493
Cdd:PRK12316 4638 ERLAYMMEDSGAALLLT-QSHLLQrlPIPDGlASLALDRDEDWEGFPAHdpAVRLHPDN-LAYVIYTSGSTGRPKGVAVS 4715
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4494 HKTMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAkRDIRQLNDFVRTHGIQTAFLPTAF 4572
Cdd:PRK12316 4716 HGSLVNHLHATGERYELTPdDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVY 4794
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4573 LKLLASEkhyFEPFAEC--VDHIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTMYTVDPDTDQELQ---PIGK 4647
Cdd:PRK12316 4795 LQQLAEH---AERDGEPpsLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAaymPIGT 4871
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4648 PISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSN-QRMYKTGDLARYLPEGNIEYAGRR 4726
Cdd:PRK12316 4872 PLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPgGRLYRTGDLARYRADGVIDYLGRV 4951
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4727 DHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSdLYAYF----------TAEQSLSISQLKEKLAGQIPGYM 4794
Cdd:PRK12316 4952 DHQVKIRGFRIELGEIEARLREHpaVREAVVIAQEGAVGKQ-LVGYVvpqdpaladaDEAQAELRDELKAALRERLPEYM 5030
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4795 IPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQTGTdYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTL 4874
Cdd:PRK12316 5031 VPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQA-YVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
                        1050      1060      1070
                  ....*....|....*....|....*....|...
gi 166797876 4875 IAKIHKQFSKNISLREVFQCPTVGEMAQAIAEA 4907
Cdd:PRK12316 5110 TSRIQLELGLELPLRELFQTPTLAAFVELAAAA 5142
PRK12467 PRK12467
peptide synthase; Provisional
3887-5092 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 687.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGkLDRDKLQQAFRTLILRHESLRTGFKMADG--EPVQYVLDHAAF--- 3961
Cdd:PRK12467 2647 YPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGEleEPLQVVYKQARLpfs 2725
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3962 EAEW---YQGEEDDADLYIRQFIRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGETLPP 4038
Cdd:PRK12467 2726 RLDWrdrADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQPPPA 2805
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4039 LRIQYKDYAVWqtgeARLQQIQKQEAYWLE-LYSGDVPVLHLPADYIRPsARDFAGATMHF-TLDKQKSDGLKQLASQTE 4116
Cdd:PRK12467 2806 REGRYRDYIAW----LQAQDAEASEAFWKEqLAALEEPTRLARALYPAP-AEAVAGHGAHYlHLDATQTRQLIEFARRHR 2880
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4117 STLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPhADL---EPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYE 4193
Cdd:PRK12467 2881 VTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRP-AQLrgaEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALRE 2959
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4194 HQDYPfevLIDqlnIAR--DLSRNPLFDTMFV---------LQNTEQEQLEINDVTfkpypnGHTMAKFDLTLtAVEEGA 4262
Cdd:PRK12467 2960 FEHTP---LAD---IQRwaGQGGEALFDSILVfenypiseaLKQGAPSGLRFGAVS------SREQTNYPLTL-AVGLGD 3026
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4263 GIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDIQQLFNDTAvAEKRIPTTIHQLFEQQA 4342
Cdd:PRK12467 3027 TLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATA-AAYPSERLVHQLIEAQV 3105
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4343 ERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRA 4422
Cdd:PRK12467 3106 ARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLA 3185
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4423 FMLKDSGADVLLTCAG--HAIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNL 4500
Cdd:PRK12467 3186 YMIEDSGVKLLLTQAHllEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANH 3265
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4501 L-AYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAkRDIRQLNDFVRTHGIQTAFLPTAFLKLLASe 4579
Cdd:PRK12467 3266 LcWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAE- 3343
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4580 khyFEPFAEC--VDHIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHV-VTMYTVDPDTDQELQ--PIGKPISNTEI 4654
Cdd:PRK12467 3344 ---DAGGADCasLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVtVTLWKCGGDAVCEAPyaPIGRPVAGRSI 3420
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4655 FILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSN-QRMYKTGDLARYLPEGNIEYAGRRDHQVKIR 4733
Cdd:PRK12467 3421 YVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSgGRLYRTGDLARYRADGVIEYLGRIDHQVKIR 3500
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4734 GYRVELGEVEAALLKH--VQEAVVLAKENTDGQSdLYAYFT--AEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTG 4809
Cdd:PRK12467 3501 GFRIELGEIEARLLQHpsVREAVVLARDGAGGKQ-LVAYVVpaDPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGP 3579
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4810 NGKVNRRALPMPEAGLQtgTDYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLR 4889
Cdd:PRK12467 3580 NGKVDRKALPDPDAKGS--REYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLR 3657
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4890 EVFQCPTVGEMAqaiaeaetngpDYIPkakakdvypvssvqkmvylttqiiGGELPYNMTgiletegkLPLNRLLTAFQR 4969
Cdd:PRK12467 3658 DLMSAPTIAELA-----------GYSP------------------------LGDVPVNLL--------LDLNRLETGFPA 3694
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4970 LMQGHEPLRTVVEmvrEEAVQVIksqvefsmeryeatadeveecfrafvrpfdlsqapllraglieLEQDLHIFMFDMHH 5049
Cdd:PRK12467 3695 LFCRHEGLGTVFD---YEPLAVI-------------------------------------------LEGDRHVLGLTCRH 3728
                        1210      1220      1230      1240
                  ....*....|....*....|....*....|....*....|...
gi 166797876 5050 IITDGASMnifvekliqlydgKELAPLRIQYKDFTEWKHQKEQ 5092
Cdd:PRK12467 3729 LLDDGWQD-------------TSLQAMAVQYADYILWQQAKGP 3758
PRK12467 PRK12467
peptide synthase; Provisional
7-1343 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 666.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    7 QETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDR 86
Cdd:PRK12467  239 QLAYWQEQLGGEHTVLELP----TDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQ 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   87 TSLILGIPTVSKQKAGQSA-----VNNIVLlKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMP 161
Cdd:PRK12467  315 SDIRIGVPNANRNRVETERligffVNTQVL-KAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSP 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  162 LIHtvVSLNEIHSLQCKEDTATDTL--------------FHFDLE------NNGIHLKLFYNGNLYDERYINQIVSHLDQ 221
Cdd:PRK12467  394 LFQ--VMFNHQNTATGGRDREGAQLpgltveelswarhtAQFDLAldtyesAQGLWAAFTYATDLFEATTIERLATHWRN 471
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  222 LLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDTVRDFSGsRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRL 301
Cdd:PRK12467  472 LLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAP-DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRL 550
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  302 ARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSL--AFDGP 379
Cdd:PRK12467  551 AHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLpvPAGLR 630
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  380 VIDLNDEASYHADCSLLSP-VA-GHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDA 457
Cdd:PRK12467  631 SLCLDEPADLLCGYSGHNPeVAlDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDL 710
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  458 FILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEK 537
Cdd:PRK12467  711 GVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLAR 790
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  538 LHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQIT---IGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLN 614
Cdd:PRK12467  791 VRALGPGARLINHYGPTETTVGVSTYELSDEERDFGnvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHR 870
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  615 RPELTEEKFV-EHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVArEDAD 693
Cdd:PRK12467  871 RPALTAERFVpDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGD 949
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  694 GAKQLYAYYV-------GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADENTRaENEYIAPR 766
Cdd:PRK12467  950 AGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAV-QATFVAPQ 1028
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  767 NTIEELLASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQA-GYKVDMKHLFKHPSIAELSQFVAPVSRVAdQGE 845
Cdd:PRK12467 1029 TELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGA-QPA 1107
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  846 VNGGTKLTPIQ-------HWFFEQKMPH--AHHYNQAVMLYSAegFKEGPLRRTMERIASHHDALRMIFEKTpDGYAPRI 916
Cdd:PRK12467 1108 LPDVDRDQPLPlsyaqerQWFLWQLEPGsaAYHIPQALRLKGP--LDIEALERSFDALVARHESLRTTFVQE-DGRTRQV 1184
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  917 TGTDESELFHLEVMNYKGEtDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDHLLI-AIHHLLIDGVSWRILLEDF 995
Cdd:PRK12467 1185 IHPVGSLTLEEPLLLAADK-DEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVlTLHHIVSDGWSMQVLVDEL 1263
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  996 ASGYEQAERRQTIQLP----QKTDsFPFWADQlskYAAETDMEEEIAYWT-ELSSIKP-------QPLPKDTISEGSLLR 1063
Cdd:PRK12467 1264 VALYAAYSQGQSLQLPalpiQYAD-YAVWQRQ---WMDAGERARQLAYWKaQLGGEQPvlelptdRPRPAVQSHRGARLA 1339
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1064 dseeVTIQwtkEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREpiipDADISRTIGWFTSQYp 1143
Cdd:PRK12467 1340 ----FELP---PALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRN----RAETEGLIGFFVNTQ- 1407
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1144 vVLRMEAGKNLSqrikiVKEGLRRIPDKGMNYSIIKYISGHPEADSLQLKPEISFNYLGQ--FD-QDLKHQALRISPfst 1220
Cdd:PRK12467 1408 -VLRAEVDGQAS-----FQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQvmFNhQRDDHQAQAQLP--- 1478
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1221 GLSMN--ENQERTAVLDLNGMIAEGT--LSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHCVSR--QQTSLTPSdill 1294
Cdd:PRK12467 1479 GLSVEslSWESQTAQFDLTLDTYESSegLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRlgELDLLDEA---- 1554
                        1370      1380      1390      1400
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876 1295 kdisidELEQLLEQTRELGEAeniYPLtpmqkGMLFHSLFDPNSGAYFQ 1343
Cdd:PRK12467 1555 ------ERRQILEGWNATHTG---YPL-----ARLVHQLIEDQAAATPE 1589
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
267-753 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 661.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  267 QLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPE 346
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  347 YPKERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHG 426
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  427 GIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLK 506
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  507 tMIEQMNREDFIHVQHVVVGGEQLETDTVEKL-HSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ---ITIGSPVANHQ 582
Cdd:cd17655   241 -LLDAADDSEGLSLKHLIVGGEALSTELAKKIiELFGTNPTITNAYGPTETTVDASIYQYEPETDQqvsVPIGKPLGNTR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  583 AYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIR 662
Cdd:cd17655   320 IYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  663 GYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNG 742
Cdd:cd17655   400 GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNG 479
                         490
                  ....*....|.
gi 166797876  743 KIDLKALPAAD 753
Cdd:cd17655   480 KVDRKALPEPD 490
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
277-749 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 653.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQHhlknslafdgpvidlndeasyhadcsllspvaghSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKK 436
Cdd:cd05930    81 EDSGAKLVLTDP----------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  437 AFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNRED 516
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  517 FIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSAD---EQITIGSPVANHQAYILGAHHQIQ 593
Cdd:cd05930   207 LPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRVYVLDENLRPV 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  594 PIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEA 673
Cdd:cd05930   287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876  674 AMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05930   367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
PRK05691 PRK05691
peptide synthase; Validated
1320-2566 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 642.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRgwKD-QPLQIIFKTKKIGFQF 1398
Cdd:PRK05691  677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYE--RDgVALQRIDAQGEFALQR 754
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1399 NDLREMKESQKEAMIQKyAREDKMRG-FDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEiFENYFALLQ 1477
Cdd:PRK05691  755 IDLSDLPEAEREARAAQ-IREEEARQpFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDE-FSRLYAAAC 832
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPEQSSITP--YSQYI----EWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMK 1551
Cdd:PRK05691  833 QGQTAELAPLPlgYADYGawqrQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALR 912
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1552 RTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQER 1631
Cdd:PRK05691  913 GLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQA 990
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1632 AVASQKfethplydiqarttqKQDLithlmifenyPVDQYMESIG--RQNGTSITISNVQMEEQTNydfnLTVIPG---D 1706
Cdd:PRK05691  991 TLGAQA---------------HQDL----------PFEQLVEALPqaREQGLFQVMFNHQQRDLSA----LRRLPGllaE 1041
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1707 EM-----------------------NISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLLQT 1763
Cdd:PRK05691 1042 ELpwhsreakfdlqlhseedrngrlTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQW 1121
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1764 LNDTAAPFPQTPVHQLfEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILA 1843
Cdd:PRK05691 1122 GQAPCAPAQAWLPELL-NEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLA 1200
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1844 VLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQL-AYEGVTVLLDDesSYHQDG-SDLAPISDVS--HLAYV 1919
Cdd:PRK05691 1201 ILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLpQAEGVSAIALD--SLHLDSwPSQAPGLHLHgdNLAYV 1278
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1920 IYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTG-NAIIVYDGE--DKTALLE 1996
Cdd:PRK05691 1279 IYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGcRLVLAGPGEhrDPQRIAE 1358
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1997 sIVRDPRVDIIKLTPAHLQV-LKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGrIEICNEYGPTETVVGCMIYRYD 2075
Cdd:PRK05691 1359 -LVQQYGVTTLHFVPPLLQLfIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQ-VQLHNRYGPTETAINVTHWQCQ 1436
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2076 AAKDRResVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAK 2154
Cdd:PRK05691 1437 AEDGER--SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRAR 1514
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2155 WLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGfKQLCAYYVSGGQ--TTAARLRKQLSQT 2232
Cdd:PRK05691 1515 WNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTGEAGqeAEAERLKAALAAE 1593
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2233 LASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFElqdRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSI 2312
Cdd:PRK05691 1594 LPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ---QREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSL 1670
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2313 KSIQVSSRLNQQ-GYKMEIKDLFQYatiAELSPHIKQNLRIADQGEVKGKVSLT--------PIQH-----WFFEQTTTD 2378
Cdd:PRK05691 1671 LATQIVSRTRQAcDVELPLRALFEA---SELGAFAEQVARIQAAGERNSQGAIArvdrsqpvPLSYsqqrmWFLWQMEPD 1747
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2379 QHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTeNGCEAQNEEiAQSGLyRLEVMNLKEDPDPGRT--IEA 2456
Cdd:PRK05691 1748 SPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSV-DGVPVQQVA-EDSGL-RMDWQDFSALPADARQqrLQQ 1824
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2457 KAD-EIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGR---VIQLPQKTDSFQL 2531
Cdd:PRK05691 1825 LADsEAHQPFDLERGPLLRACLVKAAEREHyFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRespLEPLPVQYLDYSV 1904
                        1290      1300      1310
                  ....*....|....*....|....*....|....*...
gi 166797876 2532 WAKRLSEYAQsetiKQEQ-EYWTKIEQTE--VKPLPKD 2566
Cdd:PRK05691 1905 WQRQWLESGE----RQRQlDYWKAQLGNEhpLLELPAD 1938
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2827-3250 0e+00

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 634.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2827 VYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWNDTPLQIVYKTQTPQIH 2906
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2907 FADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQE 2986
Cdd:cd19543    81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2987 GREPEPLSAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKGETTLLHKIAQHEQKEYAYANLICRFDHEQTKQLQQIANQH 3066
Cdd:cd19543   161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3067 QVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQNALASQS 3146
Cdd:cd19543   241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3147 YDTYPLYEIQAQTEQKQNLIDHIMIFENYPIGQQAEEtGHHGTELNITNFHMQEHSHYDLNVVVIPGKQLAVHFGFNENE 3226
Cdd:cd19543   321 HEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEE-EQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAEV 399
                         410       420
                  ....*....|....*....|....
gi 166797876 3227 YEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19543   400 FDEATIERLLGHLRRVLEQVAANP 423
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1788-2261 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 622.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDvrkqlayegvtvllddessyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAK 1947
Cdd:cd05930    81 EDSGAKLVLTDPD----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1948 EVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKT--ALLESIVRDPRVDIIKLTPAHLQVL-KEMNIAD 2024
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLLRLLlQELELAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2025 QTAVRRMIVGGENLSTRLARSIHEQFEgRIEICNEYGPTETVVGCMIYRYDAAKDRRESVPIGTAAANTSIYVLDENMKP 2104
Cdd:cd05930   207 LPSLRLVLVGGEALPPDLVRRWRELLP-GARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRP 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2105 APIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIE 2184
Cdd:cd05930   286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 2185 AALLQEEVIKEAVVTAREDVHGFKQLCAYYVS--GGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05930   366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPdeGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1318-1741 0e+00

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 615.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1318 IYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPLQIIFKTKKIGFQ 1397
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1398 FNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQ 1477
Cdd:cd19543    81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPEQSSITPYSQYIEWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKRTAGKH 1557
Cdd:cd19543   161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1558 HVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERAVASQK 1637
Cdd:cd19543   241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1638 FETHPLYDIQARTTQKQDLITHLMIFENYPVDQYMESIGRQNGtsITISNVQMEEQTNYDFNLTVIPGDEMNISFEYNAN 1717
Cdd:cd19543   321 HEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEEEQDEDG--LRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAE 398
                         410       420
                  ....*....|....*....|....
gi 166797876 1718 VYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19543   399 VFDEATIERLLGHLRRVLEQVAAN 422
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
267-749 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 591.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  267 QLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPE 346
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  347 YPKERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLnDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHG 426
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVI-DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  427 GIVnSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERIT-HFSTSPrlL 505
Cdd:cd12117   160 GVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTvLWLTAA--L 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  506 KTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQ---SADEQITIGSPVANHQ 582
Cdd:cd12117   237 FNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTeldEVAGSIPIGRPIANTR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  583 AYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIR 662
Cdd:cd12117   317 VYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  663 GYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNG 742
Cdd:cd12117   397 GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANG 476

                  ....*..
gi 166797876  743 KIDLKAL 749
Cdd:cd12117   477 KVDRRAL 483
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
4336-4822 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 589.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4336 QLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPE 4415
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4416 LPEKRRAFMLKDSGADVLLTcAGHAIPPL-FEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEH 4494
Cdd:cd17655    81 YPEERIQYILEDSGADILLT-QSHLQPPIaFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4495 KTMTNL-LAYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFL 4573
Cdd:cd17655   160 RGVVNLvEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4574 KLLASEKHYFEPfaeCVDHIIAAGEQL---IATRMLRdmLARHQVTLHNHYGPSETHV-VTMYTVDPDTD-QELQPIGKP 4648
Cdd:cd17655   240 KLLDAADDSEGL---SLKHLIVGGEALsteLAKKIIE--LFGTNPTITNAYGPTETTVdASIYQYEPETDqQVSVPIGKP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4649 ISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDH 4728
Cdd:cd17655   315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDH 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4729 QVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLP 4806
Cdd:cd17655   395 QVKIRGYRIELGEIEARLLQHpdIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIP 474
                         490
                  ....*....|....*.
gi 166797876 4807 LTGNGKVNRRALPMPE 4822
Cdd:cd17655   475 LTPNGKVDRKALPEPD 490
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
3297-3781 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 587.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLS 3456
Cdd:cd05930    81 EDSGAKLVLT----------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RQVYsaYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDL 3536
Cdd:cd05930   127 EAYP--LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3537 QGVT-LQHLLIGGEALSKTTVNKLKQLFGEHGaapgITNVYGPTETCVDASLFniECSSDAwaRSQNYVPIGKPLGRNRM 3615
Cdd:cd05930   205 AALPsLRLVLVGGEALPPDLVRRWRELLPGAR----LVNLYGPTEATVDATYY--RVPPDD--EEDGRVPIGRPIPNTRV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3616 YILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQG 3695
Cdd:cd05930   277 YVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3696 FRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADK--TIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPN 3773
Cdd:cd05930   357 YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436

                  ....*...
gi 166797876 3774 GKLNRQLL 3781
Cdd:cd05930   437 GKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
4346-4818 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 572.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGADVLLTCAghaipplfegevlllddpllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQ 4505
Cdd:cd05930    81 EDSGAKLVLTDP----------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4506 DHTQLRF-DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASekHYFE 4584
Cdd:cd05930   127 EAYPLTPgDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ--ELEL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4585 PFAECVDHIIAAGEQLIAT--RMLRDMLarHQVTLHNHYGPSETHV-VTMYTVDPDTDQELQ-PIGKPISNTEIFILNEA 4660
Cdd:cd05930   205 AALPSLRLVLVGGEALPPDlvRRWRELL--PGARLVNLYGPTEATVdATYYRVPPDDEEDGRvPIGRPIPNTRVYVLDEN 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4661 GTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELG 4740
Cdd:cd05930   283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4741 EVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQ--SLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRR 4816
Cdd:cd05930   363 EIEAALLAHpgVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442

                  ..
gi 166797876 4817 AL 4818
Cdd:cd05930   443 AL 444
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2362-2788 0e+00

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 563.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2362 VSLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQNEEIAQsGLYRLEV 2441
Cdd:cd19534     2 VPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVE-ELFRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2442 MNLKEDPDPgRTIEAKADEIQSSMHLSDGPLMKAGLFQ-CADGDHLLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVI 2520
Cdd:cd19534    81 VDLSSLAQA-AAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2521 QLPQKTdSFQLWAKRLSEYAQSETIKQEQEYWTKIEQTEVKPLPKDFHETHttaKDSETAAVEWTKEETELLLKQANRAY 2600
Cdd:cd19534   160 PLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTY---GDARTVSFTLDEEETEALLQEANAAY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2601 HTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDISRTVGWFTSLYPVVLHAQPGKEISDYIKTTKEGLRQI 2680
Cdd:cd19534   236 RTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLRRI 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2681 PHKGIGYGIARYLSGGMPSKLN----PEISFNYLGQFDQDLQRHGVQLSSYSCGSDSSGHQ-ERPYVLNINGMITDGRLK 2755
Cdd:cd19534   316 PNKGIGYGILRYLTPEGTKRLAfhpqPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDtPRFALLDINAVVEGGQLV 395
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 2756 LTISYSSKQYAKETIMRLSETIQSRLRTIITHC 2788
Cdd:cd19534   396 ITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
3886-4298 4.23e-180

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 560.82  E-value: 4.23e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3886 YYPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEW 3965
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3966 -----YQGEEDDADL--YIRQFI-RPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGET-- 4035
Cdd:cd19531    81 vdlsgLPEAEREAEAqrLAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4036 ----LPPLRIQYKDYAVWQtgEARLQQ--IQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLK 4109
Cdd:cd19531   161 rpspLPPLPIQYADYAVWQ--REWLQGevLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4110 QLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENAL 4189
Cdd:cd19531   239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4190 KAYEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTLE 4269
Cdd:cd19531   319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLE 398
                         410       420
                  ....*....|....*....|....*....
gi 166797876 4270 YLTALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19531   399 YNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1778-2261 1.98e-179

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 561.44  E-value: 1.98e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDSQAGIVLMQRDVRKQLAyEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHG 1937
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAG-GLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1938 GL------TNYIwwakevyVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIVRDpRVDIIK 2008
Cdd:cd12117   160 GVvrlvknTNYV-------TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGtllDPDALGALIAEE-GVTVLW 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2009 LTPAHLQVLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQfEGRIEICNEYGPTETVVGCMIYRYDAAKDRRESVPIGT 2088
Cdd:cd12117   232 LTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAA-CPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2089 AAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRID 2168
Cdd:cd12117   311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRID 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2169 EQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEM 2248
Cdd:cd12117   391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDEL 470
                         490
                  ....*....|...
gi 166797876 2249 PLTSNGKINKKGL 2261
Cdd:cd12117   471 PLTANGKVDRRAL 483
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
852-1279 7.44e-176

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 548.78  E-value: 7.44e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  852 LTPIQHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGtDESELFHLEVMN 931
Cdd:cd19534     4 LTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRG-DVEELFRLEVVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  932 YKGEtDPAQAIADKANEIQSSMVLDKGPLMKLGLFQ-CPDGDHLLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQL 1010
Cdd:cd19534    83 LSSL-AQAAAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1011 PQKTdSFPFWADQLSKYAAETDMEEEIAYWTELSSIKPQPLPKDTISEGsllRDSEEVTIQWTKEETEQLLKQANRAYNT 1090
Cdd:cd19534   162 PSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTY---GDARTVSFTLDEEETEALLQEANAAYRT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1091 DINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPDADISRTIGWFTSQYPVVLRMEAGKNLSQRIKIVKEGLRRIPD 1170
Cdd:cd19534   238 EINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLRRIPN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1171 KGMNYSIIKYISGHPEADSLQL-KPEISFNYLGQFDQDLKHQALRISPFS-TGLSMNENQERTAVLDLNGMIAEGTLSLT 1248
Cdd:cd19534   318 KGIGYGILRYLTPEGTKRLAFHpQPEISFNYLGQFDQGERDDALFVSAVGgGGSDIGPDTPRFALLDINAVVEGGQLVIT 397
                         410       420       430
                  ....*....|....*....|....*....|.
gi 166797876 1249 LSYSSKQYERSTMAQFARGLKESLQEVIAHC 1279
Cdd:cd19534   398 VSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
4338-4819 1.69e-173

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 544.63  E-value: 1.69e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4338 FEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELP 4417
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4418 EKRRAFMLKDSGADVLLTCAGHAipPLFEGE---VLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEH 4494
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALA--GELAVElvaVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4495 KTMTNLLAYeqdhtQLRF------DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFL 4568
Cdd:cd17651   159 RSLANLVAW-----QARAsslgpgARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4569 PTAFLKLLASE--KHYFEPFAecVDHIIAAGEQLIATRMLRDMLARHQ-VTLHNHYGPSETHVVTMYTVDPDTDQ--ELQ 4643
Cdd:cd17651   234 PTVALRALAEHgrPLGVRLAA--LRYLLTGGEQLVLTEDLREFCAGLPgLRLHNHYGPTETHVVTALSLPGDPAAwpAPP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4644 PIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYA 4723
Cdd:cd17651   312 PIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4724 GRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQ--SLSISQLKEKLAGQIPGYMIPSYF 4799
Cdd:cd17651   392 GRADDQVKIRGFRIELGEIEAALARHpgVREAVVLAREDRPGEKRLVAYVVGDPeaPVDAAELRAALATHLPEYMVPSAF 471
                         490       500
                  ....*....|....*....|
gi 166797876 4800 IQLEKLPLTGNGKVNRRALP 4819
Cdd:cd17651   472 VLLDALPLTPNGKLDRRALP 491
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
3287-3781 4.38e-172

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 540.25  E-value: 4.38e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3287 ELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPD 3366
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3367 SPSERIRYILNDSSISVLLYCGKLQDDIGFSGTCIDLmEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHR 3446
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVI-DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3447 QVIHLIEGLSrqvYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTpAH 3526
Cdd:cd12117   160 GVVRLVKNTN---YVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT-AA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3527 LKLLIAAGDLQGV-TLQHLLIGGEALSKTTVNKLKQlfgehgAAPG--ITNVYGPTETCVdaslFNIECSSDAWARSQNY 3603
Cdd:cd12117   236 LFNQLADEDPECFaGLRELLTGGEVVSPPHVRRVLA------ACPGlrLVNGYGPTENTT----FTTSHVVTELDEVAGS 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3604 VPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEY 3683
Cdd:cd12117   306 IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3684 IGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFV 3763
Cdd:cd12117   386 LGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFV 465
                         490
                  ....*....|....*...
gi 166797876 3764 QLDKMPLTPNGKLNRQLL 3781
Cdd:cd12117   466 VLDELPLTANGKVDRRAL 483
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
268-749 1.38e-171

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 539.17  E-value: 1.38e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  268 LFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEY 347
Cdd:cd17646     3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  348 PKERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGG 427
Cdd:cd17646    83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  428 IVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERIT--HFstSPRLL 505
Cdd:cd17646   163 IVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTtcHF--VPSML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  506 KTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLqPRIRINNEYGPTENSVVSTFHPVQSADEQIT--IGSPVANHQA 583
Cdd:cd17646   241 RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPNTRL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  584 YILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRG 663
Cdd:cd17646   320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  664 YRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV---GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTS 740
Cdd:cd17646   400 FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTA 479

                  ....*....
gi 166797876  741 NGKIDLKAL 749
Cdd:cd17646   480 NGKLDRAAL 488
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
4336-4818 2.98e-171

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 537.94  E-value: 2.98e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4336 QLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPE 4415
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4416 LPEKRRAFMLKDSGADVLLTCAGHAiPPLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHK 4495
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLA-GRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4496 TMTNLlAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLK 4574
Cdd:cd12117   160 GVVRL-VKNTNYVTLGPdDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4575 LLASEKhyfepfAEC---VDHIIAAGEQLIAtRMLRDMLARH-QVTLHNHYGPSETHVV-TMYTVDPDTDQELQ-PIGKP 4648
Cdd:cd12117   239 QLADED------PECfagLRELLTGGEVVSP-PHVRRVLAACpGLRLVNGYGPTENTTFtTSHVVTELDEVAGSiPIGRP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4649 ISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDH 4728
Cdd:cd12117   312 IANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDD 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4729 QVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLP 4806
Cdd:cd12117   392 QVKIRGFRIELGEIEAALRAHpgVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELP 471
                         490
                  ....*....|..
gi 166797876 4807 LTGNGKVNRRAL 4818
Cdd:cd12117   472 LTANGKVDRRAL 483
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1801-2198 1.74e-170

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 532.23  E-value: 1.74e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1801 TYGELNKRANRLARTLRA-KGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQR 1879
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1880 DVRKQLAYEGVTVLLDD--ESSYHQDGSDLAPISDVS---HLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGE 1954
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDplELAALDDAPAPPPPDAPSgpdDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1955 KANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIVRDPRVDIIKLTPAHLQVLKEMNIADQTAVRRM 2031
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeerDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2032 IVGGENLSTRLARSIHEQFeGRIEICNEYGPTETVVGCMIYRYDAAKDRRES-VPIGTAAANTSIYVLDENMKPAPIGVP 2110
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARG-PGARLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVLDDDLRPVPVGVV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2111 GEIYISGAGVARGYLNRPELTAEKFVDDPF--EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALL 2188
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
                          410
                   ....*....|
gi 166797876  2189 QEEVIKEAVV 2198
Cdd:TIGR01733  400 RHPGVREAVV 409
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1320-2343 3.84e-169

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 561.97  E-value: 3.84e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKKIG-FQF 1398
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQWVDPALTFPlPEI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1399 NDLREMKESQKEAMIQKYAreDKMRGFDLEKG---ALMRLFILRTDektyRFIW--SFHHILMDGWCLPLITKEIFENYF 1473
Cdd:PRK10252   88 IDLRTQPDPHAAAQALMQA--DLQQDLRVDSGkplVFHQLIQLGDN----RWYWyqRYHHLLVDGFSFPAITRRIAAIYC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1474 ALLQQKQPEQSSITPYSQYIEWLGRQDAKEA----AAYWDQYLEGYEEQTGL---PKDHHAAEDgRYVPEKVTCDiSSDL 1546
Cdd:PRK10252  162 AWLRGEPTPASPFTPFADVVEEYQRYRASEAwqrdAAFWAEQRRQLPPPASLspaPLPGRSASA-DILRLKLEFT-DGAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1547 TSKMKRTAGKHHVTLNTLLQTAWavlLQKYNRSRDVVFGSVVSGRpAGIPNVeTMIGLFINTIPVRFRCEAGTTFAELMK 1626
Cdd:PRK10252  240 RQLAAQASGVQRPDLALALVALW---LGRLCGRMDYAAGFIFMRR-LGSAAL-TATGPVLNVLPLRVHIAAQETLPELAT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1627 eaqerAVASQ--KFETHPLYDIQ------ARTTQKQDL---ITHLMIFEnYPVDqymesIGRQNGTSITISNVQMEeqtn 1695
Cdd:PRK10252  315 -----RLAAQlkKMRRHQRYDAEqivrdsGRAAGDEPLfgpVLNIKVFD-YQLD-----FPGVQAQTHTLATGPVN---- 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1696 yDFNLTVIPGDEMNISFEYNANVyERASIERVREHFMQILH---QVVTDADIRVDQAELLTEGERRtLLQTLNDTAAPFP 1772
Cdd:PRK10252  380 -DLELALFPDEHGGLSIEILANP-QRYDEATLIAHAERLKAliaQFAADPALLCGDVDILLPGEYA-QLAQVNATAVEIP 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1773 QTPVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYV 1852
Cdd:PRK10252  457 ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1853 PIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLA-YEGVTVLLDDESSYHQDGSDLAPiSDVSHLAYVIYTSGSTGRPKG 1931
Cdd:PRK10252  537 PLDTGYPDDRLKMMLEDARPSLLITTADQLPRFAdVPDLTSLCYNAPLAPQGAAPLQL-SQPHHTAYIIFTSGSTGRPKG 615
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1932 VLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIvRDPRVDIIK 2008
Cdd:PRK10252  616 VMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEahrDPLAMQQFF-AEYGVTTTH 694
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2009 LTPAHLQVL-----KEMNIADQTAVRRMIVGGENLSTRLARsiheQFEGRI--EICNEYGPTETVVGCMIY---RYDAAK 2078
Cdd:PRK10252  695 FVPSMLAAFvasltPEGARQSCASLRQVFCSGEALPADLCR----EWQQLTgaPLHNLYGPTEAAVDVSWYpafGEELAA 770
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2079 DRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLAD 2158
Cdd:PRK10252  771 VRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDD 850
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2159 GNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVH------GFKQLCAYYVS--GGQTTAARLRKQLS 2230
Cdd:PRK10252  851 GAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQaaatggDARQLVGYLVSqsGLPLDTSALQAQLR 930
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2231 QTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPdfELQDRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGD 2310
Cdd:PRK10252  931 ERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLP--ELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGH 1008
                        1050      1060      1070
                  ....*....|....*....|....*....|....
gi 166797876 2311 SIKSIQVSSRLNQQ-GYKMEIKDLFQYATIAELS 2343
Cdd:PRK10252 1009 SLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLA 1042
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
269-750 4.57e-169

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 531.92  E-value: 4.57e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  269 FEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYP 348
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  349 KERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGH-SHLAYVIYTSGTTGKPKGVMVEHGG 427
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDaDDLAYVIYTSGSTGRPKGVVMPHRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  428 IVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKT 507
Cdd:cd17651   161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  508 MIEQMNREDFIH--VQHVVVGGEQLE-TDTVEKLHSLQPRIRINNEYGPTENSVVSTF---HPVQSADEQITIGSPVANH 581
Cdd:cd17651   241 LAEHGRPLGVRLaaLRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVVTALslpGDPAAWPAPPPIGRPIDNT 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  582 QAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKI 661
Cdd:cd17651   321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLT 739
Cdd:cd17651   401 RGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPeaPVDAAELRAALATHLPEYMVPSAFVLLDALPLT 480
                         490
                  ....*....|.
gi 166797876  740 SNGKIDLKALP 750
Cdd:cd17651   481 PNGKLDRRALP 491
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1777-2261 1.08e-168

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 530.70  E-value: 1.08e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1777 HQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDP 1856
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1857 EYPQDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEH 1936
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1937 GGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVY--DGEDKTALLESIVRDPRVDIIKLTPAHL 2014
Cdd:cd17646   161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVArpGGHRDPAYLAALIREHGVTTCHFVPSML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2015 QV-LKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEgrIEICNEYGPTETVVGCMIYRYDAAKDRReSVPIGTAAANT 2093
Cdd:cd17646   241 RVfLAEPAAGSCASLRRVFCSGEALPPELAARFLALPG--AELHNLYGPTEAAIDVTHWPVRGPAETP-SVPIGRPVPNT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2094 SIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKI 2173
Cdd:cd17646   318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2174 RGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVS---GGQTTAARLRKQLSQTLASYMVPAYFIELDEMPL 2250
Cdd:cd17646   398 RGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPaagAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPL 477
                         490
                  ....*....|.
gi 166797876 2251 TSNGKINKKGL 2261
Cdd:cd17646   478 TANGKLDRAAL 488
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3888-4908 1.25e-168

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 560.43  E-value: 1.25e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYV------------ 3955
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVdpaltfplpeii 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3956 -----LDHAAFEAEWYQgeeddADLyiRQFIRPFHldEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRI 4030
Cdd:PRK10252   89 dlrtqPDPHAAAQALMQ-----ADL--QQDLRVDS--GKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4031 Y---------EGETLPPLRIQYKDYAVWQTGEARlqqiQKQEAYWLELYSGDVPVLHLPAdyiRPSARDFAGATMH-FTL 4100
Cdd:PRK10252  160 YcawlrgeptPASPFTPFADVVEEYQRYRASEAW----QRDAAFWAEQRRQLPPPASLSP---APLPGRSASADILrLKL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4101 DKQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQY 4180
Cdd:PRK10252  233 EFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4181 LSEVKENALKAYEHQDYPFEvlidqlNIARDLSR----NPLFDTMFVLQNTEqEQLEINDVTfkpyPNGHTMAKF---DL 4253
Cdd:PRK10252  313 ATRLAAQLKKMRRHQRYDAE------QIVRDSGRaagdEPLFGPVLNIKVFD-YQLDFPGVQ----AQTHTLATGpvnDL 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4254 TLTAVEEGAGiQFTLEYLT--ALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDIQQlFNDTAVAekrIP 4331
Cdd:PRK10252  382 ELALFPDEHG-GLSIEILAnpQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQ-VNATAVE---IP 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4332 -TTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFL 4410
Cdd:PRK10252  457 eTTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4411 PIDPELPEKRRAFMLKDSGADVLLTCAGHA--IPPLFEGEVLLLDDPLLYQGRTDNLNLSCSenDLMYVIYTSGTTGQPK 4488
Cdd:PRK10252  537 PLDTGYPDDRLKMMLEDARPSLLITTADQLprFADVPDLTSLCYNAPLAPQGAAPLQLSQPH--HTAYIIFTSGSTGRPK 614
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4489 GVQLEHKTMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTA- 4566
Cdd:PRK10252  615 GVMVGQTAIVNRLLWMQNHYPLTAdDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTh 694
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4567 FLPT---AFLKLLASEKhyFEPFAECVDHIIAAGEQLIATrmLRDMLARH-QVTLHNHYGPSETHV-VTMYTVDPDTDQE 4641
Cdd:PRK10252  695 FVPSmlaAFVASLTPEG--ARQSCASLRQVFCSGEALPAD--LCREWQQLtGAPLHNLYGPTEAAVdVSWYPAFGEELAA 770
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4642 LQ----PIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPE 4717
Cdd:PRK10252  771 VRgssvPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDD 850
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4718 GNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLA------KENTDGQSDLYAYFTAEQ--SLSISQLKEKLA 4787
Cdd:PRK10252  851 GAVEYLGRSDDQLKIRGQRIELGEIDRAMQALpdVEQAVTHAcvinqaAATGGDARQLVGYLVSQSglPLDTSALQAQLR 930
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4788 GQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQTGTDyvAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGH 4867
Cdd:PRK10252  931 ERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGH 1008
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|.
gi 166797876 4868 SLRGMTLIAKIHKQFSKNISLREVFQCPTVGEMAQAIAEAE 4908
Cdd:PRK10252 1009 SLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEE 1049
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1780-2262 2.35e-168

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 529.99  E-value: 2.35e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1780 FEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYP 1859
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1860 QDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDG-SDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGAdAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 LTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLEsIVRDPRVDIIKLTPAHLQ 2015
Cdd:cd17651   161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvrtDPPALAA-WLDEQRISRVFLPTVALR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 VLKEMNIADQT---AVRRMIVGGENLST--RLARSIHEQFEGRIeiCNEYGPTET-VVGCMIYRYDAAkDRRESVPIGTA 2089
Cdd:cd17651   240 ALAEHGRPLGVrlaALRYLLTGGEQLVLteDLREFCAGLPGLRL--HNHYGPTEThVVTALSLPGDPA-AWPAPPPIGRP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2090 AANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDE 2169
Cdd:cd17651   317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADD 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2170 QVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVS--GGQTTAARLRKQLSQTLASYMVPAYFIELDE 2247
Cdd:cd17651   397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGdpEAPVDAAELRAALATHLPEYMVPSAFVLLDA 476
                         490
                  ....*....|....*
gi 166797876 2248 MPLTSNGKINKKGLP 2262
Cdd:cd17651   477 LPLTPNGKLDRRALP 491
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2829-3867 4.98e-161

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 538.09  E-value: 4.98e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLER-LFETYAvLRTRFYSGwNDTPLQIVYKTQT-PQIH 2906
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAgLAEADT-LRMRFTED-NGEVWQWVDPALTfPLPE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2907 FADLRDieEHLREDAIAAYQREDKAKGFDLARD-PLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQ 2985
Cdd:PRK10252   87 IIDLRT--QPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2986 EGREPEPLSAVPYSDYIEWLDRQDQGAA----KRYWSGYLEGYKGETTLLHKIAQHEQKEYAYANLICRFDHEQTKQLQQ 3061
Cdd:PRK10252  165 RGEPTPASPFTPFADVVEEYQRYRASEAwqrdAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLAA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3062 IANQHQVT--LNTLIqTLWgvlLQKYSGSADVVFGSVVSGR----PAEIPdveqmiGLFINTIPVRIRCDEDST------ 3129
Cdd:PRK10252  245 QASGVQRPdlALALV-ALW---LGRLCGRMDYAAGFIFMRRlgsaALTAT------GPVLNVLPLRVHIAAQETlpelat 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3130 -FADTMQMVQQNalasQSYDTyplyeiqaqtEQKQNlidhimifenyPIGQQAEETGHHGTELNITNFH-------MQEH 3201
Cdd:PRK10252  315 rLAAQLKKMRRH----QRYDA----------EQIVR-----------DSGRAAGDEPLFGPVLNIKVFDyqldfpgVQAQ 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3202 SHY-------DLNVVVIPGKQ--LAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEyLLSRF 3272
Cdd:PRK10252  370 THTlatgpvnDLELALFPDEHggLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYA-QLAQV 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3273 QSNDMHYPrEKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILG 3352
Cdd:PRK10252  449 NATAVEIP-ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3353 VLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYCGKLQDDigFSGtcIDLMEEHFYHEKD-----SSLALSyQSSQLAY 3427
Cdd:PRK10252  528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPR--FAD--VPDLTSLCYNAPLapqgaAPLQLS-QPHHTAY 602
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3428 AIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQvY--SAYDAelnIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDG 3505
Cdd:PRK10252  603 IIFTSGSTGRPKGVMVGQTAIVNRLLWMQNH-YplTADDV---VLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDP 678
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3506 AALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGV-----TLQHLLIGGEALSKTTVNKLKQLFGehgaAPgITNVYGPTE 3580
Cdd:PRK10252  679 LAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGArqscaSLRQVFCSGEALPADLCREWQQLTG----AP-LHNLYGPTE 753
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3581 TCVDASLFNiECSSDAWARSQNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF 3660
Cdd:PRK10252  754 AAVDVSWYP-AFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF 832
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3661 VPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE------AAAAALKDADDEYYLCGYF 3734
Cdd:PRK10252  833 APGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQavthacVINQAAATGGDARQLVGYL 912
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3735 AADKT--IQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAP-VKKRDSGieyVPPQTSAEIQLTAIWED 3811
Cdd:PRK10252  913 VSQSGlpLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPeLKAQVPG---RAPKTGTETIIAAAFSS 989
                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 3812 VLGLEQVGIRDHFFEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLARTI 3867
Cdd:PRK10252  990 LLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLL 1045
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
3284-3782 2.08e-160

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 505.82  E-value: 2.08e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPI 3363
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3364 DPDSPSERIRYILNDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLI 3443
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLT----------------------------------QPENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3444 EHRQVIHLIEGLSRQVYSAydAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGT 3523
Cdd:cd17644   127 EHQSLVNLSHGLIKEYGIT--SSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLP 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3524 PAHLKLLIAAGDLQGVTLQH----LLIGGEALSKTTVNKLKQLFGEHgaaPGITNVYGPTETCVDASLFNIecsSDAWAR 3599
Cdd:cd17644   205 PAYWHLLVLELLLSTIDLPSslrlVIVGGEAVQPELVRQWQKNVGNF---IQLINVYGPTEATIAATVCRL---TQLTER 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3600 SQNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFV--PEDRMYRTGDLARLLP 3677
Cdd:cd17644   279 NITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLP 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3678 DGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADK--TIQISELRKRMARHLPG 3755
Cdd:cd17644   359 DGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYeeSPSTVELRQFLKAKLPD 438
                         490       500
                  ....*....|....*....|....*..
gi 166797876 3756 YMIPAHFVQLDKMPLTPNGKLNRQLLP 3782
Cdd:cd17644   439 YMIPSAFVVLEELPLTPNGKIDRRALP 465
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
290-686 1.10e-159

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 501.41  E-value: 1.10e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   290 TYRELNEKASRLARTLR-NCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   369 HLKNSLAFDGPVIDLND--EASYHADCSLLSPV---AGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSP 443
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDplELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   444 ADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQER-ITHFSTSPRLLKTMIEQMnREDFIHVQH 522
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAAL-PPALASLRL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   523 VVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ----ITIGSPVANHQAYILGAHHQIQPIGIP 598
Cdd:TIGR01733  240 VILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPrespVPIGRPLANTRLYVLDDDLRPVPVGVV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   599 GELYVGGAGVARGYLNRPELTEEKFVEHLHVP--GQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMF 676
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
                          410
                   ....*....|
gi 166797876   677 NLENVREAAV 686
Cdd:TIGR01733  400 RHPGVREAVV 409
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
277-750 2.64e-159

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 501.40  E-value: 2.64e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQHhlknslafdgpvidlndeasyhadcsllspvaghSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKK 436
Cdd:cd17652    81 ADARPALLLTTP----------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  437 AFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEqmnrED 516
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPP----DD 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  517 FIHVQHVVVGGEQLETDTVEKLhslQPRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIG 596
Cdd:cd17652   203 LPDLRTLVVAGEACPAELVDRW---APGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPG 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  597 IPGELYVGGAGVARGYLNRPELTEEKFVEH-LHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAM 675
Cdd:cd17652   280 VPGELYIAGAGLARGYLNRPGLTAERFVADpFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAAL 359
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  676 FNLENVREAAVVAREDADGAKQLYAYYVGEPS--LTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALP 750
Cdd:cd17652   360 TEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
PRK12316 PRK12316
peptide synthase; Provisional
47-842 4.67e-159

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 559.96  E-value: 4.67e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   47 RSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDRTSLILGIPTVSKQKAGQSAVNNIVLLKNTLSNESTFKT-- 124
Cdd:PRK12316 4318 RELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAqq 4397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  125 VFGQLKEAVNDslknQNLPFRKMarhlsvqyndEHMPL-------------------IHTVVSLNEIHSLQCKEDTATDT 185
Cdd:PRK12316 4398 SVVEWLQQVQR----QNLALREH----------EHTPLyeiqrwagqggealfdsllVFENYPVSEALQQGAPGGLRFGE 4463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  186 LFHFDLEN----------NGIHLKLFYNGNLYDERYINQIVSHLDQLLSVILFQPQAAIHTAEILPEAQKQKLLFDFNDT 255
Cdd:PRK12316 4464 VTNHEQTNypltlavglgETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRT 4543
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  256 VRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWK 335
Cdd:PRK12316 4544 DAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLK 4623
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  336 AGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSL----AFDGPVIDLNDEASYHADCSLLSPVAGhSHLAYVIYT 411
Cdd:PRK12316 4624 AGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpipdGLASLALDRDEDWEGFPAHDPAVRLHP-DNLAYVIYT 4702
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  412 SGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQnAIK 491
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYA-EIH 4781
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  492 QERITHFSTSPRLLKTMIEQM-NREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSAD- 569
Cdd:PRK12316 4782 EHRVTVLVFPPVYLQQLAEHAeRDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDa 4861
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  570 ---EQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFV-EHLHVPGQKMYKTGDLARWLP 645
Cdd:PRK12316 4862 cgaAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVpDPFGAPGGRLYRTGDLARYRA 4941
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  646 DGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGaKQLYAYYV-GEPSLTAA---------QFRE 715
Cdd:PRK12316 4942 DGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVpQDPALADAdeaqaelrdELKA 5020
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  716 ELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADEnTRAENEYIAPRNTIEELLASIWQEVLGAERIGILDNFFDF 795
Cdd:PRK12316 5021 ALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDA-SLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFEL 5099
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876  796 GGDSIKSIQVSSRL-YQAGYKVDMKHLFKHPSIAELSQFVAPVSRVAD 842
Cdd:PRK12316 5100 GGHSLLAIQVTSRIqLELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
277-749 3.49e-158

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 499.90  E-value: 3.49e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHsHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKK 436
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPD-DLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  437 AFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSP---RLLKTMiEQMN 513
Cdd:cd12116   160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPatwRMLLDA-GWQG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  514 REDFihvqHVVVGGEQLETDTVEKLhsLQPRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQ 593
Cdd:cd12116   239 RAGL----TALCGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  594 PIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHV-PGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVE 672
Cdd:cd12116   313 PPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876  673 AAMFNLENVREAAVVAREDaDGAKQLYAYYVGE--PSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd12116   393 AALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKagAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
276-750 8.11e-157

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 496.23  E-value: 8.11e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  276 TPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYL 355
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  356 LHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWK 435
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  436 KAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMN-R 514
Cdd:cd17656   161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREfI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  515 EDFIH-VQHVVVGGEQLE-TDT-VEKLHSLQprIRINNEYGPTENSVVS--TFHPVQSADEQITIGSPVANHQAYILGAH 589
Cdd:cd17656   241 NRFPTcVKHIITAGEQLViTNEfKEMLHEHN--VHLHNHYGPSETHVVTtyTINPEAEIPELPPIGKPISNTWIYILDQE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  590 HQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIG 669
Cdd:cd17656   319 QQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  670 EVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd17656   399 EIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478

                  .
gi 166797876  750 P 750
Cdd:cd17656   479 P 479
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1788-2262 2.82e-156

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 492.92  E-value: 2.82e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQrdvrkqlayegvtvllddessyhqdgsdlapisdVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAK 1947
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1948 EVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTA--LLESIVRDPRVDIIKLTPAHLQVLKEMNIADq 2025
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgePLADLLREHRITHVTLPPAALAALPPDDLPD- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2026 taVRRMIVGGENLSTRLARsihEQFEGRIEIcNEYGPTETVVGCMIYRYDAAKDRresVPIGTAAANTSIYVLDENMKPA 2105
Cdd:cd17652   206 --LRTLVVAGEACPAELVD---RWAPGRRMI-NAYGPTETTVCATMAGPLPGGGV---PPIGRPVPGTRVYVLDARLRPV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2106 PIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIE 2184
Cdd:cd17652   277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2185 AALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLP 2262
Cdd:cd17652   357 AALTEHPGVAEAVVVVRDDRPGDKRLVAYVVpaPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1776-2261 3.34e-156

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 492.99  E-value: 3.34e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPID 1855
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1856 PEYPQDRIRYMLDDSQAGIVLMQRDvrkqlayegvtvllddessyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIE 1935
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTDPD----------------------------------DLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1936 HGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDgedkTAL-LESIVRDPRVDIIKLTPAHL 2014
Cdd:cd12115   127 HRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLaLPDLPAAAEVTLINTVPSAA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2015 QVLKEMNiADQTAVRRMIVGGENLSTRLARSIHEQFEGRiEICNEYGPTETVV---GCMIyrydaAKDRRESVPIGTAAA 2091
Cdd:cd12115   203 AELLRHD-ALPASVRVVNLAGEPLPRDLVQRLYARLQVE-RVVNLYGPSEDTTystVAPV-----PPGASGEVSIGRPLA 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2092 NTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQV 2171
Cdd:cd12115   276 NTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQV 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2172 KIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVS--GGQTTAARLRKQLSQTLASYMVPAYFIELDEMP 2249
Cdd:cd12115   356 KVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAepGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALP 435
                         490
                  ....*....|..
gi 166797876 2250 LTSNGKINKKGL 2261
Cdd:cd12115   436 LTPNGKIDRSAL 447
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
264-750 1.57e-154

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 488.87  E-value: 1.57e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  264 TVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPL 343
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  344 DPEYPKERLQYLLHDADADVLLVQHHlknslafdgpvidlndeasyhadcsllspvaghsHLAYVIYTSGTTGKPKGVMV 423
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQPE----------------------------------NLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  424 EHGGIVN-SLQWKKAFFKHSPaDRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSP 502
Cdd:cd17644   127 EHQSLVNlSHGLIKEYGITSS-DRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  503 RLLKTMIEQMNREDFI---HVQHVVVGGEQLETDTVEKLHS-LQPRIRINNEYGPTENSVVST-FHPVQSADEQIT---I 574
Cdd:cd17644   206 AYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKnVGNFIQLINVYGPTEATIAATvCRLTQLTERNITsvpI 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  575 GSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHVPGQKMYKTGDLARWLPDGRIEYL 652
Cdd:cd17644   286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHpfNSSESERLYKTGDLARYLPDGNIEYL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  653 GRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVG--EPSLTAAQFREELSRELPNYMIPSRF 730
Cdd:cd17644   366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyEESPSTVELRQFLKAKLPDYMIPSAF 445
                         490       500
                  ....*....|....*....|
gi 166797876  731 IPLERIPLTSNGKIDLKALP 750
Cdd:cd17644   446 VVLEELPLTPNGKIDRRALP 465
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
4359-4755 1.08e-153

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 484.08  E-value: 1.08e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4359 TYRQLNERSNQLARVLQD-KGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCA 4437
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4438 GHAIPPLFEG--EVLLLDDPLLYQGRTDNLNLSCSE---NDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLR- 4511
Cdd:TIGR01733   81 ALASRLAGLVlpVILLDPLELAALDDAPAPPPPDAPsgpDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDp 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4512 FDRVLQFAAMSFDVCYQEMFSALSSGG-ILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEKHyfePFAECV 4590
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGAtLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALP---PALASL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4591 DHIIAAGEQL---IATRMLRdmlARHQVTLHNHYGPSETHV-VTMYTVDPD--TDQELQPIGKPISNTEIFILNEAGTLQ 4664
Cdd:TIGR01733  238 RLVILGGEALtpaLVDRWRA---RGPGARLINLYGPTETTVwSTATLVDPDdaPRESPVPIGRPLANTRLYVLDDDLRPV 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4665 PVGIVGELCISGVSLARGYHNRESLTLETFVPHPYD--SNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEV 4742
Cdd:TIGR01733  315 PVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEI 394
                          410
                   ....*....|....*
gi 166797876  4743 EAALLKH--VQEAVV 4755
Cdd:TIGR01733  395 EAALLRHpgVREAVV 409
PRK05691 PRK05691
peptide synthase; Validated
7-1050 1.16e-153

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 542.07  E-value: 1.16e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    7 QETYW-ENLFDEEDGLSAfpyfkAADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTD 85
Cdd:PRK05691  865 QLAYWkAQLGDEQPVLEL-----ATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSG 939
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   86 RTSLILGIPTVSKQKAG-QSAVN---NIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHL---------S 152
Cdd:PRK05691  940 QGDIRIGVPNANRPRLEtQGLVGffiNTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALpqareqglfQ 1019
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  153 VQYNDEHMPLihtvVSLNEIHSLQCKE------DTATDTLFHFDLENNG-IHLKLFYNGNLYDERYINQIVSHLDQLLSV 225
Cdd:PRK05691 1020 VMFNHQQRDL----SALRRLPGLLAEElpwhsrEAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQ 1095
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  226 ILFQPQAAIHTAEILPEAQKQKLLfdfndtvrDFS------GSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKAS 299
Cdd:PRK05691 1096 VCEDPQRALGDVQLLDAAERAQLA--------QWGqapcapAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQAN 1167
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  300 RLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSL-AFDG 378
Cdd:PRK05691 1168 RLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLpQAEG 1247
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  379 -PVIDLndeASYHADCSLLSPVAGHSH---LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYV 454
Cdd:PRK05691 1248 vSAIAL---DSLHLDSWPSQAPGLHLHgdnLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIS 1324
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  455 FDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLETDT 534
Cdd:PRK05691 1325 FDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAEL 1404
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  535 VEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSAD-EQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYL 613
Cdd:PRK05691 1405 RNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDgERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYL 1484
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  614 NRPELTEEKFV-EHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDA 692
Cdd:PRK05691 1485 GRPALTAERFVpDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGA 1564
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  693 DGAkQLYAYYVGE--PSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADENTRaenEYIAPRNTIE 770
Cdd:PRK05691 1565 AGA-QLVGYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQR---EHVEPRTELQ 1640
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  771 ELLASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRLYQA-GYKVDMKHLFKHpsiAELSQFVAPVSRVADQGEVNGG 849
Cdd:PRK05691 1641 QQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEA---SELGAFAEQVARIQAAGERNSQ 1717
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  850 TKLT--------PIQH-----WFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTpDGyAPRI 916
Cdd:PRK05691 1718 GAIArvdrsqpvPLSYsqqrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSV-DG-VPVQ 1795
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  917 TGTDESELfHLEVMNYkgETDPA-------QAIADkaNEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSW 988
Cdd:PRK05691 1796 QVAEDSGL-RMDWQDF--SALPAdarqqrlQQLAD--SEAHQPFDLERGPLLRACLVKAAEREHyFVLTLHHIVTEGWAM 1870
                        1050      1060      1070      1080      1090      1100      1110
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  989 RILLEDFASGYEQ--AERRQTIQ-LPQKTDSFPFWADQlskYAAETDMEEEIAYWT----------ELSSIKPQP 1050
Cdd:PRK05691 1871 DIFARELGALYEAflDDRESPLEpLPVQYLDYSVWQRQ---WLESGERQRQLDYWKaqlgnehpllELPADRPRP 1942
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1788-2262 1.36e-153

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 485.72  E-value: 1.36e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQrdvrkqlayegvtvllddessyHQDgsdlapisdvsHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAK 1947
Cdd:cd17649    81 EDSGAGLLLTH----------------------HPR-----------QLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1948 EVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE--DKTALLESIVRDPRVDIIKLTPAHL-QVLKEMNIA- 2023
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAYLqQLAEEADRTg 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2024 --DQTAVRRMIVGGENLSTRLARsihEQFEGRIEICNEYGPTETVVGCMIYRYDA-AKDRRESVPIGTAAANTSIYVLDE 2100
Cdd:cd17649   208 dgRPPSLRLYIFGGEALSPELLR---RWLKAPVRLFNAYGPTEATVTPLVWKCEAgAARAGASMPIGRPLGGRSAYILDA 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2101 NMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIE 2179
Cdd:cd17649   285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIE 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2180 LGEIEAALLQEEVIKEAVVTAReDVHGFKQLCAYYVSG----GQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGK 2255
Cdd:cd17649   365 LGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRaaaaQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGK 443

                  ....*..
gi 166797876 2256 INKKGLP 2262
Cdd:cd17649   444 LDRKALP 450
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
4335-4818 3.64e-153

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 486.01  E-value: 3.64e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4335 HQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDP 4414
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4415 ELPEKRRAFMLKDSGADVLLTCAGHAIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEH 4494
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4495 KTMTNLLAYEQDHTQL-RFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTA-FLPT-- 4570
Cdd:cd17646   161 AGIVNRLLWMQDEYPLgPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTChFVPSml 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4571 -AFLKLLASEKhyfepfAECVDHIIAAGEQLIATRMLRdMLARHQVTLHNHYGPSETHV-VTMYTVDPDTDQELQPIGKP 4648
Cdd:cd17646   241 rVFLAEPAAGS------CASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIdVTHWPVRGPAETPSVPIGRP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4649 ISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDH 4728
Cdd:cd17646   314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDD 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4729 QVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA---EQSLSISQLKEKLAGQIPGYMIPSYFIQLE 4803
Cdd:cd17646   394 QVKIRGFRVEPGEIEAALAAHpaVTHAVVVARAAPAGAARLVGYVVPaagAAGPDTAALRAHLAERLPEYMVPAAFVVLD 473
                         490
                  ....*....|....*
gi 166797876 4804 KLPLTGNGKVNRRAL 4818
Cdd:cd17646   474 ALPLTANGKLDRAAL 488
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
3296-3782 4.15e-153

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 485.44  E-value: 4.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3296 TPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYI 3375
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3376 LNDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEgl 3455
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3456 SRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGD 3535
Cdd:cd17656   159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSERE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3536 LQG---VTLQHLLIGGEALSKTtvNKLKQLFGEHGAApgITNVYGPTETCVDASlfnieCSSDAWARSQNYVPIGKPLGR 3612
Cdd:cd17656   239 FINrfpTCVKHIITAGEQLVIT--NEFKEMLHEHNVH--LHNHYGPSETHVVTT-----YTINPEAEIPELPPIGKPISN 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3613 NRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVK 3692
Cdd:cd17656   310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3693 IQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTP 3772
Cdd:cd17656   390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTP 469
                         490
                  ....*....|
gi 166797876 3773 NGKLNRQLLP 3782
Cdd:cd17656   470 NGKVDRKALP 479
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
3289-3782 5.34e-152

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 483.00  E-value: 5.34e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3289 FEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSP 3368
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3369 SERIRYILNDSSISVLLycgkLQDDIGF-------SGTCIDlmEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGT 3441
Cdd:cd17651    81 AERLAFMLADAGPVLVL----THPALAGelavelvAVTLLD--QPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3442 LIEHRQVIHLIEGLSRqvYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITD 3521
Cdd:cd17651   155 VMPHRSLANLVAWQAR--ASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3522 GTPAHLKLLIAAGDLQGVT---LQHLLIGGEALSKTTvnKLKQLFGEHgaaPGIT--NVYGPTETCVdASLFNIECSSDA 3596
Cdd:cd17651   233 LPTVALRALAEHGRPLGVRlaaLRYLLTGGEQLVLTE--DLREFCAGL---PGLRlhNHYGPTETHV-VTALSLPGDPAA 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3597 WARSqnyVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLL 3676
Cdd:cd17651   307 WPAP---PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3677 PDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKT--IQISELRKRMARHLP 3754
Cdd:cd17651   384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLP 463
                         490       500
                  ....*....|....*....|....*...
gi 166797876 3755 GYMIPAHFVQLDKMPLTPNGKLNRQLLP 3782
Cdd:cd17651   464 EYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1788-2261 1.39e-150

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 477.19  E-value: 1.39e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDvrkqlayegvtvllddessyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAK 1947
Cdd:cd17643    81 ADSGPSLLLTDPD----------------------------------DLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1948 EVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIV--YDGEDKTALLESIVRDPRVDIIKLTP-AHLQVLKE--MNI 2022
Cdd:cd17643   127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVvpYEVARSPEDFARLLRDEGVTVLNQTPsAFYQLVEAadRDG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2023 ADQTAVRRMIVGGENLSTRLARSIHEQFEG-RIEICNEYGPTETVVGCMIYRYDAAK-DRRESVPIGTAAANTSIYVLDE 2100
Cdd:cd17643   207 RDPLALRYVIFGGEALEAAMLRPWAGRFGLdRPQLVNMYGITETTVHVTFRPLDAADlPAAAASPIGRPLPGLRVYVLDA 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2101 NMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIE 2179
Cdd:cd17643   287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIE 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2180 LGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAAR--LRKQLSQTLASYMVPAYFIELDEMPLTSNGKIN 2257
Cdd:cd17643   367 LGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIaeLRALLKELLPDYMVPARYVPLDALPLTVNGKLD 446

                  ....
gi 166797876 2258 KKGL 2261
Cdd:cd17643   447 RAAL 450
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
277-749 2.77e-150

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 476.19  E-value: 2.77e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQhhlknslafdgpvidlndeasyhadcsllsPvaghSHLAYVIYTSGTTGKPKGVMVEHGGIVNS-LQWK 435
Cdd:cd17650    81 EDSGAKLLLTQ------------------------------P----EDLAYVIYTSGTTGKPKGVMVEHRNVAHAaHAWR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  436 KAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQM--N 513
Cdd:cd17650   127 REYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVyrN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  514 REDFIHVQHVVVGGEQLET-DTVEKLHSLQPRIRINNEYGPTENSVVSTFHPvQSADEQIT-----IGSPVANHQAYILG 587
Cdd:cd17650   207 GLDLSAMRLLIVGSDGCKAqDFKTLAARFGQGMRIINSYGVTEATIDSTYYE-EGRDPLGDsanvpIGRPLPNTAMYVLD 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  588 AHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIE 667
Cdd:cd17650   286 ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIE 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  668 IGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLK 747
Cdd:cd17650   366 LGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445

                  ..
gi 166797876  748 AL 749
Cdd:cd17650   446 AL 447
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
4923-5335 1.30e-149

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 473.00  E-value: 1.30e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4923 VYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMER 5002
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5003 YEATA-------DEVEECFRAFV-RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDG---- 5070
Cdd:cd19531    81 VDLSGlpeaereAEAQRLAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAflag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5071 --KELAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQL 5148
Cdd:cd19531   161 rpSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5149 EELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKA 5228
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5229 FEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQTDIEVDSLAVRPYEQTETAAKFDLQLNFLIDQDEIQGSFDYC 5308
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                         410       420
                  ....*....|....*....|....*..
gi 166797876 5309 TKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19531   401 TDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
266-750 2.11e-149

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 473.19  E-value: 2.11e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  266 YQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDP 345
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  346 EYPKERLQYLLHDADADVLLVQHhlknslafdgpvidlndeasyhadcsllspvaghSHLAYVIYTSGTTGKPKGVMVEH 425
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTNP----------------------------------DDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  426 GGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERIThFSTSPRLL 505
Cdd:cd17645   127 HNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTGA 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  506 KTMIEQMNREDFihvQHVVVGGEQLETdTVEKLHSLQpririnNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYI 585
Cdd:cd17645   206 AEQFMQLDNQSL---RVLLTGGDKLKK-IERKGYKLV------NNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYI 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  586 LGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYR 665
Cdd:cd17645   276 LDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  666 IEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:cd17645   356 IEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435

                  ....*
gi 166797876  746 LKALP 750
Cdd:cd17645   436 RKALP 440
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1788-2261 2.73e-149

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 474.09  E-value: 2.73e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDVRKQLAyEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAK 1947
Cdd:cd12116    81 EDAEPALVLTDDALPDRLP-AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1948 EVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIvRDPRVDIIKLTPAHLQVLKEmniAD 2024
Cdd:cd12116   160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtqrDPEALARLI-EAHSITVMQATPATWRMLLD---AG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2025 QTAVR--RMIVGGENLSTRLArsihEQFEGRI-EICNEYGPTETVVGCMIYRYDAAKdrrESVPIGTAAANTSIYVLDEN 2101
Cdd:cd12116   236 WQGRAglTALCGGEALPPDLA----ARLLSRVgSLWNLYGPTETTIWSTAARVTAAA---GPIPIGRPLANTQVYVLDAA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2102 MKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIEL 2180
Cdd:cd12116   309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2181 GEIEAALLQEEVIKEAVVTAREDvHGFKQLCAYYVSGGQTT--AARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:cd12116   389 GEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAApdAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDR 467

                  ...
gi 166797876 2259 KGL 2261
Cdd:cd12116   468 KAL 470
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1776-2262 4.28e-149

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 473.46  E-value: 4.28e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPID 1855
Cdd:cd17644     2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1856 PEYPQDRIRYMLDDSQAGIVLMQRDvrkqlayegvtvllddessyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIE 1935
Cdd:cd17644    82 PNYPQERLTYILEDAQISVLLTQPE----------------------------------NLAYVIYTSGSTGKPKGVMIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1936 HGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIvRDPRVDIIKLTPA 2012
Cdd:cd17644   128 HQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEmrsSLEDFVQYI-QQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2013 HLQ----VLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCMIYRY-DAAKDRRESVPIG 2087
Cdd:cd17644   207 YWHllvlELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLtQLTERNITSVPIG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2088 TAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFE--PGAKMYKTGDLAKWLADGNIEYAG 2165
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2166 RIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTT--AARLRKQLSQTLASYMVPAYFI 2243
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESpsTVELRQFLKAKLPDYMIPSAFV 446
                         490
                  ....*....|....*....
gi 166797876 2244 ELDEMPLTSNGKINKKGLP 2262
Cdd:cd17644   447 VLEELPLTPNGKIDRRALP 465
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
265-749 2.38e-148

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 470.65  E-value: 2.38e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  265 VYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLD 344
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  345 PEYPKERLQYLLHDADADVLLVQHHlknslafdgpvidlndeasyhadcsllspvaghsHLAYVIYTSGTTGKPKGVMVE 424
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTDPD----------------------------------DLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  425 HGGIVNSLQWKKAFFkhsPAD---RVLVLYPYVFDAFILNFFGPLISGATLHLLPNeenkeTFAIQNAIKQERITHFSTS 501
Cdd:cd12115   127 HRNAAAFLQWAAAAF---SAEelaGVLASTSICFDLSVFELFGPLATGGKVVLADN-----VLALPDLPAAAEVTLINTV 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  502 PrllkTMIEQMNREDFI--HVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPV-QSADEQITIGSPV 578
Cdd:cd12115   199 P----SAAAELLRHDALpaSVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVpPGASGEVSIGRPL 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  579 ANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQ 658
Cdd:cd12115   275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  659 VKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPS--LTAAQFREELSRELPNYMIPSRFIPLERI 736
Cdd:cd12115   355 VKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGaaGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
                         490
                  ....*....|...
gi 166797876  737 PLTSNGKIDLKAL 749
Cdd:cd12115   435 PLTPNGKIDRSAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
277-749 3.76e-148

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 469.87  E-value: 3.76e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQHHlknslafdgpvidlndeasyhadcsllspvaghsHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKK 436
Cdd:cd17643    81 ADSGPSLLLTDPD----------------------------------DLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  437 AFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIE--QMNR 514
Cdd:cd17643   127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaaDRDG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  515 EDFIHVQHVVVGGEQLETDTVEKL--HSLQPRIRINNEYGPTENSVVSTFHPVQSAD----EQITIGSPVANHQAYILGA 588
Cdd:cd17643   207 RDPLALRYVIFGGEALEAAMLRPWagRFGLDRPQLVNMYGITETTVHVTFRPLDAADlpaaAASPIGRPLPGLRVYVLDA 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  589 HHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH-LHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIE 667
Cdd:cd17643   287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANpFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIE 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  668 IGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVG--EPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:cd17643   367 LGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAddGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLD 446

                  ....
gi 166797876  746 LKAL 749
Cdd:cd17643   447 RAAL 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1787-2262 8.03e-148

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 470.42  E-value: 8.03e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1787 TPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYM 1866
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1867 LDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWA 1946
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1947 KEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTAL--LESIVRDPRVDIIKLTPAHLQVLKEMNIAD 2024
Cdd:cd17656   161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVeqLFDLVKRHNIEVVFLPVAFLKFIFSEREFI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2025 Q---TAVRRMIVGGENL--STRLARSIHEQfegRIEICNEYGPTETVVGCMiYRYDAAKDRRESVPIGTAAANTSIYVLD 2099
Cdd:cd17656   241 NrfpTCVKHIITAGEQLviTNEFKEMLHEH---NVHLHNHYGPSETHVVTT-YTINPEAEIPELPPIGKPISNTWIYILD 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2100 ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIE 2179
Cdd:cd17656   317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2180 LGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKK 2259
Cdd:cd17656   397 LGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476

                  ...
gi 166797876 2260 GLP 2262
Cdd:cd17656   477 ALP 479
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
3286-3781 4.06e-147

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 468.68  E-value: 4.06e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3286 HELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDP 3365
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3366 DSPSERIRYILNDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEH 3445
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3446 RQVIHLIEGLSRQvYSaYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPA 3525
Cdd:cd17646   161 AGIVNRLLWMQDE-YP-LGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3526 HLKLLIAAGDL-QGVTLQHLLIGGEALSKTTVNKLKQLFGehgaAPgITNVYGPTETCVDASLFniECSSDAWARSqnyV 3604
Cdd:cd17646   239 MLRVFLAEPAAgSCASLRRVFCSGEALPPELAARFLALPG----AE-LHNLYGPTEAAIDVTHW--PVRGPAETPS---V 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 PIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYI 3684
Cdd:cd17646   309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3685 GRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQ---ISELRKRMARHLPGYMIPAH 3761
Cdd:cd17646   389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgpdTAALRAHLAERLPEYMVPAA 468
                         490       500
                  ....*....|....*....|
gi 166797876 3762 FVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd17646   469 FVVLDALPLTANGKLDRAAL 488
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3310-3715 4.40e-147

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 465.20  E-value: 4.40e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3310 TYEELNRRANQLARTLQA-KGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYCG 3388
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3389 KLQDDIGFSGTCIDLMEEHFYHEKDSSLALSY-----QSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRqvYSAY 3463
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPpdapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR--RYGL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3464 DAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYY-RQHSIDITDGTPAHLKLLIAAGDLQGVTLQ 3542
Cdd:TIGR01733  159 DPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAALPPALASLR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3543 HLLIGGEALSKTTVNKLKQLFGEhgaaPGITNVYGPTETCVDASLFNIEcssDAWARSQNYVPIGKPLGRNRMYILDSKK 3622
Cdd:TIGR01733  239 LVILGGEALTPALVDRWRARGPG----ARLINLYGPTETTVWSTATLVD---PDDAPRESPVPIGRPLANTRLYVLDDDL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3623 RLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPED--RMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIEL 3700
Cdd:TIGR01733  312 RPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIEL 391
                          410
                   ....*....|....*
gi 166797876  3701 GEIESVMLNVPDIQE 3715
Cdd:TIGR01733  392 GEIEAALLRHPGVRE 406
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
4346-4819 8.86e-147

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 465.57  E-value: 8.86e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGADVLLTCAGHaipplfegevlllddpllyqgrtdnlnlscsendLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQ 4505
Cdd:cd17652    81 ADARPALLLTTPDN----------------------------------LAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4506 DHTQLRFD-RVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEKhyfe 4584
Cdd:cd17652   127 AAFDVGPGsRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD---- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4585 pfAECVDHIIAAGEqlIATRMLRDMLARHQVTLhNHYGPSETHV-VTMYTVDPDTDQelQPIGKPISNTEIFILNEAGTL 4663
Cdd:cd17652   203 --LPDLRTLVVAGE--ACPAELVDRWAPGRRMI-NAYGPTETTVcATMAGPLPGGGV--PPIGRPVPGTRVYVLDARLRP 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4664 QPVGIVGELCISGVSLARGYHNRESLTLETFVPHPY-DSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEV 4742
Cdd:cd17652   276 VPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4743 EAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQS--LSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd17652   356 EAALTEHpgVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435

                  .
gi 166797876 4819 P 4819
Cdd:cd17652   436 P 436
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
3297-3781 2.31e-146

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 464.63  E-value: 2.31e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLs 3456
Cdd:cd17650    81 EDSGAKLLLT----------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDL 3536
Cdd:cd17650   126 RREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3537 QGVTLQH---LLIGGEAlskTTVNKLKQLFGEHGAAPGITNVYGPTETCVDASLFniECSSDAWARSQNyVPIGKPLGRN 3613
Cdd:cd17650   206 NGLDLSAmrlLIVGSDG---CKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYY--EEGRDPLGDSAN-VPIGRPLPNT 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3614 RMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKI 3693
Cdd:cd17650   280 AMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKI 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3694 QGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPN 3773
Cdd:cd17650   360 RGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPN 439

                  ....*...
gi 166797876 3774 GKLNRQLL 3781
Cdd:cd17650   440 GKVDRRAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1788-2261 2.54e-145

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 461.94  E-value: 2.54e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDvrkqlayegvtvllddessyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIEHGGLTN-YIWWA 1946
Cdd:cd17650    81 EDSGAKLLLTQPE----------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHaAHAWR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1947 KEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDK--TALLESIVRDPRVDIIKLTPAHLQ-VLKEM--N 2021
Cdd:cd17650   127 REYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKldPAALYDLILKSRITLMESTPALIRpVMAYVyrN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2022 IADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCMIYRYDAAK-DRRESVPIGTAAANTSIYVLDE 2100
Cdd:cd17650   207 GLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPlGDSANVPIGRPLPNTAMYVLDE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2101 NMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIEL 2180
Cdd:cd17650   287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIEL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2181 GEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKG 2260
Cdd:cd17650   367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446

                  .
gi 166797876 2261 L 2261
Cdd:cd17650   447 L 447
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
4335-4819 3.07e-145

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 461.25  E-value: 3.07e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4335 HQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDP 4414
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4415 ELPEKRRAFMLKDSGADVLLTCAGhaipplfegevlllddpllyqgrtdnlnlscsenDLMYVIYTSGTTGQPKGVQLEH 4494
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTNPD----------------------------------DLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4495 KTMTNLLAYEQDHTQL-RFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPT-AF 4572
Cdd:cd17645   127 HNLVNLCEWHRPYFGVtPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTgAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4573 LKLLASEKHYFEPfaecvdhIIAAGEQLiatrmlrDMLARHQVTLHNHYGPSE-THVVTMYTVDPDtDQELqPIGKPISN 4651
Cdd:cd17645   207 EQFMQLDNQSLRV-------LLTGGDKL-------KKIERKGYKLVNNYGPTEnTVVATSFEIDKP-YANI-PIGKPIDN 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4652 TEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVK 4731
Cdd:cd17645   271 TRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVK 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4732 IRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTG 4809
Cdd:cd17645   351 IRGYRIEPGEIEPFLMNHplIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTA 430
                         490
                  ....*....|
gi 166797876 4810 NGKVNRRALP 4819
Cdd:cd17645   431 NGKVDRKALP 440
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
192-835 3.09e-145

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 491.48  E-value: 3.09e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  192 ENNGIHLKLFYNGNLYDERYINQIVSHLDQLLSVILFQPQAAIHTAEILPEAQKQKLlFDFNDTVRDFSgSRTVYQLFEE 271
Cdd:PRK10252  389 EHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQL-AQVNATAVEIP-ETTLSALVAQ 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  272 QAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKER 351
Cdd:PRK10252  467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  352 LQYLLHDADADVLLVQHHLKNSLAfDGPVIDLN--DEASYHADCSLLSPVAGHsHLAYVIYTSGTTGKPKGVMVEHGGIV 429
Cdd:PRK10252  547 LKMMLEDARPSLLITTADQLPRFA-DVPDLTSLcyNAPLAPQGAAPLQLSQPH-HTAYIIFTSGSTGRPKGVMVGQTAIV 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  430 NSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERIT--HFStsPRLLKT 507
Cdd:PRK10252  625 NRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTttHFV--PSMLAA 702
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  508 MIEQMNREDFIH----VQHVVVGGEQLETDTVEKLHSLQpRIRINNEYGPTENSVVSTFHPVqSADEQ-------ITIGS 576
Cdd:PRK10252  703 FVASLTPEGARQscasLRQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWYPA-FGEELaavrgssVPIGY 780
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  577 PVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRID 656
Cdd:PRK10252  781 PVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSD 860
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  657 HQVKIRGYRIEIGEVEAAMFNLENVREAAVVAR------EDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPS 728
Cdd:PRK10252  861 DQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSglPLDTSALQAQLRERLPPHMVPV 940
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  729 RFIPLERIPLTSNGKIDLKALPAADENTRAENEyiAPRNTIEELLASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSR 808
Cdd:PRK10252  941 VLLQLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQ 1018
                         650       660
                  ....*....|....*....|....*...
gi 166797876  809 LYQA-GYKVDMKHLFKHPSIAELSQFVA 835
Cdd:PRK10252 1019 LSRQfARQVTPGQVMVASTVAKLATLLD 1046
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
277-750 4.71e-145

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 461.07  E-value: 4.71e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQHHlknslafdgpvidlndeasyhadcsllspvaghSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKK 436
Cdd:cd17649    81 EDSGAGLLLTHHP---------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  437 AFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNRE- 515
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTg 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  516 --DFIHVQHVVVGGEQLETDTVEKlhSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ----ITIGSPVANHQAYILGAH 589
Cdd:cd17649   208 dgRPPSLRLYIFGGEALSPELLRR--WLKAPVRLFNAYGPTEATVTPLVWKCEAGAARagasMPIGRPLGGRSAYILDAD 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  590 HQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH-LHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEI 668
Cdd:cd17649   286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  669 GEVEAAMFNLENVREAAVVAReDADGAKQLYAYYVGE----PSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd17649   366 GEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRaaaaQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444

                  ....*.
gi 166797876  745 DLKALP 750
Cdd:cd17649   445 DRKALP 450
PRK05691 PRK05691
peptide synthase; Validated
3877-4904 1.43e-144

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 512.02  E-value: 1.43e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3877 AIPAIEKRPYYPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVL 3956
Cdd:PRK05691 3248 PVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVI 3327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3957 DHAAFEAEWYQGEEDDADLYIRQFIRPFH----------LDEPPL-LRvgLIELQPDRGILMFDMHHIISDGTSMSVLIK 4025
Cdd:PRK05691 3328 HKPGRTPIDYLDWRGLPEDGQEQRLQALHkqereagfdlLNQPPFhLR--LIRVDEARYWFMMSNHHILIDAWCRSLLMN 3405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4026 EFIRIY----EGE----TLPPlriQYKDYAVWqtgearLQQIQKQEA--YWLELYSGDVPVLHLPADyiRPSARDFAGAT 4095
Cdd:PRK05691 3406 DFFEIYtalgEGReaqlPVPP---RYRDYIGW------LQRQDLAQArqWWQDNLRGFERPTPIPSD--RPFLREHAGDS 3474
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4096 M-------HFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRP--HADLEPIIGMFVNTLA 4166
Cdd:PRK05691 3475 GgmvvgdcYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvsMPQMQRTVGLFINSIA 3554
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4167 MR-NYPEKGK--TFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIARDlsrNPLFDTMFVLQNT--EQEQLEINDVTFKP 4241
Cdd:PRK05691 3555 LRvQLPAAGQrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKG---QPLFDSLFVFENApvEVSVLDRAQSLNAS 3631
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4242 YPNGHTMAKFdlTLTAV-EEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTkEEERDIqqLF 4320
Cdd:PRK05691 3632 SDSGRTHTNF--PLTAVcYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLG-EQERDF--LL 3706
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4321 NDTAVAEKRIP--TTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIG 4398
Cdd:PRK05691 3707 DGCNRSERDYPleQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGM 3786
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4399 ILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCA-----GHAIPPLFEG----EVLLLDDPLLYQGRTDNLNLSC 4469
Cdd:PRK05691 3787 IVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAacreqARALLDELGCanrpRLLVWEEVQAGEVASHNPGIYS 3866
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4470 SENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQL-RFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAK 4548
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALsEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIA 3946
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4549 RDIRQLNDFVRTHGIQT-AFLPTAFLKLLASEKHYFEPfaecVDHIIAAGEQLiATRMLRDMLARH-QVTLHNHYGPSE- 4625
Cdd:PRK05691 3947 HDPQGLLAHVQAQGITVlESVPSLIQGMLAEDRQALDG----LRWMLPTGEAM-PPELARQWLQRYpQIGLVNAYGPAEc 4021
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4626 THVVTMYTVD-PDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDS-NQ 4703
Cdd:PRK05691 4022 SDDVAFFRVDlASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGApGE 4101
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4704 RMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSdLYAYFTA-----EQS 4776
Cdd:PRK05691 4102 RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQaeVREAAVAVQEGVNGKH-LVGYLVPhqtvlAQG 4180
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4777 LSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQTGTDYVAPRTNMEEQLICIWQDVLKVKEIG 4856
Cdd:PRK05691 4181 ALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVG 4260
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 4857 VKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQCPTVGEMAQAI 4904
Cdd:PRK05691 4261 VHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
3286-3782 1.39e-143

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 456.63  E-value: 1.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3286 HELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDP 3365
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3366 DSPSERIRYILNDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIEH 3445
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLT----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3446 RQVIHLIEGlsRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITD-GTP 3524
Cdd:cd17645   127 HNLVNLCEW--HRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFlPTG 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3525 AHLKLLiaagDLQGVTLQHLLIGGEALSKTTVNKLKqlfgehgaapgITNVYGPTETCVDASLFNIEcssdawaRSQNYV 3604
Cdd:cd17645   205 AAEQFM----QLDNQSLRVLLTGGDKLKKIERKGYK-----------LVNNYGPTENTVVATSFEID-------KPYANI 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 PIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYI 3684
Cdd:cd17645   263 PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFL 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3685 GRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQ 3764
Cdd:cd17645   343 GRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVH 422
                         490
                  ....*....|....*...
gi 166797876 3765 LDKMPLTPNGKLNRQLLP 3782
Cdd:cd17645   423 LKALPLTANGKVDRKALP 440
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3297-3781 4.27e-142

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 452.53  E-value: 4.27e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLS 3456
Cdd:cd17643    81 ADSGPSLLLT----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RQVYsaYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDL 3536
Cdd:cd17643   127 RWFG--FNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADR 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3537 QG---VTLQHLLIGGEALsktTVNKLKQLFGEHGA-APGITNVYGPTETCVDASLFNIecsSDAWARSQNYVPIGKPLGR 3612
Cdd:cd17643   205 DGrdpLALRYVIFGGEAL---EAAMLRPWAGRFGLdRPQLVNMYGITETTVHVTFRPL---DAADLPAAAASPIGRPLPG 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3613 NRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPE-DRMYRTGDLARLLPDGNIEYIGRIDHQV 3691
Cdd:cd17643   279 LRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPgSRMYRTGDLARRLPDGELEYLGRADEQV 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3692 KIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAAD--KTIQISELRKRMARHLPGYMIPAHFVQLDKMP 3769
Cdd:cd17643   359 KIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALP 438
                         490
                  ....*....|..
gi 166797876 3770 LTPNGKLNRQLL 3781
Cdd:cd17643   439 LTVNGKLDRAAL 450
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
3297-3781 3.73e-141

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 450.59  E-value: 3.73e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFyHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLS 3456
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA-AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RQVysAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAG-- 3534
Cdd:cd12116   160 ERL--GLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGwq 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3535 DLQGVTlqhLLIGGEALSKTtvnkLKQLFGEHGAApgITNVYGPTETCVDASlfniecssdaWAR---SQNYVPIGKPLG 3611
Cdd:cd12116   238 GRAGLT---ALCGGEALPPD----LAARLLSRVGS--LWNLYGPTETTIWST----------AARvtaAAGPIPIGRPLA 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3612 RNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPED-RMYRTGDLARLLPDGNIEYIGRIDHQ 3690
Cdd:cd12116   299 NTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGsRLYRTGDLVRRRADGRLEYLGRADGQ 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3691 VKIQGFRIELGEIESVMLNVPDIQEaAAAALKDADDEYYLCGYF--AADKTIQISELRKRMARHLPGYMIPAHFVQLDKM 3768
Cdd:cd12116   379 VKIRGHRIELGEIEAALAAHPGVAQ-AAVVVREDGGDRRLVAYVvlKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDAL 457
                         490
                  ....*....|...
gi 166797876 3769 PLTPNGKLNRQLL 3781
Cdd:cd12116   458 PLTANGKLDRKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
3297-3782 1.40e-140

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 447.47  E-value: 1.40e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLS 3456
Cdd:cd17652    81 ADARPALLLT----------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RqvysAYDAELNIAML--APYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLiAAG 3534
Cdd:cd17652   127 A----AFDVGPGSRVLqfASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL-PPD 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3535 DLQGvtLQHLLIGGEALSKTTVNKLkqlfgehgaAPG--ITNVYGPTETCVDASLfnIECSSDAwarsqNYVPIGKPLGR 3612
Cdd:cd17652   202 DLPD--LRTLVVAGEACPAELVDRW---------APGrrMINAYGPTETTVCATM--AGPLPGG-----GVPPIGRPVPG 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3613 NRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRMYRTGDLARLLPDGNIEYIGRIDHQV 3691
Cdd:cd17652   264 TRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQV 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3692 KIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYF--AADKTIQISELRKRMARHLPGYMIPAHFVQLDKMP 3769
Cdd:cd17652   344 KIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVvpAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALP 423
                         490
                  ....*....|...
gi 166797876 3770 LTPNGKLNRQLLP 3782
Cdd:cd17652   424 LTPNGKLDRRALP 436
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1777-2262 2.87e-140

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 447.00  E-value: 2.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1777 HQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDP 1856
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1857 EYPQDRIRYMLDDSQAGIVLMQRDvrkqlayegvtvllddessyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIEH 1936
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTNPD----------------------------------DLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1937 GGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTAL--LESIVRDPRVDIIKL-TPAH 2013
Cdd:cd17645   127 HNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLdaLNDYFNQEGITISFLpTGAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2014 LQVLKemniADQTAVRRMIVGGENLSTRLARSIheqfegriEICNEYGPTETVVGCMIYRYDAAKdrrESVPIGTAAANT 2093
Cdd:cd17645   207 EQFMQ----LDNQSLRVLLTGGDKLKKIERKGY--------KLVNNYGPTENTVVATSFEIDKPY---ANIPIGKPIDNT 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2094 SIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKI 2173
Cdd:cd17645   272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2174 RGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSN 2253
Cdd:cd17645   352 RGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTAN 431

                  ....*....
gi 166797876 2254 GKINKKGLP 2262
Cdd:cd17645   432 GKVDRKALP 440
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
3297-3782 3.76e-139

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 444.12  E-value: 3.76e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYcgklqddigfsgtcidlmeehfyHEKDsslalsyqssQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLS 3456
Cdd:cd17649    81 EDSGAGLLLT-----------------------HHPR----------QLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RqVY--SAYDAELNiamLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLI--A 3532
Cdd:cd17649   128 E-RYglTPGDRELQ---FASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAeeA 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3533 AGDLQGV--TLQHLLIGGEALSkttVNKLKQLFGEHGAapgITNVYGPTETCVDASLFniECSSDAwARSQNYVPIGKPL 3610
Cdd:cd17649   204 DRTGDGRppSLRLYIFGGEALS---PELLRRWLKAPVR---LFNAYGPTEATVTPLVW--KCEAGA-ARAGASMPIGRPL 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3611 GRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF-VPEDRMYRTGDLARLLPDGNIEYIGRIDH 3689
Cdd:cd17649   275 GGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDH 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3690 QVKIQGFRIELGEIESVMLNVPDIQEaAAAALKDADDEYYLCGYFAADKTIQISELRKRMARH----LPGYMIPAHFVQL 3765
Cdd:cd17649   355 QVKIRGFRIELGEIEAALLEHPGVRE-AAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTAlrasLPDYMVPAHLVFL 433
                         490
                  ....*....|....*..
gi 166797876 3766 DKMPLTPNGKLNRQLLP 3782
Cdd:cd17649   434 ARLPLTPNGKLDRKALP 450
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
4333-4819 5.65e-139

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 444.19  E-value: 5.65e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPI 4412
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4413 DPELPEKRRAFMLKDSGADVLLTcaghaipplfegevlllddpllyqgrtdnlnlscSENDLMYVIYTSGTTGQPKGVQL 4492
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLT----------------------------------QPENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4493 EHKTMTNL-LAYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTA 4571
Cdd:cd17644   127 EHQSLVNLsHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4572 FLKLLASE-KHYFEPFAECVDHIIAAGEQLIATR--MLRDMLaRHQVTLHNHYGPSETHV-VTMYTVDPDTDQELQ--PI 4645
Cdd:cd17644   207 YWHLLVLElLLSTIDLPSSLRLVIVGGEAVQPELvrQWQKNV-GNFIQLINVYGPTEATIaATVCRLTQLTERNITsvPI 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4646 GKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSN--QRMYKTGDLARYLPEGNIEYA 4723
Cdd:cd17644   286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSesERLYKTGDLARYLPDGNIEYL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4724 GRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA--EQSLSISQLKEKLAGQIPGYMIPSYF 4799
Cdd:cd17644   366 GRIDNQVKIRGFRIELGEIEAVLSQHndVKTAVVIVREDQPGNKRLVAYIVPhyEESPSTVELRQFLKAKLPDYMIPSAF 445
                         490       500
                  ....*....|....*....|
gi 166797876 4800 IQLEKLPLTGNGKVNRRALP 4819
Cdd:cd17644   446 VVLEELPLTPNGKIDRRALP 465
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
4346-4818 4.77e-136

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 435.20  E-value: 4.77e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGAdvlltcaghaipplfegeVLLLDDPllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAyeq 4505
Cdd:cd17643    81 ADSGP------------------SLLLTDP----------------DDLAYVIYTSGSTGRPKGVVVSHANVLALFA--- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4506 dHTQLRF-----DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGI----QTaflPTAFLKLL 4576
Cdd:cd17643   124 -ATQRWFgfnedDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVtvlnQT---PSAFYQLV 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4577 ASEKHYFEPFAEcVDHIIAAGEQLIAtRMLRDMLARH---QVTLHNHYGPSETHV-VTMYTVDPD--TDQELQPIGKPIS 4650
Cdd:cd17643   200 EAADRDGRDPLA-LRYVIFGGEALEA-AMLRPWAGRFgldRPQLVNMYGITETTVhVTFRPLDAAdlPAAAASPIGRPLP 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4651 NTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDS-NQRMYKTGDLARYLPEGNIEYAGRRDHQ 4729
Cdd:cd17643   278 GLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQ 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4730 VKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA--EQSLSISQLKEKLAGQIPGYMIPSYFIQLEKL 4805
Cdd:cd17643   358 VKIRGFRIELGEIEAALATHpsVRDAAVIVREDEPGDTRLVAYVVAddGAAADIAELRALLKELLPDYMVPARYVPLDAL 437
                         490
                  ....*....|...
gi 166797876 4806 PLTGNGKVNRRAL 4818
Cdd:cd17643   438 PLTVNGKLDRAAL 450
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
265-749 1.36e-134

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 432.35  E-value: 1.36e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  265 VYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLD 344
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  345 PEYPKERLQYLLHDADADVLLVQHHlknslafdgpvidlndeasyhadcsllspvaghSHLAYVIYTSGTTGKPKGVMVE 424
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSSP---------------------------------SDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  425 HGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAiqNAIKQERITHFSTSPrl 504
Cdd:cd05918   128 HRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLA--GFINRLRVTWAFLTP-- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  505 lkTMIEQMNREDFIHVQHVVVGGEQLETDTVEKlhsLQPRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHqAY 584
Cdd:cd05918   204 --SVARLLDPEDVPSLRTLVLGGEALTQSDVDT---WADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CW 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  585 IL--GAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHL-------HVPGQKMYKTGDLARWLPDGRIEYLGRI 655
Cdd:cd05918   278 VVdpDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRK 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  656 DHQVKIRGYRIEIGEVEAAM---FNLENVREAAVVAREDADGAKQLYAYYVGEPSLT-------------------AAQF 713
Cdd:cd05918   358 DTQVKIRGQRVELGEIEHHLrqsLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefralVAEL 437
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 166797876  714 REELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05918   438 RSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
277-750 1.59e-134

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 431.05  E-value: 1.59e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCG-VQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYL 355
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  356 LHDADADVLlvqhhlknslafdgpvidlndeasyhadcsllspVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSL-QW 434
Cdd:cd17648    81 LEDTGARVV----------------------------------ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRtSL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  435 KKAFFKHSPAD-RVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKtMIEQMN 513
Cdd:cd17648   127 SERYFGRDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQ-QYDLAR 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  514 REdfiHVQHVVVGGEQLETDTVEKLHSlQPRIRINNEYGPTENSV---VSTFHPVQSADEqiTIGSPVANHQAYILGAHH 590
Cdd:cd17648   206 LP---HLKRVDAAGEEFTAPVFEKLRS-RFAGLIINAYGPTETTVtnhKRFFPGDQRFDK--SLGRPVRNTKCYVLNDAM 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  591 QIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH-LHVPGQK-------MYKTGDLARWLPDGRIEYLGRIDHQVKIR 662
Cdd:cd17648   280 KRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNpFQTEQERargrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIR 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  663 GYRIEIGEVEAAMFNLENVREAAVVAREDADGA-----KQLYAYYVGEP-SLTAAQFREELSRELPNYMIPSRFIPLERI 736
Cdd:cd17648   360 GQRIEPGEVEAALASYPGVRECAVVAKEDASQAqsriqKYLVGYYLPEPgHVPESDLLSFLRAKLPRYMVPARLVRLEGI 439
                         490
                  ....*....|....
gi 166797876  737 PLTSNGKIDLKALP 750
Cdd:cd17648   440 PVTINGKLDVRALP 453
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
3887-4316 1.72e-134

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 430.99  E-value: 1.72e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKM-ADGEPVQYVLDHAAFEAEW 3965
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3966 YQG---EEDDADLYIRQFIR-----PFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYE----G 4033
Cdd:pfam00668   85 IDIsdlSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqllkG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4034 ETLPPLRIQ-YKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLA 4112
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4113 SQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAY 4192
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4193 EHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNT-----EQEQLEINDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFT 4267
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgqdsQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTIK 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 166797876  4268 LEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELARLNMMTKEEERDI 4316
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
4346-4818 7.16e-134

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 428.81  E-value: 7.16e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGADVLLTcaghaipplfegevllldDPllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLEHKTMTNL-LAYE 4504
Cdd:cd17650    81 EDSGAKLLLT------------------QP----------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAaHAWR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4505 QDHTQLRFD-RVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTA-FLPTAFLKLLAS-EKH 4581
Cdd:cd17650   127 REYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMeSTPALIRPVMAYvYRN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4582 YFEPFAEcvdHIIAAGEQLIATRMLRDMLAR---HQVTLhNHYGPSETHVVTMY---TVDPDTDQELQPIGKPISNTEIF 4655
Cdd:cd17650   207 GLDLSAM---RLLIVGSDGCKAQDFKTLAARfgqGMRII-NSYGVTEATIDSTYyeeGRDPLGDSANVPIGRPLPNTAMY 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4656 ILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGY 4735
Cdd:cd17650   283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:cd17650   363 RIELGEIESQLARHpaIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442

                  ....*
gi 166797876 4814 NRRAL 4818
Cdd:cd17650   443 DRRAL 447
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
4346-4818 1.32e-133

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 429.02  E-value: 1.32e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGADVLLTCAghAIPPLFEGEVLLLDDPLLYQGRT-DNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYE 4504
Cdd:cd12116    81 EDAEPALVLTDD--ALPDRLPAGLPVLLLALAAAAAApAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4505 QDHTQLR-FDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGI---QTAflPTAFLKLLASEK 4580
Cdd:cd12116   159 RERLGLGpGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSItvmQAT--PATWRMLLDAGW 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4581 HYFEPFaecvdHIIAAGEQLIATrmLRDMLARHQVTLHNHYGPSETHV-VTMYTVDPDTDQelQPIGKPISNTEIFILNE 4659
Cdd:cd12116   237 QGRAGL-----TALCGGEALPPD--LAARLLSRVGSLWNLYGPTETTIwSTAARVTAAAGP--IPIGRPLANTQVYVLDA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4660 AGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPY-DSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVE 4738
Cdd:cd12116   308 ALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4739 LGEVEAALLKH--VQEAVVLAKENtDGQSDLYAYFTAE--QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVN 4814
Cdd:cd12116   388 LGEIEAALAAHpgVAQAAVVVRED-GGDRRLVAYVVLKagAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466

                  ....
gi 166797876 4815 RRAL 4818
Cdd:cd12116   467 RKAL 470
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
277-749 1.35e-133

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 429.38  E-value: 1.35e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  277 PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQHH--LKNSLAFDGPVIDLNDEAsyhADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQW 434
Cdd:cd12114    81 ADAGARLVLTDGPdaQLDVAVFDVLILDLDALA---APAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  435 KKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQM-- 512
Cdd:cd12114   158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLea 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  513 NREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ---ITIGSPVANHQAYILGAH 589
Cdd:cd12114   238 AQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDwrsIPYGRPLANQRYRVLDPR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  590 HQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHvpGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIG 669
Cdd:cd12114   318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD--GERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  670 EVEAAMFNLENVREAAVVAREDaDGAKQLYAYYV---GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDL 746
Cdd:cd12114   396 EIEAALQAHPGVARAVVVVLGD-PGGKRLAAFVVpdnDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474

                  ...
gi 166797876  747 KAL 749
Cdd:cd12114   475 AAL 477
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
4346-4819 6.73e-127

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 409.07  E-value: 6.73e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGADVLLTcaghaipplfegevlllddpllYQGRTdnlnlscsendLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQ 4505
Cdd:cd17649    81 EDSGAGLLLT----------------------HHPRQ-----------LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4506 DHTQLRF-DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASE-KHYF 4583
Cdd:cd17649   128 ERYGLTPgDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDRTG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4584 EPFAECVDHIIAAGEQLiATRMLRDMLARHqVTLHNHYGPSETHVVTM-YTVDPDTDQ--ELQPIGKPISNTEIFILNEA 4660
Cdd:cd17649   208 DGRPPSLRLYIFGGEAL-SPELLRRWLKAP-VRLFNAYGPTEATVTPLvWKCEAGAARagASMPIGRPLGGRSAYILDAD 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4661 GTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPY-DSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVEL 4739
Cdd:cd17649   286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4740 GEVEAALLKH--VQEAVVLAkENTDGQSDLYAYFTAE----QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:cd17649   366 GEIEAALLEHpgVREAAVVA-LDGAGGKQLVAYVVLRaaaaQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444

                  ....*.
gi 166797876 4814 NRRALP 4819
Cdd:cd17649   445 DRKALP 450
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
3285-3781 5.05e-126

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 406.32  E-value: 5.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3285 IHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPID 3364
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3365 PDSPSERIRYILNDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIE 3444
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLT----------------------------------DPDDLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3445 HRQVIHLIeGLSRQVYSAydaELNIAMLA--PYYFDASVQQMYASLLSGHTLFIVpkeivSDGAALCRYYRQHSIDITDG 3522
Cdd:cd12115   127 HRNAAAFL-QWAAAAFSA---EELAGVLAstSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINT 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3523 TPAHLKLLIAAGDLQGvTLQHLLIGGEALSKTTVNKLkqlfgeHGAAPG--ITNVYGPTETCVDASLFNIECSSDAWars 3600
Cdd:cd12115   198 VPSAAAELLRHDALPA-SVRVVNLAGEPLPRDLVQRL------YARLQVerVVNLYGPSEDTTYSTVAPVPPGASGE--- 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3601 qnyVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGN 3680
Cdd:cd12115   268 ---VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGL 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3681 IEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAAD--KTIQISELRKRMARHLPGYMI 3758
Cdd:cd12115   345 LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMV 424
                         490       500
                  ....*....|....*....|...
gi 166797876 3759 PAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd12115   425 PSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1788-2261 2.18e-125

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 405.50  E-value: 2.18e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDVRKQLAyEGVTVLLDDESSyhQDGSDLAPISDV--SHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWW 1945
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDV-AVFDVLILDLDA--LAAPAPPPPVDVapDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1946 AKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDK--TALLESIVRDPRVDIIKLTPAHLQVLKEMNIA 2023
Cdd:cd12114   158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRrdPAHWAELIERHGVTLWNSVPALLEMLLDVLEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2024 DQTAVR--RMI-VGGENLSTRLARSIHEQFEGrIEICNEYGPTETVVGCMIYRYDAAKDRRESVPIGTAAANTSIYVLDE 2100
Cdd:cd12114   238 AQALLPslRLVlLSGDWIPLDLPARLRALAPD-ARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2101 NMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPfePGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIEL 2180
Cdd:cd12114   317 RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2181 GEIEAALLQEEVIKEAVVTAREDVHGfKQLCAYYVSGGQ---TTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKIN 2257
Cdd:cd12114   395 GEIEAALQAHPGVARAVVVVLGDPGG-KRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473

                  ....
gi 166797876 2258 KKGL 2261
Cdd:cd12114   474 RAAL 477
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1788-2262 6.41e-125

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 403.32  E-value: 6.41e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKG-VQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYM 1866
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1867 LDDSQAGIVlmqrdvrkqlayegvtvllddessyhqdgsdlapISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWA 1946
Cdd:cd17648    81 LEDTGARVV----------------------------------ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1947 KEVY-VKGEKANFPL-YSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTA--LLESIVRDPRVDIIKLTPAhlqVLKEMNI 2022
Cdd:cd17648   127 SERYfGRDNGDEAVLfFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDpdRFYAYINREKVTYLSGTPS---VLQQYDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2023 ADQTAVRRMIVGGENLSTRLARSIHEQFEGRieICNEYGPTETVVGCMIYRYdaAKDRRESVPIGTAAANTSIYVLDENM 2102
Cdd:cd17648   204 ARLPHLKRVDAAGEEFTAPVFEKLRSRFAGL--IINAYGPTETTVTNHKRFF--PGDQRFDKSLGRPVRNTKCYVLNDAM 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2103 KPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEP--------GAKMYKTGDLAKWLADGNIEYAGRIDEQVKIR 2174
Cdd:cd17648   280 KRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIR 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2175 GYRIELGEIEAALLQEEVIKEAVVTAREDVHGF-----KQLCAYYVSG-GQTTAARLRKQLSQTLASYMVPAYFIELDEM 2248
Cdd:cd17648   360 GQRIEPGEVEAALASYPGVRECAVVAKEDASQAqsriqKYLVGYYLPEpGHVPESDLLSFLRAKLPRYMVPARLVRLEGI 439
                         490
                  ....*....|....
gi 166797876 2249 PLTSNGKINKKGLP 2262
Cdd:cd17648   440 PVTINGKLDVRALP 453
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
4334-4818 1.60e-124

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 402.08  E-value: 1.60e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4334 IHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPID 4413
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4414 PELPEKRRAFMLKDSGADVLLTcaghaipplfegevllldDPllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLE 4493
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLT------------------DP----------------DDLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4494 HKTMTNLLAYEQDH---TQLRfdRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNeakrdIRQLNDFVRTHG---IQTaf 4567
Cdd:cd12115   127 HRNAAAFLQWAAAAfsaEELA--GVLASTSICFDLSVFELFGPLATGGKVVLADN-----VLALPDLPAAAEvtlINT-- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4568 LPTAFLKLLASEKhyFEPFAECVDhiiAAGEQLIATrMLRDMLARHQVT-LHNHYGPSETHVVTMYTVDPDTDQELQPIG 4646
Cdd:cd12115   198 VPSAAAELLRHDA--LPASVRVVN---LAGEPLPRD-LVQRLYARLQVErVVNLYGPSEDTTYSTVAPVPPGASGEVSIG 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4647 KPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRR 4726
Cdd:cd12115   272 RPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRA 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4727 DHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLS--ISQLKEKLAGQIPGYMIPSYFIQL 4802
Cdd:cd12115   352 DNQVKVRGFRIELGEIEAALRSIpgVREAVVVAIGDAAGERRLVAYIVAEPGAAglVEDLRRHLGTRLPAYMVPSRFVRL 431
                         490
                  ....*....|....*.
gi 166797876 4803 EKLPLTGNGKVNRRAL 4818
Cdd:cd12115   432 DALPLTPNGKIDRSAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
4334-4818 1.69e-124

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 403.08  E-value: 1.69e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4334 IHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPID 4413
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4414 PELPEKRRAFMLKDSGADVLLTCaghaipplfegevlllddpllyqgrtdnlnlscSENDLMYVIYTSGTTGQPKGVQLE 4493
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTS---------------------------------SPSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4494 HKTM-TNLLAYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDirQLNDFVRTHGIQTAFLPTAF 4572
Cdd:cd05918   128 HRALsTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTPSV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4573 LKLLASEKhyfepfAECVDHIIAAGEQliatrMLRDMLAR--HQVTLHNHYGPSETHV-VTMYTVDPDTDQELqpIGKPI 4649
Cdd:cd05918   206 ARLLDPED------VPSLRTLVLGGEA-----LTQSDVDTwaDRVRLINAYGPAECTIaATVSPVVPSTDPRN--IGRPL 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4650 SNTeIFILNEAGT--LQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYD-------SNQRMYKTGDLARYLPEGNI 4720
Cdd:cd05918   273 GAT-CWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWlkqegsgRGRRLYRTGDLVRYNPDGSL 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4721 EYAGRRDHQVKIRGYRVELGEVEAALLKHVQE---------------------AVVLAKENTDGQSDLYAYF---TAEQS 4776
Cdd:cd05918   352 EYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGakevvvevvkpkdgssspqlvAFVVLDGSSSGSGDGDSLFlepSDEFR 431
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 166797876 4777 LSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05918   432 ALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
3297-3782 6.28e-124

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 400.62  E-value: 6.28e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKG-VQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYI 3375
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3376 LNDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGL 3455
Cdd:cd17648    81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3456 SRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLiaagD 3535
Cdd:cd17648   127 SERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY----D 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3536 LQGVT-LQHLLIGGEALSKTTVNKLKQLFgehgaaPG-ITNVYGPTETcvdaSLFNIECSSDAWARSQNyvPIGKPLGRN 3613
Cdd:cd17648   203 LARLPhLKRVDAAGEEFTAPVFEKLRSRF------AGlIINAYGPTET----TVTNHKRFFPGDQRFDK--SLGRPVRNT 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3614 RMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPED--------RMYRTGDLARLLPDGNIEYIG 3685
Cdd:cd17648   271 KCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3686 RIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEY-----YLCGYFAADK-TIQISELRKRMARHLPGYMIP 3759
Cdd:cd17648   351 RNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkYLVGYYLPEPgHVPESDLLSFLRAKLPRYMVP 430
                         490       500
                  ....*....|....*....|...
gi 166797876 3760 AHFVQLDKMPLTPNGKLNRQLLP 3782
Cdd:cd17648   431 ARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
267-749 5.71e-122

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 393.98  E-value: 5.71e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  267 QLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPE 346
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  347 YPKERLQYLLHDADAdvllvqhhlknslafdgpvidlndeasyhadCSLLSPVAGHShLAYVIYTSGTTGKPKGVMVEHG 426
Cdd:cd17653    81 LPSARIQAILRTSGA-------------------------------TLLLTTDSPDD-LAYIIFTSGSTGIPKGVMVPHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  427 GIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLlpnEENKETFAiqNAIKQERITHfSTsPRLLK 506
Cdd:cd17653   129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL---ADPSDPFA--HVARTVDALM-ST-PSILS 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  507 TMieqmNREDFIHVQHVVVGGEQLETDTVEKLhslQPRIRINNEYGPTENSVVSTFHPVqSADEQITIGSPVANHQAYIL 586
Cdd:cd17653   202 TL----SPQDFPNLKTIFLGGEAVPPSLLDRW---SPGRRLYNAYGPTECTISSTMTEL-LPGQPVTIGKPIPNSTCYIL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  587 GAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRI 666
Cdd:cd17653   274 DADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  667 EIGEVEAAMFNLEN-VREAAVVAREDadgakQLYAYYVGEpSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:cd17653   354 NLEEIEEVVLQSQPeVTQAAAIVVNG-----RLVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427

                  ....
gi 166797876  746 LKAL 749
Cdd:cd17653   428 RKAL 431
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2824-3269 3.55e-121

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 392.47  E-value: 3.55e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2824 VENVYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWNDTPLQIVYKTQTP 2903
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2904 QIHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSA 2983
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2984 LQEGREPEPLSAVPYSDYIEWLDR----QDQGAAKRYWSGYLEGYKGETTLLHKIAQHEQKEYAYANLICRFDHEQTKQL 3059
Cdd:pfam00668  161 LLKGEPLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3060 QQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAeiPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQ 3139
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3140 NALASQSYDTYPLYEIQAQTEQKQN-----LIDHIMIFENYPiGQQAEETGHHGTELNITN-FHMQEHSHYDLNVVVIP- 3212
Cdd:pfam00668  319 DLLSAEPHQGYPFGDLVNDLRLPRDlsrhpLFDPMFSFQNYL-GQDSQEEEFQLSELDLSVsSVIEEEAKYDLSLTASEr 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  3213 GKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLL 3269
Cdd:pfam00668  398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1316-1761 5.03e-121

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 392.08  E-value: 5.03e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1316 ENIYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPLQIIFKTKKIG 1395
Cdd:pfam00668    2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1396 FQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFAL 1475
Cdd:pfam00668   82 LEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1476 LQQKQPEQSSITPYSQYIEW----LGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMK 1551
Cdd:pfam00668  162 LKGEPLPLPPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1552 RTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQER 1631
Cdd:pfam00668  242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1632 AVASQKFETHPLYDIQARTTQKQD-----LITHLMIFENYPVDQYMESIGRQNGTSITISNVqMEEQTNYDFNLTVIP-G 1705
Cdd:pfam00668  320 LLSAEPHQGYPFGDLVNDLRLPRDlsrhpLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSV-IEEEAKYDLSLTASErG 398
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  1706 DEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRTLL 1761
Cdd:pfam00668  399 GGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1776-2261 7.95e-121

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 392.68  E-value: 7.95e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPID 1855
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1856 PEYPQDRIRYMLDDSQAGIVLmqrdvrkqlayegvtvllddessyhqdgsdlapISDVSHLAYVIYTSGSTGRPKGVLIE 1935
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVL---------------------------------TSSPSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1936 HGGL-TNYIWWAKEVYVKGEKANFpLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTALLESIVRDPRVDIIKLTPAhl 2014
Cdd:cd05918   128 HRALsTSALAHGRALGLTSESRVL-QFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPS-- 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2015 qVLKEMNIADQTAVRRMIVGGENLSTRLArsihEQFEGRIEICNEYGPTETVVGCMIYRYDAAKDRREsvpIGTAAAnTS 2094
Cdd:cd05918   205 -VARLLDPEDVPSLRTLVLGGEALTQSDV----DTWADRVRLINAYGPAECTIAATVSPVVPSTDPRN---IGRPLG-AT 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2095 IYVLD-ENM-KPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDP-------FEPGAKMYKTGDLAKWLADGNIEYAG 2165
Cdd:cd05918   276 CWVVDpDNHdRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVG 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2166 RIDEQVKIRGYRIELGEIEAALLQ-EEVIKEAVVTA--REDVHGFKQLCAYYVSGG-------------------QTTAA 2223
Cdd:cd05918   356 RKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVvkPKDGSSSPQLVAFVVLDGsssgsgdgdslflepsdefRALVA 435
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 166797876 2224 RLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05918   436 ELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
273-749 1.16e-120

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 390.84  E-value: 1.16e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVqhhlknslafdgpvidlndeasyhadcsllspvAGHShLAYVIYTSGTTGKPKGVMVEHGGIVNSL 432
Cdd:cd05945    81 REILDAAKPALLIA---------------------------------DGDD-NAYIIFTSGSTGRPKGVQISHDNLVSFT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  433 QWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAIKQERITHFSTSPRLLK--TMIE 510
Cdd:cd05945   127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAmcLLSP 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  511 QMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFH----PVQSADEQITIGSPVANHQAYIL 586
Cdd:cd05945   207 TFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevtpEVLDGYDRLPIGYAKPGAKLVIL 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  587 GAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVehlHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRI 666
Cdd:cd05945   287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  667 EIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQ---FREELSRELPNYMIPSRFIPLERIPLTSNGK 743
Cdd:cd05945   364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLtkaIKAELAERLPPYMIPRRFVYLDELPLNANGK 443

                  ....*.
gi 166797876  744 IDLKAL 749
Cdd:cd05945   444 IDRKAL 449
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3285-3781 1.30e-118

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 386.13  E-value: 1.30e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3285 IHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPID 3364
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3365 PDSPSERIRYILNDSsisvllycgklqddigfsgtcidlmeehfyhekDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIE 3444
Cdd:cd05918    81 PSHPLQRLQEILQDT---------------------------------GAKVVLTSSPSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3445 HRQVIHLIEGLSRqvysAYDAELNIAML--APYYFDASVQQMYASLLSGHTLFIVPKE-IVSDGAALCRYYRqhsIDITD 3521
Cdd:cd05918   128 HRALSTSALAHGR----ALGLTSESRVLqfASYTFDVSILEIFTTLAAGGCLCIPSEEdRLNDLAGFINRLR---VTWAF 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3522 GTPAHLKLLiaagDLQGV-TLQHLLIGGEALSKTTVNKLkqlfgehgaAPGIT--NVYGPTETCVDASLFNIECSSDAwa 3598
Cdd:cd05918   201 LTPSVARLL----DPEDVpSLRTLVLGGEALTQSDVDTW---------ADRVRliNAYGPAECTIAATVSPVVPSTDP-- 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3599 rsQNyvpIGKPLGrNRMYILDSKK--RLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADP-------FVPEDRMYRT 3669
Cdd:cd05918   266 --RN---IGRPLG-ATCWVVDPDNhdRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRT 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3670 GDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEA---AAAALKDADDEYYLCGYFAADKT------- 3739
Cdd:cd05918   340 GDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEvvvEVVKPKDGSSSPQLVAFVVLDGSssgsgdg 419
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 3740 ------------IQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05918   420 dslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
4922-5344 2.80e-118

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 384.38  E-value: 2.80e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4922 DVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTV-VEMVREEAVQVIKSQVEFSM 5000
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVfIRQENGEPVQVILEERPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  5001 ERYE---ATADEVEECFRAFVR-----PFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYD--- 5069
Cdd:pfam00668   83 EIIDisdLSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqll 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  5070 -GKELAPLRIQ-YKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQ 5147
Cdd:pfam00668  163 kGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  5148 LEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLK 5227
Cdd:pfam00668  243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLS 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  5228 AFEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQTDIEVD--SLAVRPYEQT---ETAAKFDLQLNFLIDQDEIQ 5302
Cdd:pfam00668  323 AEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEefQLSELDLSVSsviEEEAKYDLSLTASERGGGLT 402
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 166797876  5303 GSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQL 5344
Cdd:pfam00668  403 IKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDL 444
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1778-2261 1.48e-117

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 381.27  E-value: 1.48e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDSQAGIVLmqrdvrkqlayegvtvllddessyhqdgsdlaPISDVSHLAYVIYTSGSTGRPKGVLIEHG 1937
Cdd:cd17653    81 LPSARIQAILRTSGATLLL--------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1938 GLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKtalLESIVRDprVDIIKLTPAHLQVL 2017
Cdd:cd17653   129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDP---FAHVART--VDALMSTPSILSTL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2018 KEmniADQTAVRRMIVGGENLSTRLARSiheqFEGRIEICNEYGPTETVVGCMIYRYDAakdrRESVPIGTAAANTSIYV 2097
Cdd:cd17653   204 SP---QDFPNLKTIFLGGEAVPPSLLDR----WSPGRRLYNAYGPTECTISSTMTELLP----GQPVTIGKPIPNSTCYI 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2098 LDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYR 2177
Cdd:cd17653   273 LDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFR 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2178 IELGEIEAALLQEEvikEAVVTAREDVHGfKQLCAYYVSggQTTA-ARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKI 2256
Cdd:cd17653   353 INLEEIEEVVLQSQ---PEVTQAAAIVVN-GRLVAFVTP--ETVDvDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426

                  ....*
gi 166797876 2257 NKKGL 2261
Cdd:cd17653   427 DRKAL 431
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
265-752 5.66e-115

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 374.53  E-value: 5.66e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  265 VYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLD 344
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  345 PEYPKERLQYLLHDADADVLLVqhhlknslafdgpvidlndeasyhadcsllspvaghshlAYVIYTSGTTGKPKGVMVE 424
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  425 HGGIVNSLQWKKAFFKHSPADRVLVLYPYVFD-AFILNFFGPLISGATLHLLPNEENKETFAiqnAIKQERITHFSTSPr 503
Cdd:COG0318   122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPRFDPERVLE---LIERERVTVLFGVP- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  504 llkTMIEQM------NREDFIHVQHVVVGGEQLETDTVEKLHSLQpRIRINNEYGPTENSVVSTFHPVQSADEQI-TIGS 576
Cdd:COG0318   198 ---TMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPgSVGR 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  577 PVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHlhvpgqkMYKTGDLARWLPDGRIEYLGRID 656
Cdd:COG0318   274 PLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVGRKK 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  657 HQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLE 734
Cdd:COG0318   347 DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPgaELDAEELRAFLRERLARYKVPRRVEFVD 426
                         490
                  ....*....|....*...
gi 166797876  735 RIPLTSNGKIDLKALPAA 752
Cdd:COG0318   427 ELPRTASGKIDRRALRER 444
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
4346-4819 2.19e-113

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 370.19  E-value: 2.19e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGA-CTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFM 4424
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4425 LKDSGADVLLTcaghaipplfegevlllddpllyqgrtdnlnlscSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLlaye 4504
Cdd:cd17648    81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNL---- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4505 qdHTQL--RFD-------RVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIqtaflptAFLKL 4575
Cdd:cd17648   123 --RTSLseRYFgrdngdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKV-------TYLSG 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4576 LASEKHYFEpFAECvDH---IIAAGEQLIATRmLRDMLARHQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNT 4652
Cdd:cd17648   194 TPSVLQQYD-LARL-PHlkrVDAAGEEFTAPV-FEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNT 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4653 EIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDS--------NQRMYKTGDLARYLPEGNIEYAG 4724
Cdd:cd17648   271 KCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4725 RRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKE-----NTDGQSDLYAYFTAEQ-SLSISQLKEKLAGQIPGYMIP 4796
Cdd:cd17648   351 RNDFQVKIRGQRIEPGEVEAALASYpgVRECAVVAKEdasqaQSRIQKYLVGYYLPEPgHVPESDLLSFLRAKLPRYMVP 430
                         490       500
                  ....*....|....*....|...
gi 166797876 4797 SYFIQLEKLPLTGNGKVNRRALP 4819
Cdd:cd17648   431 ARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
4336-4818 2.36e-113

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 369.33  E-value: 2.36e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4336 QLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPE 4415
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4416 LPEKRRAFMLKDSGADVLLTcaghaipplfegevlllddpllyqgrTDnlnlscSENDLMYVIYTSGTTGQPKGVQLEHK 4495
Cdd:cd17653    81 LPSARIQAILRTSGATLLLT--------------------------TD------SPDDLAYIIFTSGSTGIPKGVMVPHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4496 TMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEA--KRDIRQLNDFVRThgiqtaflPTAF 4572
Cdd:cd17653   129 GVLNYVSQPPARLDVGPgSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDpfAHVARTVDALMST--------PSIL 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4573 LKLLASEKHYfepfaecVDHIIAAGEQLIAtrmlrDMLAR--HQVTLHNHYGPSETHVVTMYT-VDPDTDQelqPIGKPI 4649
Cdd:cd17653   201 STLSPQDFPN-------LKTIFLGGEAVPP-----SLLDRwsPGRRLYNAYGPTECTISSTMTeLLPGQPV---TIGKPI 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4650 SNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQ 4729
Cdd:cd17653   266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQ 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4730 VKIRGYRVELGEVEAALLK---HVQEAVVLAKENTdgqsdLYAYFTAEqSLSISQLKEKLAGQIPGYMIPSYFIQLEKLP 4806
Cdd:cd17653   346 VKVRGFRINLEEIEEVVLQsqpEVTQAAAIVVNGR-----LVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDSFP 419
                         490
                  ....*....|..
gi 166797876 4807 LTGNGKVNRRAL 4818
Cdd:cd17653   420 LTANGKVDRKAL 431
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1785-2261 1.87e-112

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 367.34  E-value: 1.87e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIR 1864
Cdd:cd05945     2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1865 YMLDDSQAGIVLmqrdvrkqlayegvtvllddessyhQDGSDlapisdvshLAYVIYTSGSTGRPKGVLIEHGGLTNYIW 1944
Cdd:cd05945    82 EILDAAKPALLI-------------------------ADGDD---------NAYIIFTSGSTGRPKGVQISHDNLVSFTN 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1945 WAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIvRDPRVDIIKLTPAHLQVL---K 2018
Cdd:cd05945   128 WMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDataDPKQLFRFL-AEHGITVWVSTPSFAAMCllsP 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2019 EMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRiEICNEYGPTETVVGCMIYRYDAA-KDRRESVPIGTAAANTSIYV 2097
Cdd:cd05945   207 TFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVTYIEVTPEvLDGYDRLPIGYAKPGAKLVI 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2098 LDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYR 2177
Cdd:cd05945   286 LDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVRLEADGLLFYRGRLDFQVKLNGYR 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2178 IELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAA---RLRKQLSQTLASYMVPAYFIELDEMPLTSNG 2254
Cdd:cd05945   363 IELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYMIPRRFVYLDELPLNANG 442

                  ....*..
gi 166797876 2255 KINKKGL 2261
Cdd:cd05945   443 KIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
269-662 4.24e-112

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 365.10  E-value: 4.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   269 FEEQAERTPENAAV-KFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEY 347
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   348 PKERLQYLLHDADADVLLVQHHLKNS-----------------LAFDGPV--IDLNDEASYHADCSLLSPVAGHSHLAYV 408
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgklevvklvlvLDRDPVLkeEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   409 IYTSGTTGKPKGVMVEHGGIVNSLQWKKAF----FKHSPADRVLVLYPYVFDA-FILNFFGPLISGATLHLLPNEENKET 483
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   484 FAIQNAIKQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRiRINNEYGPTENSVVST 561
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAgaPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   562 FHPVQSADEQI--TIGSPVANHQAYILGAHH-QIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTG 638
Cdd:pfam00501  320 TPLPLDEDLRSlgSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
                          410       420
                   ....*....|....*....|....
gi 166797876   639 DLARWLPDGRIEYLGRIDHQVKIR 662
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
3297-3778 3.82e-111

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 364.67  E-value: 3.82e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYCGK--LQDDIGFSGTCIDLMEEHfyHEKDSSLALSyQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEG 3454
Cdd:cd12114    81 ADAGARLVLTDGPdaQLDVAVFDVLILDLDALA--APAPPPPVDV-APDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3455 LSRQVysAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAG 3534
Cdd:cd12114   158 INRRF--AVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3535 DLQGVTLQHL---LIGGE--ALSKTTvnKLKQLFgehgAAPGITNVYGPTETCVDASLFNIECSSDAWaRSqnyVPIGKP 3609
Cdd:cd12114   236 EAAQALLPSLrlvLLSGDwiPLDLPA--RLRALA----PDARLISLGGATEASIWSIYHPIDEVPPDW-RS---IPYGRP 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3610 LGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPfvPEDRMYRTGDLARLLPDGNIEYIGRIDH 3689
Cdd:cd12114   306 LANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDG 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3690 QVKIQGFRIELGEIESVMLNVPDIQEaAAAALKDADDEYYLCGYFAAD---KTIQISELRKRMARHLPGYMIPAHFVQLD 3766
Cdd:cd12114   384 QVKVRGYRIELGEIEAALQAHPGVAR-AVVVVLGDPGGKRLAAFVVPDndgTPIAPDALRAFLAQTLPAYMIPSRVIALE 462
                         490
                  ....*....|..
gi 166797876 3767 KMPLTPNGKLNR 3778
Cdd:cd12114   463 ALPLTANGKVDR 474
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
4346-4818 2.12e-110

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 362.36  E-value: 2.12e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4346 PDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML 4425
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4426 KDSGADVLLTCAGHAIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSEnDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAyeq 4505
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPD-DLAYVIFTSGSTGTPKGVMISHRAALNTIL--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4506 DHTQlRF-----DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIqTA--FLPtAFLKLLas 4578
Cdd:cd12114   157 DINR-RFavgpdDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGV-TLwnSVP-ALLEML-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4579 ekhyfepfaecVDHIIAAGEQLIATRM---------------LRDMLAR-HQVTLHnhyGPSETHV-VTMYTVDP-DTDQ 4640
Cdd:cd12114   232 -----------LDVLEAAQALLPSLRLvllsgdwipldlparLRALAPDaRLISLG---GATEASIwSIYHPIDEvPPDW 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4641 ELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDsnQRMYKTGDLARYLPEGNI 4720
Cdd:cd12114   298 RSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDG--ERLYRTGDLGRYRPDGTL 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4721 EYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKeNTDGQSDLYAYFTAE-QSLSISQ--LKEKLAGQIPGYMI 4795
Cdd:cd12114   376 EFLGRRDGQVKVRGYRIELGEIEAALQAHpgVARAVVVVL-GDPGGKRLAAFVVPDnDGTPIAPdaLRAFLAQTLPAYMI 454
                         490       500
                  ....*....|....*....|...
gi 166797876 4796 PSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd12114   455 PSRVIALEALPLTANGKVDRAAL 477
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3287-3781 1.22e-109

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 358.55  E-value: 1.22e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3287 ELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPD 3366
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3367 SPSERIRYILNDSSISVLLYCGKLQDdigfsgtcidlmeehfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHR 3446
Cdd:cd17653    81 LPSARIQAILRTSGATLLLTTDSPDD--------------------------------LAYIIFTSGSTGIPKGVMVPHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3447 QVIHLIEGLSRQVYS-AYDAELNIAMLApyyFDASVQQMYASLLSGHTLfiVPKEIVSDGAALCRyyrqhSIDITDGTPA 3525
Cdd:cd17653   129 GVLNYVSQPPARLDVgPGSRVAQVLSIA---FDACIGEIFSTLCNGGTL--VLADPSDPFAHVAR-----TVDALMSTPS 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3526 HLKLLIAAgDLQgvTLQHLLIGGEALSKTTVNKLkqlfgehGAAPGITNVYGPTETCVdaslfnieCSSDAWARSQNYVP 3605
Cdd:cd17653   199 ILSTLSPQ-DFP--NLKTIFLGGEAVPPSLLDRW-------SPGRRLYNAYGPTECTI--------SSTMTELLPGQPVT 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3606 IGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIG 3685
Cdd:cd17653   261 IGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLG 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3686 RIDHQVKIQGFRIELGEIESVMLNvpdiQEAAAAALKDADDEYYLCGyFAADKTIQISELRKRMARHLPGYMIPAHFVQL 3765
Cdd:cd17653   341 REDNQVKVRGFRINLEEIEEVVLQ----SQPEVTQAAAIVVNGRLVA-FVTPETVDVDGLRSELAKHLPSYAVPDRIIAL 415
                         490
                  ....*....|....*.
gi 166797876 3766 DKMPLTPNGKLNRQLL 3781
Cdd:cd17653   416 DSFPLTANGKVDRKAL 431
AMP-binding pfam00501
AMP-binding enzyme;
3289-3694 4.06e-109

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 356.24  E-value: 4.06e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3289 FEEQAHRTPDNTAV-VFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDS 3367
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3368 PSERIRYILNDSSISVLLYCGKLQ----------DDIGFSGTCID----LMEEHFYHEKDSSLALSY-----QSSQLAYA 3428
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealgkLEVVKLVLVLDrdpvLKEEPLPEEAKPADVPPPpppppDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3429 IYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSA--YDAELNIAMLAPYYFDASVQ-QMYASLLSGHTLFIVPKEIVSDG 3505
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGfgLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3506 AALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGV---TLQHLLIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETC 3582
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAllsSLRLVLSGGAPLPPELARRFRELFGGA-----LVNGYGLTETT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3583 VDAslfnieCSSDAWARSQNYVP-IGKPLGRNRMYILD-SKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpf 3660
Cdd:pfam00501  316 GVV------TTPLPLDEDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD---- 385
                          410       420       430
                   ....*....|....*....|....*....|....
gi 166797876  3661 vpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQ 3694
Cdd:pfam00501  386 --EDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
3888-4294 2.84e-108

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 354.42  E-value: 2.84e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLD--HAAFEAEW 3965
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPaaEARPDLTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3966 YQGEEDDADLYIRQFI-RPFHL-DEPPLlRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIY----EGE--TLP 4037
Cdd:cd19540    83 VDVTEDELAARLAEAArRGFDLtAELPL-RARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRapDWA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4038 PLRIQYKDYAVWQT---GEARLQQ--IQKQEAYWLELYSGdVP-VLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQL 4111
Cdd:cd19540   162 PLPVQYADYALWQRellGDEDDPDslAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4112 ASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKA 4191
Cdd:cd19540   241 AREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4192 YEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVE------EGAGIQ 4265
Cdd:cd19540   321 FAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGLT 400
                         410       420
                  ....*....|....*....|....*....
gi 166797876 4266 FTLEYLTALFKPETIERMMGHFEQLVDSI 4294
Cdd:cd19540   401 GELEYATDLFDRSTAERLADRFVRVLEAV 429
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1776-2281 4.35e-108

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 354.89  E-value: 4.35e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPID 1855
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1856 PEYPQDRIRYMLDDSQAGIVLMqrdvrkqlayegvtvllddessyhqdgsdlapisdvshlAYVIYTSGSTGRPKGVLIE 1935
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1936 HGGLTNYIWW--------AKEVYVkgekANFPLYSSISFdltVTSIFTPLVTGNAIIVYDGEDKTALLESIVRDpRVDII 2007
Cdd:COG0318   122 HRNLLANAAAiaaalgltPGDVVL----VALPLFHVFGL---TVGLLAPLLAGATLVLLPRFDPERVLELIERE-RVTVL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2008 KLTPAHLQ-VLKEMNIA--DQTAVRRMIVGGENLSTRLARSIHEQFEgrIEICNEYGPTETVVGCMIYRYDAAKDRRESV 2084
Cdd:COG0318   194 FGVPTMLArLLRHPEFAryDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPGERRPGSV 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2085 piGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYA 2164
Cdd:COG0318   272 --GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIV 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2165 GRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYF 2242
Cdd:COG0318   343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVPRRV 422
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876 2243 IELDEMPLTSNGKINKKGLpapdfelqdRAEYKAPRTKA 2281
Cdd:COG0318   423 EFVDELPRTASGKIDRRAL---------RERYAAGALEA 452
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
3293-3778 6.61e-108

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 354.25  E-value: 6.61e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERI 3372
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3373 RYILNDSSISVLLYCGklqDDigfsgtcidlmeehfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQVIHLI 3452
Cdd:cd05945    81 REILDAAKPALLIADG---DD-------------------------------NAYIIFTSGSTGRPKGVQISHDNLVSFT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3453 EGLSrqvySAYD--AELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLL 3530
Cdd:cd05945   127 NWML----SDFPlgPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMC 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3531 IAAGDL---QGVTLQHLLIGGEALSKTTVNKLKQLFgehgaaPG--ITNVYGPTETCVdaslfniECSSDAWARSQ--NY 3603
Cdd:cd05945   203 LLSPTFtpeSLPSLRHFLFCGEVLPHKTARALQQRF------PDarIYNTYGPTEATV-------AVTYIEVTPEVldGY 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3604 --VPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVpedRMYRTGDLARLLPDGNI 3681
Cdd:cd05945   270 drLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ---RAYRTGDLVRLEADGLL 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3682 EYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYF---AADKTIQISELRKRMARHLPGYMI 3758
Cdd:cd05945   347 FYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVvpkPGAEAGLTKAIKAELAERLPPYMI 426
                         490       500
                  ....*....|....*....|
gi 166797876 3759 PAHFVQLDKMPLTPNGKLNR 3778
Cdd:cd05945   427 PRRFVYLDELPLNANGKIDR 446
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
4342-4818 1.87e-107

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 352.70  E-value: 1.87e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRR 4421
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4422 AFMLKDSGADVLLTcaghaipplfegevlllddpllyqgrtdnlnlscSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLL 4501
Cdd:cd05945    81 REILDAAKPALLIA----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4502 AYEQDHTQLR-FDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEK 4580
Cdd:cd05945   127 NWMLSDFPLGpGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSP 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4581 HYFEPFAECVDHIIAAGEQLiATRMLRDMLARHQVT-LHNHYGPSETHV-VTMYTVDPDTDQELQ--PIGKPISNTEIFI 4656
Cdd:cd05945   207 TFTPESLPSLRHFLFCGEVL-PHKTARALQQRFPDArIYNTYGPTEATVaVTYIEVTPEVLDGYDrlPIGYAKPGAKLVI 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4657 LNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYR 4736
Cdd:cd05945   286 LDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYR 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4737 VELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSI---SQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNG 4811
Cdd:cd05945   363 IELEEIEAALRQVpgVKEAVVVPKYKGEKVTELIAFVVPKPGAEAgltKAIKAELAERLPPYMIPRRFVYLDELPLNANG 442

                  ....*..
gi 166797876 4812 KVNRRAL 4818
Cdd:cd05945   443 KIDRKAL 449
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
3888-4298 9.47e-107

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 350.03  E-value: 9.47e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEWYQ 3967
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3968 GEEDDADL--YIRQFIR-PFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGET------LPP 4038
Cdd:cd19538    83 KEVDEEELesEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCkgeapeLAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4039 LRIQYKDYAVWQ-----TGEARLQQIQKQEAYWLELYSGdVPV-LHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLA 4112
Cdd:cd19538   163 LPVQYADYALWQqellgDESDPDSLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4113 SQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAY 4192
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4193 EHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQEQLEINDVTFKPYPNGHTMAKFDLTLT-----AVEEGAGIQFT 4267
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFElreqyNDGTPNGIEGF 401
                         410       420       430
                  ....*....|....*....|....*....|.
gi 166797876 4268 LEYLTALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19538   402 IEYRTDLFDHETIEALAQRYLLLLESAVENP 432
AMP-binding pfam00501
AMP-binding enzyme;
1780-2174 2.07e-103

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 340.06  E-value: 2.07e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1780 FEEQSQRTPDQAAV-IDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY 1858
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1859 PQDRIRYMLDDSQAGIVL--------MQRDVRKQLAYEGVTVLLD-----------DESSYHQDGSDLAPISDVSHLAYV 1919
Cdd:pfam00501   81 PAEELAYILEDSGAKVLItddalkleELLEALGKLEVVKLVLVLDrdpvlkeeplpEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1920 IYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKAN----FPLYSSISFDLTVTS-IFTPLVTGNAIIVYDGEDKT-- 1992
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpddrVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALdp 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1993 ALLESIVRDPRVDIIKLTPAHLQVL---KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFegRIEICNEYGPTETVVGC 2069
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLleaGAPKRALLSSLRLVLSGGAPLPPELARRFRELF--GGALVNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2070 MIYRYDAAKDRRESvPIGTAAANTSIYVLDEN-MKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPfepgakMYK 2148
Cdd:pfam00501  319 TTPLPLDEDLRSLG-SVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG------WYR 391
                          410       420
                   ....*....|....*....|....*.
gi 166797876  2149 TGDLAKWLADGNIEYAGRIDEQVKIR 2174
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
4338-4733 1.96e-101

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 334.28  E-value: 1.96e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4338 FEQQAERNPDHEAV-MFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPEL 4416
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4417 PEKRRAFMLKDSGADVLLTCAGHAIPPLFEGE--------VLLLDDPLLYQGRTDNLNLSC-----------SENDLMYV 4477
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALgklevvklVLVLDRDPVLKEEPLPEEAKPadvppppppppDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4478 IYTSGTTGQPKGVQLEHKTMTNLLA-----YEQDHTQLRFDRVLQFAAMSFDVCYQ-EMFSALSSGGILFIIGNEAKRDI 4551
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLsikrvRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4552 RQLNDFVRTHGIQTAFL-PTAFLKLLASEKHYFEPFAEcVDHIIAAGEQLIATRMLRdMLARHQVTLHNHYGPSETHVVT 4630
Cdd:pfam00501  241 AALLELIERYKVTVLYGvPTLLNMLLEAGAPKRALLSS-LRLVLSGGAPLPPELARR-FRELFGGALVNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4631 MYTVDPDTDQELQP-IGKPISNTEIFILNEA-GTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPhpydsnQRMYKT 4708
Cdd:pfam00501  319 TTPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 166797876  4709 GDLARYLPEGNIEYAGRRDHQVKIR 4733
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
4334-4818 1.05e-100

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 333.70  E-value: 1.05e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4334 IHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPID 4413
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4414 PELPEKRRAFMLKDSGADVLLTCaghaipplfegevlllddpllyqgrtdnlnlscsendlmYVIYTSGTTGQPKGVQLE 4493
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVTA---------------------------------------LILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4494 HKTMTNLLAYEQDHTQLR-FDRVLQFAAMSFDV-CYQEMFSALSSGGILFIIgneAKRDIRQLNDFVRTHGIQTAFL-PT 4570
Cdd:COG0318   122 HRNLLANAAAIAAALGLTpGDVVLVALPLFHVFgLTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGvPT 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4571 AFLKLLASEKhyFEPFA-ECVDHIIAAGEQLiATRMLRDMLARHQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPI 4649
Cdd:COG0318   199 MLARLLRHPE--FARYDlSSLRLVVSGGAPL-PPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4650 SNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQ 4729
Cdd:COG0318   276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4730 VKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAE--QSLSISQLKEKLAGQIPGYMIPSYFIQLEKL 4805
Cdd:COG0318   349 IISGGENVYPAEVEEVLAAHpgVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                         490
                  ....*....|...
gi 166797876 4806 PLTGNGKVNRRAL 4818
Cdd:COG0318   429 PRTASGKIDRRAL 441
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2358-2800 7.03e-95

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 316.97  E-value: 7.03e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2358 VKGKVSLTPIQH--WFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQ-NEEIAQS 2434
Cdd:pfam00668    1 VQDEYPLSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQvILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2435 GLYRLEVMNLKEDPDPGRTIEAKADEIQSSMHLSDGPLMKAGLFQCAD-GDHLLIAIHHLIIDGISWRILLEDIVSGYKQ 2513
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAEnRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2514 AENGRVIQLPQKTDsFQLWAKRLSEYAQSETIKQEQEYWTKIEQTEVKP--LPKDFHET--HTTAKDSETAAVEwtkEET 2589
Cdd:pfam00668  161 LLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVlqLPKDYARPadRSFKGDRLSFTLD---EDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2590 ELLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREqiiqDIDISRTVGWFTSLYPVVLHAQPGKEISDY 2669
Cdd:pfam00668  237 EELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP----SPDIERMVGMFVNTLPLRIDPKGGKTFSEL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2670 IKTTKEGLRQI-PHKGIGYGIARYLSG-----GMPSKLNPEISF-NYLGQFDQDLQRhgvQLSSYSCGSDSSGHQERPYV 2742
Cdd:pfam00668  313 IKRVQEDLLSAePHQGYPFGDLVNDLRlprdlSRHPLFDPMFSFqNYLGQDSQEEEF---QLSELDLSVSSVIEEEAKYD 389
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876  2743 LNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHCVHKEQSELTPSD 2800
Cdd:pfam00668  390 LSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSD 447
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
4912-5344 2.42e-94

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 338.75  E-value: 2.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4912 PDYIPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQV 4991
Cdd:COG1020     6 AAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4992 IKSQVEFSMERY--------EATADEVEECFRAFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEK 5063
Cdd:COG1020    86 IQPVVAAPLPVVvllvdleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5064 LIQLYD------GKELAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTL 5137
Cdd:COG1020   166 LLRLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5138 DKTVTQGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDY 5217
Cdd:COG1020   246 PAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAEL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5218 ITETKETMLKAFEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQTDIEVDSLAVRPYEQTETAAKFDLQLNFLID 5297
Cdd:COG1020   326 LARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVET 405
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 5298 QDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQL 5344
Cdd:COG1020   406 GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPL 452
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
3285-3788 3.85e-94

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 314.44  E-value: 3.85e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3285 IHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPID 3364
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3365 PDSPSERIRYILNDSSISVLLYcgklqddigfsgtcidlmeehfyhekdsslalsyqssqlAYAIYTSGTTGKPKGTLIE 3444
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3445 HRQVIHLIEGLSRqvYSAYDAELNIAMLAPYYFDAS-VQQMYASLLSGHTLFIVPKEivsDGAALCRYYRQHSIDITDGT 3523
Cdd:COG0318   122 HRNLLANAAAIAA--ALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPRF---DPERVLELIERERVTVLFGV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3524 PAHLKLLIAAGDLQGV---TLQHLLIGGEALSKTTVNKLKQLFGehgaaPGITNVYGPTETCVdASLFNIECSSDAWARS 3600
Cdd:COG0318   197 PTMLARLLRHPEFARYdlsSLRLVVSGGAPLPPELLERFEERFG-----VRIVEGYGLTETSP-VVTVNPEDPGERRPGS 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3601 qnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGN 3680
Cdd:COG0318   271 -----VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------RDGWLRTGDLGRLDEDGY 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3681 IEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYF--AADKTIQISELRKRMARHLPGYMI 3758
Cdd:COG0318   339 LYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVvlRPGAELDAEELRAFLRERLARYKV 418
                         490       500       510
                  ....*....|....*....|....*....|
gi 166797876 3759 PAHFVQLDKMPLTPNGKLNRQLLPAPVKKR 3788
Cdd:COG0318   419 PRRVEFVDELPRTASGKIDRRALRERYAAG 448
PRK05691 PRK05691
peptide synthase; Validated
4330-5344 5.86e-94

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 344.46  E-value: 5.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4330 IPTTIHQLFEQQAERNPDHEAVMF------GNQTLTYRQLNERSNQLARVLQDKGACTDQVVaVLTDRSAHMIIGILAIL 4403
Cdd:PRK05691    7 LPLTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4404 KAGAAFLPIDPelPE-------KRRAFMLKDSGADVLLTCAGHAiPPLFEGEVLLLDD--PLLYqgrTDNLNLSCSEN-- 4472
Cdd:PRK05691   86 YAGVIAVPAYP--PEsarrhhqERLLSIIADAEPRLLLTVADLR-DSLLQMEELAAANapELLC---VDTLDPALAEAwq 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 -------DLMYVIYTSGTTGQPKGVQLEHKtmtNLLAYEQDHTQ-----LRFDRVLqfaaMSFDVCYQEM---------- 4530
Cdd:PRK05691  160 epalqpdDIAFLQYTSGSTALPKGVQVSHG---NLVANEQLIRHgfgidLNPDDVI----VSWLPLYHDMgliggllqpi 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4531 FSALSSggILFIIGNEAKRDIRQLNDFVRTHGiqTAFLPTAFLKLLASEK------------------------------ 4580
Cdd:PRK05691  233 FSGVPC--VLMSPAYFLERPLRWLEAISEYGG--TISGGPDFAYRLCSERvsesalerldlsrwrvaysgsepirqdsle 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4581 HYFEPFAEC---VDHIIAA---------------GEQLIATRMLRDMLARhqvtlhNHygpsethvvtmytVDPDTDQEL 4642
Cdd:PRK05691  309 RFAEKFAACgfdPDSFFASyglaeatlfvsggrrGQGIPALELDAEALAR------NR-------------AEPGTGSVL 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4643 QPIGKPISNTEIFILnEAGTLQ--PVGIVGELCISGVSLARGYHNRESLTLETFVPHpydSNQRMYKTGDLArYLPEGNI 4720
Cdd:PRK05691  370 MSCGRSQPGHAVLIV-DPQSLEvlGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH---DGRTWLRTGDLG-FLRDGEL 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4721 EYAGRRDHQVKIRGYRVELGEVEAALLKHVQEA----VVLAKENTDGQSDLYayFTAEQSLSISQL--KEKLAGQIPGYM 4794
Cdd:PRK05691  445 FVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkgrVAAFAVNHQGEEGIG--IAAEISRSVQKIlpPQALIKSIRQAV 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4795 ------IPSYFIQLE--KLPLTGNGKVNRRALPM-------------PEAGLQTGTDYVAPRTNMEEQLICIWQDVLKVK 4853
Cdd:PRK05691  523 aeacqeAPSVVLLLNpgALPKTSSGKLQRSACRLrladgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVE 602
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4854 EIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQCPTVGEMAQAIAEAETNG---PDYIPKAKAKDVYPVSSVQ 4930
Cdd:PRK05691  603 QVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGgaaQAAIARLPRGQALPQSLAQ 682
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4931 KMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMERYEAT---A 5007
Cdd:PRK05691  683 NRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSdlpE 762
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5008 DEVEEcfRAFVR-------PFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGK------ELA 5074
Cdd:PRK05691  763 AEREA--RAAQIreeearqPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELA 840
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5075 PLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTGS 5154
Cdd:PRK05691  841 PLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQA 920
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5155 TAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEHQEY 5234
Cdd:PRK05691  921 TLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDL 1000
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5235 PFEELVEKLGVKRDlsrNPLFDTMFvlqNTEQTDIEvdslAVR----------PYEQTEtaAKFDLQLNFLID-QDEIQG 5303
Cdd:PRK05691 1001 PFEQLVEALPQARE---QGLFQVMF---NHQQRDLS----ALRrlpgllaeelPWHSRE--AKFDLQLHSEEDrNGRLTL 1068
                        1130      1140      1150      1160
                  ....*....|....*....|....*....|....*....|.
gi 166797876 5304 SFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQL 5344
Cdd:PRK05691 1069 SFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQL 1109
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
852-1291 2.55e-93

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 312.35  E-value: 2.55e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   852 LTPIQH--WFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGyAPRITGTDESElFHLEV 929
Cdd:pfam00668    7 LSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENG-EPVQVILEERP-FELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   930 MNYKG--ETDPAQAIADKANE-IQSSMVLDKGPLMKLGLFQC-PDGDHLLIAIHHLLIDGVSWRILLEDFASGYEQAERR 1005
Cdd:pfam00668   85 IDISDlsESEEEEAIEAFIQRdLQSPFDLEKGPLFRAGLFRIaENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1006 QTIQLPQKTDsFPFWADQLSKYAAETDMEEEIAYWTEL--SSIKPQPLPKDTIS--EGSLLRDSEEVTIQwtkEETEQLL 1081
Cdd:pfam00668  165 EPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQleGELPVLQLPKDYARpaDRSFKGDRLSFTLD---EDTEELL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1082 KQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGRepiiPDADISRTIGWFTSQYPVVLRMEAGKNLSQRIKIV 1161
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR----PSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1162 KEGLRRI-PDKGMNYSIIKYISGHPEADSLQ--LKPEISF-NYLGQFDQDlkhQALRISPFSTGLSMNENQERTAVLDLN 1237
Cdd:pfam00668  317 QEDLLSAePHQGYPFGDLVNDLRLPRDLSRHplFDPMFSFqNYLGQDSQE---EEFQLSELDLSVSSVIEEEAKYDLSLT 393
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 166797876  1238 GMIAEGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHCVSRQQTSLTPSD 1291
Cdd:pfam00668  394 ASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSD 447
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
3888-4292 4.97e-93

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 310.47  E-value: 4.97e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMAD-GEPVQYVL--DHAAFEAE 3964
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILppGPAPLEVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3965 wyqgEEDDADLYIRQFI---------RPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEG-- 4033
Cdd:cd19539    83 ----DLSDPDSDRERRLeellreresRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAArr 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4034 ----ETLPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLElYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLK 4109
Cdd:cd19539   159 kgpaAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRR-RLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4110 QLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENAL 4189
Cdd:cd19539   238 ELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4190 KAYEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQEQLEI-NDVTFKPYPNGHTMAKFDLTLTAVEEGAGIQFTL 4268
Cdd:cd19539   318 DAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELaGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSL 397
                         410       420
                  ....*....|....*....|....
gi 166797876 4269 EYLTALFKPETIERMMGHFEQLVD 4292
Cdd:cd19539   398 GYATSLFDEETIQGFLADYLQVLR 421
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
4946-5335 2.39e-91

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 305.89  E-value: 2.39e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4946 YNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVI--KSQVEFSMERYEATADEVEECFRAFV-RPFD 5022
Cdd:cd19540    24 YNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLTVVDVTEDELAARLAEAArRGFD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5023 LSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLY----DGKE--LAPLRIQYKDFTEWkhqkeQRE-- 5094
Cdd:cd19540   104 LTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRApdWAPLPVQYADYALW-----QREll 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5095 --------RIKSQEEYWlgvfHEEL---PS-FELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFS 5162
Cdd:cd19540   179 gdeddpdsLAARQLAYW----RETLaglPEeLELPTDRPRPAVASYRGGTVEFTIDAELHARLAALAREHGATLFMVLHA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5163 AYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEHQEYPFEELVEK 5242
Cdd:cd19540   255 ALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPFERLVEA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5243 LGVKRDLSRNPLFDTMFVLQNTEQTDIEVDSLAVRPYEQTETAAKFDLQLNFLIDQDE------IQGSFDYCTKLFKKKT 5316
Cdd:cd19540   335 LNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDAdgapagLTGELEYATDLFDRST 414
                         410
                  ....*....|....*....
gi 166797876 5317 IAVLAKDYVMILSAIMRNP 5335
Cdd:cd19540   415 AERLADRFVRVLEAVVADP 433
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
4925-5335 2.23e-88

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 297.25  E-value: 2.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4925 PVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMERY- 5003
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEi 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5004 -EATADEVEECFRAFVR-PFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGK------ELAP 5075
Cdd:cd19538    83 kEVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5076 LRIQYKDFTEWK-----HQKEQRERIKSQEEYWLGVFHEeLPS-FELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLE 5149
Cdd:cd19538   163 LPVQYADYALWQqellgDESDPDSLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5150 ELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAF 5229
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5230 EHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQTDIEVDSLAVRPYEQTETAAKFDLQLNF-----LIDQDEIQGS 5304
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELreqynDGTPNGIEGF 401
                         410       420       430
                  ....*....|....*....|....*....|.
gi 166797876 5305 FDYCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19538   402 IEYRTDLFDHETIEALAQRYLLLLESAVENP 432
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
4066-4905 1.29e-87

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 318.55  E-value: 1.29e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4066 WLElYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKqksdglKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSp 4145
Cdd:TIGR03443    2 WSE-RLDNPTLSVLPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4146 iagRPHADLEPIIgmfvntlaMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIARDLSRNP-LFDTMFvl 4224
Cdd:TIGR03443   74 ---SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAF-- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4225 QNTEQEQLEIndvtfkpYPNGHTMakfDLTLTAVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQPEAELAR 4304
Cdd:TIGR03443  141 QDAPDNQQTT-------YSTGSTT---DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4305 LNMMTKEEerdiQQLFNDtavaekriPTT----------IHQLFEQQAERNPDHEAVM---------FGNQTLTYRQLNE 4365
Cdd:TIGR03443  211 VSLITPSQ----KSLLPD--------PTKdldwsgfrgaIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4366 RSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML---KDSGAdVLLTCAGhAIP 4442
Cdd:TIGR03443  279 ASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLsvaKPRAL-IVIEKAG-TLD 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4443 PLFEG-------------EVLLLDDPLLYQGRTDNLNLSCSENDLMY------VI----------YTSGTTGQPKGVQLE 4493
Cdd:TIGR03443  357 QLVRDyidkelelrteipALALQDDGSLVGGSLEGGETDVLAPYQALkdtptgVVvgpdsnptlsFTSGSEGIPKGVLGR 436
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4494 HKTmtnlLAYEQDHTQLRF-----DRVLQFAAMSFDVCYQEMFSALSSGGILFI-----IGNEAKrdirqLNDFVRTHGI 4563
Cdd:TIGR03443  437 HFS----LAYYFPWMAKRFglsenDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVptaddIGTPGR-----LAEWMAKYGA 507
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4564 QTAFLPTAFLKLLASEKHyfEPFAEcVDHIIAAGEQLIATRMLR-DMLARHqVTLHNHYGPSETH------VVTMYTVDP 4636
Cdd:TIGR03443  508 TVTHLTPAMGQLLSAQAT--TPIPS-LHHAFFVGDILTKRDCLRlQTLAEN-VCIVNMYGTTETQravsyfEIPSRSSDS 583
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4637 ---DTDQELQPIGKPISNTEIFILNEAGTLQP--VGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQ-------- 4703
Cdd:TIGR03443  584 tflKNLKDVMPAGKGMKNVQLLVVNRNDRTQTcgVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldke 663
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4704 --------------RMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDL 4767
Cdd:TIGR03443  664 nnkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHplVRENVTLVRRDKDEEPTL 743
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4768 YAYFTA-------EQSLS---------------------ISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALP 4819
Cdd:TIGR03443  744 VSYIVPqdksdelEEFKSevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALP 823
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4820 MPE-------AGLQTGTDYVAPRTNMEEQLICIWQDVL--KVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLRE 4890
Cdd:TIGR03443  824 FPDtaqlaavAKNRSASAADEEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGL 903
                          970
                   ....*....|....*
gi 166797876  4891 VFQCPTVGEMAQAIA 4905
Cdd:TIGR03443  904 IFKSPTIKGFAKEVD 918
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
270-755 6.42e-85

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 289.74  E-value: 6.42e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   270 EEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPK 349
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   350 ERLQYLLHDADADVLLVQHHLKNSLAfDGPVI--DLNDEA-SYHADCSLLSPVAGHSHLaYVIYTSGTTGKPKGVMVEHG 426
Cdd:TIGR01734   87 ERIEMIIEAAGPELVIHTAELSIDAV-GTQIItlSALEQAeTSGGPVSFDHAVKGDDNY-YIIYTSGSTGNPKGVQISHD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   427 GIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEEN---KETFAiqnAIKQERITHFSTSPR 503
Cdd:TIGR01734  165 NLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITnnfKLLFE---ELPKTGLNVWVSTPS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   504 LLKT--MIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTfhPVQSADEQIT------IG 575
Cdd:TIGR01734  242 FVDMclLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVT--SVKITQEILDqyprlpIG 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   576 SPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHlhvPGQKMYKTGDLARwLPDGRIEYLGRI 655
Cdd:TIGR01734  320 FAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH---EGQPAYRTGDAGT-ITDGQLFYQGRL 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   656 DHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADG-AKQLYAYYVGEPSLTAAQF------REELSRELPNYMIPS 728
Cdd:TIGR01734  396 DFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHkVEYLIAAIVPETEDFEKEFqltkaiKKELKKSLPAYMIPR 475
                          490       500
                   ....*....|....*....|....*..
gi 166797876   729 RFIPLERIPLTSNGKIDLKALpAADEN 755
Cdd:TIGR01734  476 KFIYRDQLPLTANGKIDRKAL-AEEVN 501
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1780-2261 1.46e-84

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 288.72  E-value: 1.46e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1780 FEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYP 1859
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1860 QDRIRYMLDDSQAGIVLMQRDVrkQLAYEGVTVLLDDESsyhQDGSDLAPISDVSHL------AYVIYTSGSTGRPKGVL 1933
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEEL--PLEILGIPVITLDEL---KDIFATGNPYDFDHAvkgddnYYIIFTSGTTGKPKGVQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1934 IEHGGLTNYIWWAKEVYVKGEKANF---PLYSsisFDLTVTSIFTPLVTGNAIIVYDgEDKTA----LLESIVRDPrVDI 2006
Cdd:PRK04813  163 ISHDNLVSFTNWMLEDFALPEGPQFlnqAPYS---FDLSVMDLYPTLASGGTLVALP-KDMTAnfkqLFETLPQLP-INV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2007 IKLTPAHLQV---LKEMNIADQTAVRRMIVGGENLSTRLARSIHEQF-EGRIeiCNEYGPTETVVGC--------MIYRY 2074
Cdd:PRK04813  238 WVSTPSFADMcllDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFpSATI--YNTYGPTEATVAVtsieitdeMLDQY 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2075 DaakdrreSVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDdpfEPGAKMYKTGDLAK 2154
Cdd:PRK04813  316 K-------RLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2155 wLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSG-------GQTTAArLRK 2227
Cdd:PRK04813  386 -LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKeedfereFELTKA-IKK 463
                         490       500       510
                  ....*....|....*....|....*....|....
gi 166797876 2228 QLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK04813  464 ELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
3076-3869 4.18e-81

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 298.13  E-value: 4.18e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3076 TLWGVLLQKYSGSADVVFGSvvsgrpaeipDVEQMIGLFIntipVRIRCDEDSTFADTMQMVQQNALASQSYDTYPLYEI 3155
Cdd:TIGR03443   54 AAFAALVYRLTGDEDIVLGT----------SSNKSGRPFV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDEL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3156 QAQTEQKQNLIDHIMIFEnypIGQQaeetghHGTELNITNFhmQEHSHYDLNVVVIPGK-QLAVHFGFNENEYEKSEVER 3234
Cdd:TIGR03443  120 SEHIQAAKKLERTPPLFR---LAFQ------DAPDNQQTTY--STGSTTDLTVFLTPSSpELELSIYYNSLLFSSDRITI 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3235 LRGHFEKLMQQVLRQPSVKIEDLELLTQQEKEYLLSrfQSNDMHYPREK-TIHELFEEQAHRTPDNTAVV----FEG--- 3306
Cdd:TIGR03443  189 VADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLPD--PTKDLDWSGFRgAIHDIFADNAEKHPDRTCVVetpsFLDpss 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3307 --KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSER------------- 3371
Cdd:TIGR03443  267 ktRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpral 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3372 --IR-----------YILNDSSISVLLYCGKLQDDIGFSGTCIDLME-------EHFYHEK-------DSSLALSYqssq 3424
Cdd:TIGR03443  347 ivIEkagtldqlvrdYIDKELELRTEIPALALQDDGSLVGGSLEGGEtdvlapyQALKDTPtgvvvgpDSNPTLSF---- 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3425 layaiyTSGTTGKPKGTLIEHRQVIHLIEGLSRQVysAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSD 3504
Cdd:TIGR03443  423 ------TSGSEGIPKGVLGRHFSLAYYFPWMAKRF--GLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGT 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3505 GAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLIGGEALSKTTVNKLKQLfgehgaAPG--ITNVYGPTETC 3582
Cdd:TIGR03443  495 PGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTL------AENvcIVNMYGTTETQ 568
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3583 VDASLFNIECSSDawarSQNY-------VPIGKPLGRNRMYILDSKKRLQPKGVQ--GELYIAGDGVGRGYLNLPELTDE 3653
Cdd:TIGR03443  569 RAVSYFEIPSRSS----DSTFlknlkdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAE 644
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3654 KFVADPFV----------------------PEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVP 3711
Cdd:TIGR03443  645 KFVNNWFVdpshwidldkennkperefwlgPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHP 724
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3712 DIQEAAAAALKDADDEYYLCGYF--------------------AADKTIQ--------ISELRKRMARHLPGYMIPAHFV 3763
Cdd:TIGR03443  725 LVRENVTLVRRDKDEEPTLVSYIvpqdksdeleefksevddeeSSDPVVKglikyrklIKDIREYLKKKLPSYAIPTVIV 804
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3764 QLDKMPLTPNGKLNRQLLPAPVKKRDSGIEYVPPQTSAEIQLTA-------IWEDVL--GLEQVGIRDHFFEIGGHSLRA 3834
Cdd:TIGR03443  805 PLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASAADEEFTEtereirdLWLELLpnRPATISPDDSFFDLGGHSILA 884
                          890       900       910
                   ....*....|....*....|....*....|....*
gi 166797876  3835 TALIAKIQKQMHVQIPLRDVFRFPTIEQLARTITK 3869
Cdd:TIGR03443  885 TRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDR 919
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
269-749 5.16e-81

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 278.32  E-value: 5.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  269 FEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYP 348
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  349 KERLQYLLHDADADVLLVQHHLKNSLAfDGPVI---DLNDEASYHADCSLLSPVAGHSHlAYVIYTSGTTGKPKGVMVEH 425
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEELPLEIL-GIPVItldELKDIFATGNPYDFDHAVKGDDN-YYIIFTSGTTGKPKGVQISH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  426 GGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEEN---KETFAiqnAIKQERITHFSTSP 502
Cdd:PRK04813  166 DNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTanfKQLFE---TLPQLPINVWVSTP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  503 RL--LKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTfhPVQSADEQIT------I 574
Cdd:PRK04813  243 SFadMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVT--SIEITDEMLDqykrlpI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  575 GSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHlhvPGQKMYKTGDLARwLPDGRIEYLGR 654
Cdd:PRK04813  321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF---DGQPAYHTGDAGY-LEDGLLFYQGR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  655 IDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV-------GEPSLTAAqFREELSRELPNYMIP 727
Cdd:PRK04813  397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVpkeedfeREFELTKA-IKKELKERLMEYMIP 475
                         490       500
                  ....*....|....*....|..
gi 166797876  728 SRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK04813  476 RKFIYRDSLPLTPNGKIDRKAL 497
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
69-849 6.32e-81

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 297.75  E-value: 6.32e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    69 YLILLAGIECLLYKYTDRTSLILGiptVSKQKAGQSAVnnivlLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMA 148
Cdd:TIGR03443   49 FIILLAAFAALVYRLTGDEDIVLG---TSSNKSGRPFV-----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELS 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   149 RHLSVQYNDEHMPlihTVVSLNEIHSLQCKEDT-----ATDTLFHFDLENNGIHLKLFYNGNLYDERYINQIVSHLDQLL 223
Cdd:TIGR03443  121 EHIQAAKKLERTP---PLFRLAFQDAPDNQQTTystgsTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLL 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   224 SVILFQPQAAIHTAEILPEAQKQKLLFDFNDTvrDFSGSR-TVYQLFEEQAERTPENAAV---------KFKNDHLTYRE 293
Cdd:TIGR03443  198 SAASSNPDEPIGKVSLITPSQKSLLPDPTKDL--DWSGFRgAIHDIFADNAEKHPDRTCVvetpsfldpSSKTRSFTYKQ 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   294 LNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKER----LQY-----LLHDADADVL 364
Cdd:TIGR03443  276 INEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiyLSVakpraLIVIEKAGTL 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   365 --LVQHHLKNSLAFDG--PVIDLNDEASY--------HADCsLLSPVAGHSHLAYVI----------YTSGTTGKPKGVM 422
Cdd:TIGR03443  356 dqLVRDYIDKELELRTeiPALALQDDGSLvggsleggETDV-LAPYQALKDTPTGVVvgpdsnptlsFTSGSEGIPKGVL 434
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   423 VEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLlPNEENKET---FAIQNAIKQERITHFS 499
Cdd:TIGR03443  435 GRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLV-PTADDIGTpgrLAEWMAKYGATVTHLT 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   500 tsPRLLKTMIEQMNREdFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENS-VVSTFH-PVQSADEQ------ 571
Cdd:TIGR03443  514 --PAMGQLLSAQATTP-IPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQrAVSYFEiPSRSSDSTflknlk 590
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   572 --ITIGSPVANHQAYILGAHHQIQPIGIP--GELYVGGAGVARGYLNRPELTEEKFV----------------------E 625
Cdd:TIGR03443  591 dvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkennkperE 670
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   626 HLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV-- 703
Cdd:TIGR03443  671 FWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVpq 750
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   704 -GEPSLTAAQ-------------------------FREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALP------- 750
Cdd:TIGR03443  751 dKSDELEEFKsevddeessdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdtaql 830
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   751 -AADENTRAENEYIAPRNTiEELLASIWQEVL--GAERIGILDNFFDFGGDSIKSIQVSSRLYQAgYKVD--MKHLFKHP 825
Cdd:TIGR03443  831 aAVAKNRSASAADEEFTET-EREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKK-LNVElpLGLIFKSP 908
                          890       900
                   ....*....|....*....|....
gi 166797876   826 SIAelsQFVAPVSRVADQGEVNGG 849
Cdd:TIGR03443  909 TIK---GFAKEVDRLKKGEELADE 929
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1318-1741 1.24e-80

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 274.33  E-value: 1.24e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1318 IYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPLQIIFKTKKIGFQ 1397
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1398 FNDLREMKEsqKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKT-YRFIWSFHHILMDGWCLPLITKEIFENYFALL 1476
Cdd:cd19536    81 ELDLTPLEE--QLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERErFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1477 QQKQPEQSSITPYSQYIEWLGRQDAKEA-AAYWDQYLEGYEEQTgLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKRTAG 1555
Cdd:cd19536   159 EYKPLSLPPAQPYRDFVAHERASIQQAAsERYWREYLAGATLAT-LPALSEAVGGGPEQDSELLVSVPLPVRSRSLAKRS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1556 khHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCeAGTTFAELMKEAQERAVAS 1635
Cdd:cd19536   238 --GIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELES 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1636 QKFETHPLYDIQARTTQkQDLITHLMIFENYPVDQYMESIGRQNGtsITISNVQMEEQTNYDFNLTVIP-GDEMNISFEY 1714
Cdd:cd19536   315 LSHEQVPLADIQRCSEG-EPLFDSIVNFRHFDLDFGLPEWGSDEG--MRRGLLFSEFKSNYDVNLSVLPkQDRLELKLAY 391
                         410       420
                  ....*....|....*....|....*..
gi 166797876 1715 NANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19536   392 NSQVLDEEQAQRLAAYYKSAIAELATA 418
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
1781-2261 2.49e-79

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 273.56  E-value: 2.49e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1781 EEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQ 1860
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1861 DRIRYMLDDSQAGIVLMQRDVR-KQLAYEGVTVLLDDESSYHQDGSDL-APISDVSHLaYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:TIGR01734   87 ERIEMIIEAAGPELVIHTAELSiDAVGTQIITLSALEQAETSGGPVSFdHAVKGDDNY-YIIYTSGSTGNPKGVQISHDN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1939 LTNYIWWAKEVYVKGEKANF---PLYssiSFDLTVTSIFTPLVTGNAIIVYDGE---DKTALLESIVRDPrVDIIKLTPA 2012
Cdd:TIGR01734  166 LVSFTNWMLADFPLSEGKQFlnqAPF---SFDLSVMDLYPCLASGGTLHCLDKDitnNFKLLFEELPKTG-LNVWVSTPS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2013 HLQV------LKEMNIADQTavrRMIVGGENLSTRLARSIHEQFEgRIEICNEYGPTE-TVVGCMIYRYDAAKDRRESVP 2085
Cdd:TIGR01734  242 FVDMclldpnFNQENYPHLT---HFLFCGEELPVKTAKALLERFP-KATIYNTYGPTEaTVAVTSVKITQEILDQYPRLP 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2086 IGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGakmYKTGDLAKwLADGNIEYAG 2165
Cdd:TIGR01734  318 IGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHEGQPA---YRTGDAGT-ITDGQLFYQG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2166 RIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAR-EDVHGFKQLCAYYV-------SGGQTTAArLRKQLSQTLASYM 2237
Cdd:TIGR01734  394 RLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKyNKDHKVEYLIAAIVpetedfeKEFQLTKA-IKKELKKSLPAYM 472
                          490       500
                   ....*....|....*....|....
gi 166797876  2238 VPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:TIGR01734  473 IPRKFIYRDQLPLTANGKIDRKAL 496
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
3287-3778 2.87e-78

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 270.61  E-value: 2.87e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3287 ELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPD 3366
Cdd:PRK04813    6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3367 SPSERIRYILNDSSISVLLYCGKLQDDIGFSGTC-IDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEH 3445
Cdd:PRK04813   86 SPAERIEMIIEVAKPSLIIATEELPLEILGIPVItLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3446 RQVIHLIEGLSrqvySAYDAELNIAML--APYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGT 3523
Cdd:PRK04813  166 DNLVSFTNWML----EDFALPEGPQFLnqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVST 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3524 PAHLKLLIAAGDLQGVT---LQHLLIGGEALSKTTVNKLKQLFgehgaaPG--ITNVYGPTETCVDASlfNIECSSDAWA 3598
Cdd:PRK04813  242 PSFADMCLLDPSFNEEHlpnLTHFLFCGEELPHKTAKKLLERF------PSatIYNTYGPTEATVAVT--SIEITDEMLD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3599 RSqNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpFVPEDRMYRTGDLARlLPD 3678
Cdd:PRK04813  314 QY-KRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAGY-LED 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3679 GNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGY-------FAADKTIqISELRKRMAR 3751
Cdd:PRK04813  389 GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYvvpkeedFEREFEL-TKAIKKELKE 467
                         490       500
                  ....*....|....*....|....*..
gi 166797876 3752 HLPGYMIPAHFVQLDKMPLTPNGKLNR 3778
Cdd:PRK04813  468 RLMEYMIPRKFIYRDSLPLTPNGKIDR 494
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
4925-5335 1.01e-77

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 266.17  E-value: 1.01e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4925 PVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVR-EEAVQVIKSQVEFSME-R 5002
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEvR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5003 YEATAD-EVEECFRAFVR-----PFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGKE---- 5072
Cdd:cd19539    83 DLSDPDsDRERRLEELLReresrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5073 --LAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFhEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEE 5150
Cdd:cd19539   163 apLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRL-RGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5151 LTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFE 5230
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5231 HQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQTDIEVD-SLAVRPYEQTETAAKFDLQLNFLIDQDEIQGSFDYCT 5309
Cdd:cd19539   322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAgGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYAT 401
                         410       420
                  ....*....|....*....|....*.
gi 166797876 5310 KLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19539   402 SLFDEETIQGFLADYLQVLRQLLANP 427
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
2827-3250 1.15e-77

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 266.10  E-value: 1.15e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2827 VYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYsgWND--TPLQIVYKTQTPQ 2904
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFT--WRDraEPLQYVRDDLAPP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2905 IHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSAL 2984
Cdd:cd19547    79 WALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2985 QEGREPEPLSAVPYSDYIEWLD-RQDQG-AAKRYWSGYLEgykgETTLLHKIAQHEQKEYAYANLICRFDHEQTKQLQQI 3062
Cdd:cd19547   159 AHGREPQLSPCRPYRDYVRWIRaRTAQSeESERFWREYLR----DLTPSPFSTAPADREGEFDTVVHEFPEQLTRLVNEA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3063 ANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQNAL 3142
Cdd:cd19547   235 ARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3143 ASQSYDTYPLYEIQAQTEQKQ----NLIDHIMIFENYPigqqaeETGHHGTELNIT--NFHMQEHSHYDLNVVVIPGKQL 3216
Cdd:cd19547   315 TTAAHGHVPLAQIKSWASGERlsggRVFDNLVAFENYP------EDNLPGDDLSIQiiDLHAQEKTEYPIGLIVLPLQKL 388
                         410       420       430
                  ....*....|....*....|....*....|....
gi 166797876 3217 AVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19547   389 AFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1521-2312 3.05e-77

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 285.81  E-value: 3.05e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1521 LPKDHHAAEDGRYVPEKVTCDISSDltskmKRTAGKHHVTLNTLLqTAWAVLLQKYNRSRDVVFGSvvSGRPAGIPNVet 1600
Cdd:TIGR03443   14 LPHDYLRPANNRLVEATYSLQLPSA-----EVTAGGGSTPFIILL-AAFAALVYRLTGDEDIVLGT--SSNKSGRPFV-- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1601 miglfintipVRFRCEAGTTFAELMKEAQERAVASQKFETHPLYDIQARTTQKQDLITHLMIFEnypvdqymesIGRQNG 1680
Cdd:TIGR03443   84 ----------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFR----------LAFQDA 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1681 TSITISNVQMEEQTnyDFNLTVIPG-DEMNISFEYNANVYERASIERVREHFMQILHQVVTDADIRVDQAELLTEGERRT 1759
Cdd:TIGR03443  144 PDNQQTTYSTGSTT--DLTVFLTPSsPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSL 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1760 LlqtlndtaaPFPQT---------PVHQLFEEQSQRTPDQAAVI---------DKDRQLTYGELNKRANRLARTLRAKGV 1821
Cdd:TIGR03443  222 L---------PDPTKdldwsgfrgAIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLKTGI 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1822 QTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQ--AGIVL-----MQRDVRKQLAYEGVTV-- 1892
Cdd:TIGR03443  293 KRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKprALIVIekagtLDQLVRDYIDKELELRte 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1893 -----LLDDES----SYHQDGSD-LAPisdVSHLAY----VI----------YTSGSTGRPKGVLIEHGGLTNYIWWAKE 1948
Cdd:TIGR03443  373 ipalaLQDDGSlvggSLEGGETDvLAP---YQALKDtptgVVvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMAK 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1949 VYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGED--KTALLESIVRDPRVDIIKLTPAHLQVLKEMNIADQT 2026
Cdd:TIGR03443  450 RFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDigTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIP 529
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2027 AVRRMIVGGENLSTRLARSIHEQFEGrIEICNEYGPTET--VVGcmiyrYDAAKDRRES----------VPIGTAAANTS 2094
Cdd:TIGR03443  530 SLHHAFFVGDILTKRDCLRLQTLAEN-VCIVNMYGTTETqrAVS-----YFEIPSRSSDstflknlkdvMPAGKGMKNVQ 603
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2095 IYVLDENMKPAPIGVP--GEIYISGAGVARGYLNRPELTAEKFVDDPF-------------EPGAK---------MYKTG 2150
Cdd:TIGR03443  604 LLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkenNKPERefwlgprdrLYRTG 683
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2151 DLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAAR------ 2224
Cdd:TIGR03443  684 DLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSDELEefksev 763
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2225 ----------------------LRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPD-------FELQDRAEYK 2275
Cdd:TIGR03443  764 ddeessdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaqlaavAKNRSASAAD 843
                          890       900       910
                   ....*....|....*....|....*....|....*....
gi 166797876  2276 APRTKAEEILVSAWESVLGAENVSIL--DNFFDLGGDSI 2312
Cdd:TIGR03443  844 EEFTETEREIRDLWLELLPNRPATISpdDSFFDLGGHSI 882
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2828-3250 6.48e-77

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 263.54  E-value: 6.48e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2828 YPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYsgWNDT--PLQIVYKTQTPQI 2905
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFI--EDGLgqPVQVVHRQAQVPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2906 HFADLRDIEEhlREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDR-KYHLIWSFHHIVMDGWCLSLITKEVFDHYSAL 2984
Cdd:cd19536    80 TELDLTPLEE--QLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDEReRFLLVISDHHSILDGWSLYLLVKEILAVYNQL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2985 QEGREPEPLSAVPYSDYIEWLDRQDQGAA-KRYWSGYLEGYKGETtlLHKIAQHEQKEyAYANLICRFDHEQTKQLQQIA 3063
Cdd:cd19536   158 LEYKPLSLPPAQPYRDFVAHERASIQQAAsERYWREYLAGATLAT--LPALSEAVGGG-PEQDSELLVSVPLPVRSRSLA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3064 NQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRCDEDsTFADTMQMVQQNALA 3143
Cdd:cd19536   235 KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQELE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3144 SQSYDTYPLYEIQAQTEQkQNLIDHIMIFENYPIGQQAEETGHHGTELnITNFHMQEHSHYDLNVVVIP-GKQLAVHFGF 3222
Cdd:cd19536   314 SLSHEQVPLADIQRCSEG-EPLFDSIVNFRHFDLDFGLPEWGSDEGMR-RGLLFSEFKSNYDVNLSVLPkQDRLELKLAY 391
                         410       420
                  ....*....|....*....|....*...
gi 166797876 3223 NENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19536   392 NSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK12316 PRK12316
peptide synthase; Provisional
4916-5346 6.54e-77

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 288.39  E-value: 6.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4916 PKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQ 4995
Cdd:PRK12316   42 AGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLD 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4996 ----VEF-------SMERYEATADEVEecfRAFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKL 5064
Cdd:PRK12316  122 rpleVEFedcsglpEAEQEARLRDEAQ---RESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEF 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5065 IQLYDG------KELAPLRIQYKDFTEWKH---QKEQRERiksQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNF 5135
Cdd:PRK12316  199 SRFYSAyatgaePGLPALPIQYADYALWQRswlEAGEQER---QLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEF 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5136 TLDKTVTQGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFL 5215
Cdd:PRK12316  276 SIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVA 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5216 DYITETKETMLKAFEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTeQTDIE----VDSLAVRPYEQTETAAKFDLQ 5291
Cdd:PRK12316  356 TLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPL-VADIEaldtVAGLEFGQLEWKSRTTQFDLT 434
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 5292 LNFLIDQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQLSE 5346
Cdd:PRK12316  435 LDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLD 489
PRK12467 PRK12467
peptide synthase; Provisional
4925-5345 1.54e-76

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 287.06  E-value: 1.54e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4925 PVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMERYE 5004
Cdd:PRK12467   51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5005 ATA---DEVEECFRAFV-----RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGK----- 5071
Cdd:PRK12467  131 LANeqgRARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgre 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5072 -ELAPLRIQYKDFTEW-KHQKEQRERIKsQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLE 5149
Cdd:PRK12467  211 pSLPALPIQYADYAIWqRSWLEAGERER-QLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALA 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5150 ELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAF 5229
Cdd:PRK12467  290 QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQ 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5230 EHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTeQTDIEVD------SLAVRPYEQTETAAKFDLQLNFLIDQDEIQG 5303
Cdd:PRK12467  370 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNT-ATGGRDRegaqlpGLTVEELSWARHTAQFDLALDTYESAQGLWA 448
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 166797876 5304 SFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQLS 5345
Cdd:PRK12467  449 AFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLL 490
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
3887-4298 1.75e-74

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 256.95  E-value: 1.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAA-FEAEW 3965
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVrFRIEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3966 YQGEEDDA------DLYIRQFIRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEG-----E 4034
Cdd:cd19066    82 IDLRNLADpearllELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4035 TLPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQ 4114
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4115 TESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEH 4194
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4195 QDYPFEVLIDQLNIARDLSRNPLFDTMFVLQNTEQEQLEINDVTF-KPYPNGHTMAKFDLTLTAVEEGAG-IQFTLEYLT 4272
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGTVFDLDLEASEDPDGdLLLRLEYSR 401
                         410       420
                  ....*....|....*....|....*.
gi 166797876 4273 ALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19066   402 GVYDERTIDRFAERYMTALRQLIENP 427
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
3283-3787 1.03e-73

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 257.38  E-value: 1.03e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3283 KTIHELFEeQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLP 3362
Cdd:TIGR01734    1 KLIEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3363 IDPDSPSERIRYILNDSSISVLLYCGKLQDDigFSGTCI-------DLMEEHFYHEKDSSLAlsyqSSQLAYAIYTSGTT 3435
Cdd:TIGR01734   80 VDTSIPSERIEMIIEAAGPELVIHTAELSID--AVGTQIitlsaleQAETSGGPVSFDHAVK----GDDNYYIIYTSGST 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3436 GKPKGTLIEHRQVIHLIEglsrQVYSAYDAELNIAML--APYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYR 3513
Cdd:TIGR01734  154 GNPKGVQISHDNLVSFTN----WMLADFPLSEGKQFLnqAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3514 QHSIDITDGTPAHLKLLIAAGDL---QGVTLQHLLIGGEALSKTTVNKLKQLFgehgAAPGITNVYGPTETCVDASlfNI 3590
Cdd:TIGR01734  230 KTGLNVWVSTPSFVDMCLLDPNFnqeNYPHLTHFLFCGEELPVKTAKALLERF----PKATIYNTYGPTEATVAVT--SV 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3591 ECSSDAWARSQNyVPIG--KPlgRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpFVPEDRMYR 3668
Cdd:TIGR01734  304 KITQEILDQYPR-LPIGfaKP--DMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYR 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3669 TGDLARLlPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEY-YLCGYFAA-----DKTIQI 3742
Cdd:TIGR01734  378 TGDAGTI-TDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKVeYLIAAIVPetedfEKEFQL 456
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 166797876  3743 S-ELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKK 3787
Cdd:TIGR01734  457 TkAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAEEVNG 502
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
4334-4818 5.89e-73

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 255.21  E-value: 5.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4334 IHQLfEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPID 4413
Cdd:PRK04813    5 IETI-EEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4414 PELPEKRRAFMLKDSGADVLLTCAGhaIPPLFEG-EVLLLDD--PLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGV 4490
Cdd:PRK04813   84 VSSPAERIEMIIEVAKPSLIIATEE--LPLEILGiPVITLDElkDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4491 QLEHKtmtNLLAY----EQDH---TQLRFdrvLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGI 4563
Cdd:PRK04813  162 QISHD---NLVSFtnwmLEDFalpEGPQF---LNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4564 QT-----AFLPTAFLKLLASEKHYFEpfaecVDHIIAAGEQLIA--TRMLRDMLArhQVTLHNHYGPSETHV-VTMYTVd 4635
Cdd:PRK04813  236 NVwvstpSFADMCLLDPSFNEEHLPN-----LTHFLFCGEELPHktAKKLLERFP--SATIYNTYGPTEATVaVTSIEI- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4636 pdTDQELQ-----PIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpYDSNQRMYKTGD 4710
Cdd:PRK04813  308 --TDEMLDqykrlPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGD 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4711 LArYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAAL--LKHVQEAVVLAKeNTDGQSD-LYAY-------FTAEQSLSiS 4780
Cdd:PRK04813  383 AG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLrqSSYVESAVVVPY-NKDHKVQyLIAYvvpkeedFEREFELT-K 459
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 166797876 4781 QLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK04813  460 AIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
404-745 6.66e-73

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 248.74  E-value: 6.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 HLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKET 483
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  484 FaiqNAIKQERITHFSTSPRLLKTMIEQMNR--EDFIHVQHVVVGGEQLETDTVEKLHSLqPRIRINNEYGPTE-NSVVS 560
Cdd:cd04433    81 L---ELIEREKVTILLGVPTLLARLLKAPESagYDLSSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTEtGGTVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  561 TFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDL 640
Cdd:cd04433   157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GWYRTGDL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  641 ARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELS 718
Cdd:cd04433   230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPgaDLDAEELRAHVR 309
                         330       340
                  ....*....|....*....|....*..
gi 166797876  719 RELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:cd04433   310 ERLAPYKVPRRVVFVDALPRTASGKID 336
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
4334-4818 9.87e-73

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 254.30  E-value: 9.87e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4334 IHQLFEQqAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPID 4413
Cdd:TIGR01734    3 IEAIQAF-AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4414 PELPEKRRAFMLKDSGADVLLTCAGHAIPpLFEGEVLLLddPLLYQGRTDNLNLS----CSENDLMYVIYTSGTTGQPKG 4489
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIHTAELSID-AVGTQIITL--SALEQAETSGGPVSfdhaVKGDDNYYIIYTSGSTGNPKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4490 VQLEHktmTNLLAYE----QDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQT 4565
Cdd:TIGR01734  159 VQISH---DNLVSFTnwmlADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4566 -----AFLPTAFLKLLASEKHYFEpfaecVDHIIAAGEQLiATRMLRDMLARH-QVTLHNHYGPSETHV-VTMYTVDPDT 4638
Cdd:TIGR01734  236 wvstpSFVDMCLLDPNFNQENYPH-----LTHFLFCGEEL-PVKTAKALLERFpKATIYNTYGPTEATVaVTSVKITQEI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4639 DQELQ--PIG--KPISNteIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHpydSNQRMYKTGDLArY 4714
Cdd:TIGR01734  310 LDQYPrlPIGfaKPDMN--LFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH---EGQPAYRTGDAG-T 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4715 LPEGNIEYAGRRDHQVKIRGYRVELGEVEAAL--LKHVQEAVVLAKENTDGQSD-LYAY-------FTAEQSLSiSQLKE 4784
Cdd:TIGR01734  384 ITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLrqSSYIESAVVVPKYNKDHKVEyLIAAivpetedFEKEFQLT-KAIKK 462
                          490       500       510
                   ....*....|....*....|....*....|....
gi 166797876  4785 KLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:TIGR01734  463 ELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3887-4298 8.02e-72

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 249.16  E-value: 8.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEwy 3966
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQ-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3967 qgEEDDADLY---IRQFIR-----PFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIY----EGE 4034
Cdd:cd20484    80 --EEDISSLKeseIIAYLRekakePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallQGK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4035 --TLPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLA 4112
Cdd:cd20484   158 qpTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4113 SQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAY 4192
Cdd:cd20484   238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4193 EHQDYPFEVLIDQLNIARDLSRNPLFDTMF----VLQNTEQEQLEindvtfKPYPNG---------HTMAKFDLTLTAVE 4259
Cdd:cd20484   318 DHAAYPFPAMVRDLNIPRSQANSPVFQVAFfyqnFLQSTSLQQFL------AEYQDVlsiefvegiHQEGEYELVLEVYE 391
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 166797876 4260 EGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd20484   392 QEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
265-749 7.29e-70

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 244.78  E-value: 7.29e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  265 VYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLD 344
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  345 PEYPKERLQYLLHDADADVLLVQHHLKNSLAFD-----GPVIDLNDeasyhadcsllspvaghshLAYVIYTSGTTGKPK 419
Cdd:cd05936    81 PLYTPRELEHILNDSGAKALIVAVSFTDLLAAGaplgeRVALTPED-------------------VAVLQYTSGTTGVPK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  420 GVMVEHGGIV-NSLQWKKAF-FKHSPADRVLVLYPY--VFdAFILNFFGPLISGATLHLLPNEENKETFaiqNAIKQERI 495
Cdd:cd05936   142 GAMLTHRNLVaNALQIKAWLeDLLEGDDVVLAALPLfhVF-GLTVALLLPLALGATIVLIPRFRPIGVL---KEIRKHRV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  496 THFSTSPRLLKTMIEQMNRE--DFIHVQHVVVGGEQLETDTVEKLHSLQpRIRINNEYGPTENSVVSTFHPVQSADEQIT 573
Cdd:cd05936   218 TIFPGVPTMYIALLNAPEFKkrDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVNPLDGPRKPGS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  574 IGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpGqkMYKTGDLARWLPDGRIEYLG 653
Cdd:cd05936   297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-----G--WLRTGDIGYMDEDGYFFIVD 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  654 RIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFI 731
Cdd:cd05936   370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEgaSLTEEEIIAFCREQLAGYKVPRQVE 449
                         490
                  ....*....|....*...
gi 166797876  732 PLERIPLTSNGKIDLKAL 749
Cdd:cd05936   450 FRDELPKSAVGKILRREL 467
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
3887-4298 4.21e-68

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 238.26  E-value: 4.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGF-KMADGEPVQYVLDHAAF---E 3962
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLQVVLKDRKLpwrE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3963 AEWYQGEEDDADLYIRQF-----IRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGE--- 4034
Cdd:cd19543    82 LDLSHLSEAEQEAELEALaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALgeg 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4035 ---TLPPLRiQYKDYAVWqtgearLQQIQKQEA--YW---LELYSGDVPvlhLPADYIRPSARDFAGATMHFTLDKQKSD 4106
Cdd:cd19543   162 qppSLPPVR-PYRDYIAW------LQRQDKEAAeaYWreyLAGFEEPTP---LPKELPADADGSYEPGEVSFELSAELTA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4107 GLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPhADL---EPIIGMFVNTLAMRNYPEKGKTFSQYLSE 4183
Cdd:cd19543   232 RLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELpgiETMVGLFINTLPVRVRLDPDQTVLELLKD 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4184 VKENALKAYEHQDYPfevLID-QlniARDLSRNPLFDTMFVLQN-----TEQEQLEINDVTFKPyPNGHTMAKFDLTLTA 4257
Cdd:cd19543   311 LQAQQLELREHEYVP---LYEiQ---AWSEGKQALFDHLLVFENypvdeSLEEEQDEDGLRITD-VSAEEQTNYPLTVVA 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 166797876 4258 VeEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19543   384 I-PGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1318-1740 1.45e-67

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 236.82  E-value: 1.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1318 IYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYrgWKD--QPLQIIFKTKKIG 1395
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFT--WRDraEPLQYVRDDLAPP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1396 FQFNDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFAL 1475
Cdd:cd19547    79 WALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1476 LQQKQPEQSSITPYSQYIEWLGRQDAK--EAAAYWDQYLegyEEQTGLPKDHHAAE-DGRYvpEKVTCDISSDLTSKMKR 1552
Cdd:cd19547   159 AHGREPQLSPCRPYRDYVRWIRARTAQseESERFWREYL---RDLTPSPFSTAPADrEGEF--DTVVHEFPEQLTRLVNE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1553 TAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFAELMkEAQERA 1632
Cdd:cd19547   234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLL-ETIHRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1633 VASQKFETH-PLYDIQARTTQKQ----DLITHLMIFENYPVDQYMEsigrqNGTSITISNVQMEEQTNYDFNLTVIPGDE 1707
Cdd:cd19547   313 LATTAAHGHvPLAQIKSWASGERlsggRVFDNLVAFENYPEDNLPG-----DDLSIQIIDLHAQEKTEYPIGLIVLPLQK 387
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 1708 MNISFEYNANVYERASIERVREHFMQILHQVVT 1740
Cdd:cd19547   388 LAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCR 420
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
3889-4120 2.39e-67

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 229.15  E-value: 2.39e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3889 VSSAQKRLYilnHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAF------- 3961
Cdd:COG4908     1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLplevvdl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3962 -EAEWYQGEEDDADLYIRQFIRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGE------ 4034
Cdd:COG4908    78 sALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALlegepp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4035 TLPPLRIQYKDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLASQ 4114
Cdd:COG4908   158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                  ....*.
gi 166797876 4115 TESTLY 4120
Cdd:COG4908   238 HGATVN 243
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1319-1741 5.77e-67

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 235.00  E-value: 5.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1319 YPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDqPLQIIF-KTKKIGFQ 1397
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGR-YEQVVLdKTVRFRIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1398 FNDLREMKESqkEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQ 1477
Cdd:cd19066    81 IIDLRNLADP--EARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPEQSSITPYSQYIEWLGRQDAKEA----AAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKRT 1553
Cdd:cd19066   159 QKPTLPPPVGSYADYAAWLEKQLESEAaqadLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1554 AGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQErav 1633
Cdd:cd19066   239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKE--- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1634 ASQKFETH-----PLYDI---QARTTQKQDLITHLMIFENYPvdqymESIGRQNGTSITISNVQMEEQTNYDFNLTVIPG 1705
Cdd:cd19066   314 QSREAIEHqrvpfIELVRhlgVVPEAPKHPLFEPVFTFKNNQ-----QQLGKTGGFIFTTPVYTSSEGTVFDLDLEASED 388
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 166797876 1706 --DEMNISFEYNANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19066   389 pdGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIEN 426
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
264-751 1.82e-65

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 233.91  E-value: 1.82e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   264 TVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPL 343
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   344 DPEYPKERLQYLLHDADADVLLVQ--------------HHLKNSLAFDGPVIDLNDEASYHADC-----SLLSPVAGH-- 402
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSserldllhpalpgcHDLRTLIIVGDPAHASEGHPGEEPASwpkllALGDADPPHpv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   403 --SHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATL----HLLP 476
Cdd:TIGR03098  161 idSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhdYLLP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   477 NEenketfaIQNAIKQERITHFSTSPRLLKTMIE-QMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTE 555
Cdd:TIGR03098  241 RD-------VLKALEKHGITGLAAVPPLWAQLAQlDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   556 nSVVSTFHPVQSADEQIT-IGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKF------VEHLH 628
Cdd:TIGR03098  314 -AFRSTYLPPEEVDRRPDsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrplppfPGELH 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   629 VPGQKMYkTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV--GEP 706
Cdd:TIGR03098  393 LPELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTppGGE 471
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 166797876   707 SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPA 751
Cdd:TIGR03098  472 ELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
289-749 7.38e-64

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 226.97  E-value: 7.38e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNslAFDGPVIDLNDEASYHADCsllspvaghshLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd17654    97 ELDN--APLSFTPEHRHFNIRTDEC-----------LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQNAI-KQERITHFSTSPRLLKTMIEQMNREDFI----HVQHV 523
Cdd:cd17654   164 LTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQSIKSTVLsatsSLRVL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  524 VVGGEQLETDTVEK-LHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYIlgahHQIQPIGIPGELY 602
Cdd:cd17654   244 ALGGEPFPSLVILSsWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEV----RDQNGSEGTGQVF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  603 VGgaGVARGYLNRPELTeekfvehlhVPGQKMYKTGDLARwLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVr 682
Cdd:cd17654   320 LG--GLNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV- 386
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  683 EAAVVAREDADgakQLYAYYVGEPSlTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd17654   387 ESCAVTLSDQQ---RLIAFIVGESS-SSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1915-2256 2.98e-63

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 221.00  E-value: 2.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1915 HLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTAL 1994
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1995 LESIvRDPRVDIIKLTPAHLQVL-KEMNIA--DQTAVRRMIVGGENLSTRLARSIHEQFegRIEICNEYGPTETVVGCMI 2071
Cdd:cd04433    81 LELI-EREKVTILLGVPTLLARLlKAPESAgyDLSSLRALVSGGAPLPPELLERFEEAP--GIKLVNGYGLTETGGTVAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2072 YRYDAAKDRRESVpiGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDdpfepgaKMYKTGD 2151
Cdd:cd04433   158 GPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GWYRTGD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2152 LAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQT--TAARLRKQL 2229
Cdd:cd04433   229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdlDAEELRAHV 308
                         330       340
                  ....*....|....*....|....*..
gi 166797876 2230 SQTLASYMVPAYFIELDEMPLTSNGKI 2256
Cdd:cd04433   309 RERLAPYKVPRRVVFVDALPRTASGKI 335
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3888-4297 4.34e-63

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 224.06  E-value: 4.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFE---AE 3964
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHlivID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3965 WYQGEEDDADL--YIRQFIR-PFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEG-------E 4034
Cdd:cd20483    83 LSEAADPEAALdqLVRNLRRqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlragrdlA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4035 TLPPLRIQYKDYAVWQtgEARLQQ--IQKQEAYWLELYSG--DVPVLhLP-ADYIRPSARDFAGATMHFTLDKQKSDGLK 4109
Cdd:cd20483   163 TVPPPPVQYIDFTLWH--NALLQSplVQPLLDFWKEKLEGipDASKL-LPfAKAERPPVKDYERSTVEATLDKELLARMK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4110 QLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENAL 4189
Cdd:cd20483   240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4190 KAYEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQnTEQEQLEINDVTFKPYPNGHTMAK--FDLTLTAVEEGA-GIQF 4266
Cdd:cd20483   320 EAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-VHGKFPEYDTGDFKFTDYDHYDIPtaCDIALEAEEDPDgGLDL 398
                         410       420       430
                  ....*....|....*....|....*....|.
gi 166797876 4267 TLEYLTALFKPETIERMMGHFEQLVDSIIKQ 4297
Cdd:cd20483   399 RLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2828-3250 9.20e-63

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 223.05  E-value: 9.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2828 YPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVY-KTQTPQIH 2906
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLdKTVRFRIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2907 FADLRDIEEhlREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQE 2986
Cdd:cd19066    81 IIDLRNLAD--PEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2987 GREPEPLSAVPYSDYIEWLDRQDQGAAK----RYWSGYLEGYKGETTLLHKIAQHEQKEYAYANLICRFDHEQTKQLQQI 3062
Cdd:cd19066   159 QKPTLPPPVGSYADYAAWLEKQLESEAAqadlAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3063 ANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAeiPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQNAL 3142
Cdd:cd19066   239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3143 ASQSYDTYPLYEIQAQTEQKQN-----LIDHIMIFENYPIGQQAEETGHHGTELnitnFHMQEHSHYDLNVVVIPG--KQ 3215
Cdd:cd19066   317 EAIEHQRVPFIELVRHLGVVPEapkhpLFEPVFTFKNNQQQLGKTGGFIFTTPV----YTSSEGTVFDLDLEASEDpdGD 392
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 166797876 3216 LAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19066   393 LLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1778-2261 1.08e-62

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 223.98  E-value: 1.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDSQA--GIVLMQ-RDVRKQLAYEGVTVLLDDESsyhqdgsdlapisdvshLAYVIYTSGSTGRPKGVLI 1934
Cdd:cd05936    83 YTPRELEHILNDSGAkaLIVAVSfTDLLAAGAPLGERVALTPED-----------------VAVLQYTSGTTGVPKGAML 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1935 EHGGL----TNYIWWAKEVYVKGEK--ANFPLYSsiSFDLTVtSIFTPLVTGNAII-VYDGEDKTALLEsiVRDPRVDII 2007
Cdd:cd05936   146 THRNLvanaLQIKAWLEDLLEGDDVvlAALPLFH--VFGLTV-ALLLPLALGATIVlIPRFRPIGVLKE--IRKHRVTIF 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2008 KLTPAHLQVL---KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRieICNEYGPTET---VVGCMIYRydaaKDRR 2081
Cdd:cd05936   221 PGVPTMYIALlnaPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP--IVEGYGLTETspvVAVNPLDG----PRKP 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2082 ESvpIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmyKTGDLAKWLADGNI 2161
Cdd:cd05936   295 GS--IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYF 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2162 EYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVP 2239
Cdd:cd05936   366 FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVlkEGASLTEEEIIAFCREQLAGYKVP 445
                         490       500
                  ....*....|....*....|..
gi 166797876 2240 AYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05936   446 RQVEFRDELPKSAVGKILRREL 467
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1318-1742 2.86e-62

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 220.64  E-value: 2.86e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1318 IYPLTPMQKGMLFHSLFDPNSgaYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPL-QIIFKTKKIGF 1396
Cdd:cd19542     1 IYPCTPMQEGMLLSQLRSPGL--YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFlQVVLKSLDPPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1397 qfndlrEMKESQKEAmIQKYAREDKMRGFdLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLItkeifENYFALL 1476
Cdd:cd19542    79 ------EEVETDEDS-LDALTRDLLDDPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPII-----LRDLAAA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1477 QQKQPEQSSiTPYSQYIEWLGRQDAKEAAAYWDQYLEGYEEQTgLPKDHHAAEDGRYVpekvtcDISSDLTSKMKRTAGK 1556
Cdd:cd19542   146 YNGQLLPPA-PPFSDYISYLQSQSQEESLQYWRKYLQGASPCA-FPSLSPKRPAERSL------SSTRRSLAKLEAFCAS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1557 HHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERAVASQ 1636
Cdd:cd19542   218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1637 KFETHPLYDIQARTTQK--QDLITHLMIFENYPVDQYMESIGrqngtSITISNVQMEEQTNYDFNLTVIP-GDEMNISFE 1713
Cdd:cd19542   298 PHQHLSLREIQRALGLWpsGTLFNTLVSYQNFEASPESELSG-----SSVFELSAAEDPTEYPVAVEVEPsGDSLKVSLA 372
                         410       420
                  ....*....|....*....|....*....
gi 166797876 1714 YNANVYERASIERVREHFMQILHQVVTDA 1742
Cdd:cd19542   373 YSTSVLSEEQAEELLEQFDDILEALLANP 401
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
852-1279 3.50e-62

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 221.13  E-value: 3.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  852 LTPIQ--HWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFeKTPDGYAPRITgTDESELFHLEV 929
Cdd:cd19066     4 LSPMQrgMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQVV-LDKTVRFRIEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  930 MNYKGETDP-AQAIADKANEIQSSMVLDKGPLMKLGLFQC-PDGDHLLIAIHHLLIDGVSWRILLEDFASGYEQAERRQT 1007
Cdd:cd19066    82 IDLRNLADPeARLLELIDQIQQTIYDLERGPLVRVALFRLaDERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1008 IqLPQKTDSFPFWADQLSKYAAETDMEEEIAYWTEL--SSIKPQPLPKDTISEgslLRDSEEV--TIQWTKEETEQLLKQ 1083
Cdd:cd19066   162 T-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYlhGLPPPLPLPKAKRPS---QVASYEVltLEFFLRSEETKRLRE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1084 ANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGRepiiPDADISRTIGWFTSQYPVVLRMEAGKNLSQRIKIVKE 1163
Cdd:cd19066   238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1164 GLRRIPDKGMNY--SIIKYISGHPEADSLQLkPEISFNYLGQFDQDLKHQALRispfstgLSMNE-NQERTAVLDLNGMI 1240
Cdd:cd19066   314 QSREAIEHQRVPfiELVRHLGVVPEAPKHPL-FEPVFTFKNNQQQLGKTGGFI-------FTTPVyTSSEGTVFDLDLEA 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 166797876 1241 AE---GTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHC 1279
Cdd:cd19066   386 SEdpdGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2827-3250 5.07e-62

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 220.69  E-value: 5.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2827 VYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVYKTQTPQIH 2906
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVQVILPPLPLPLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2907 FADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQE 2986
Cdd:cd19531    80 VVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2987 GREPePLSAVP--YSDYIEWLDRQDQGAA----KRYWSGYLEgykGETTLLhkiaqhE---------QKEYAYANLICRF 3051
Cdd:cd19531   160 GRPS-PLPPLPiqYADYAVWQREWLQGEVlerqLAYWREQLA---GAPPVL------ElptdrprpaVQSFRGARVRFTL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3052 DHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAeiPDVEQMIGLFINTIPVRIRCDEDSTFA 3131
Cdd:cd19531   230 PAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNR--AELEGLIGFFVNTLVLRTDLSGDPTFR 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3132 DTMQMVQQNALASQSYDTYPLyeiqaqtEQkqnLIDHI---------------MIFENYPiGQQAEETGHHGTELNITNf 3196
Cdd:cd19531   308 ELLARVRETALEAYAHQDLPF-------EK---LVEALqperdlsrsplfqvmFVLQNAP-AAALELPGLTVEPLEVDS- 375
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 3197 hmqEHSHYDLNVVVIPGKQ-LAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19531   376 ---GTAKFDLTLSLTETDGgLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
4924-5335 9.09e-62

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 219.97  E-value: 9.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4924 YPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFS---- 4999
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFriei 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5000 ---MERYEATADEVEECFRAFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDG-----K 5071
Cdd:cd19066    82 idlRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5072 ELAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEEL 5151
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5152 TGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEH 5231
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5232 QEYPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQTDIEVDSLAV-RPYEQTETAAKFDLQLNFLIDQD-EIQGSFDYCT 5309
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGTVFDLDLEASEDPDgDLLLRLEYSR 401
                         410       420
                  ....*....|....*....|....*.
gi 166797876 5310 KLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19066   402 GVYDERTIDRFAERYMTALRQLIENP 427
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
2827-3250 1.27e-61

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 218.32  E-value: 1.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2827 VYPLTPMQKGMLFHSLLDeaSSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWNDTPLQIVykTQTPQIH 2906
Cdd:cd19545     1 IYPCTPLQEGLMALTARQ--PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVV--VKESPIS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2907 FADLRDIEEhlredaiaaYQREDKAKGFDLArDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYsalqe 2986
Cdd:cd19545    77 WTESTSLDE---------YLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2987 gREPEPLSAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKGE--TTLLHKIAQHEQkeyayanlicrfDHEQTKQLQQIAN 3064
Cdd:cd19545   142 -QGEPVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfPPLPSSRYQPRP------------DATLEHSISLPSS 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3065 -QHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQNALA 3143
Cdd:cd19545   209 aSSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLD 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3144 SQSYDTYPLYEIQAQTEQKQN--LIDHIMIFENypigqQAEETGHHGTELNITNFHMQ--EHSHYDLNVVV-IPGKQLAV 3218
Cdd:cd19545   289 MIPFEHTGLQNIRRLGPDARAacNFQTLLVVQP-----ALPSSTSESLELGIEEESEDleDFSSYGLTLECqLSGSGLRV 363
                         410       420       430
                  ....*....|....*....|....*....|..
gi 166797876 3219 HFGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19545   364 RARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2827-3250 3.06e-61

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 217.56  E-value: 3.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2827 VYPLTPMQKGMLFHSLLDEasSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWND-TPLQIVYKTQTPQI 2905
Cdd:cd19542     1 IYPCTPMQEGMLLSQLRSP--GLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEgTFLQVVLKSLDPPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2906 HfadlrdiEEHLREDAIAAYQREDKAKGFdLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLItkevFDHYSALQ 2985
Cdd:cd19542    79 E-------EVETDEDSLDALTRDLLDDPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPII----LRDLAAAY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2986 EGREPEPlsAVPYSDYIEWLDRQDQGAAKRYWSGYLEGYKGET--TLLHKIAQHEQkeyayanlICRFDhEQTKQLQQIA 3063
Cdd:cd19542   147 NGQLLPP--APPFSDYISYLQSQSQEESLQYWRKYLQGASPCAfpSLSPKRPAERS--------LSSTR-RSLAKLEAFC 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3064 NQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQNALA 3143
Cdd:cd19542   216 ASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3144 SQSYDTYPLYEIQA--QTEQKQNLIDHIMIFENypIGQQAEETGHHGTELNITNFHMqeHSHYDLNV-VVIPGKQLAVHF 3220
Cdd:cd19542   296 SLPHQHLSLREIQRalGLWPSGTLFNTLVSYQN--FEASPESELSGSSVFELSAAED--PTEYPVAVeVEPSGDSLKVSL 371
                         410       420       430
                  ....*....|....*....|....*....|
gi 166797876 3221 GFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19542   372 AYSTSVLSEEQAEELLEQFDDILEALLANP 401
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1788-2264 3.65e-61

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 221.24  E-value: 3.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVI-------DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQ 1860
Cdd:cd17647     2 PERTCVVetpslnsSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1861 DRIRYMLDDSQ-AGIVLMQRdvrkqlayEGVTVllddessyhqdGSDLAPIsdvshlayVIYTSGSTGRPKGVLIEHGGL 1939
Cdd:cd17647    82 ARQNIYLGVAKpRGLIVIRA--------AGVVV-----------GPDSNPT--------LSFTSGSEGIPKGVLGRHFSL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1940 TNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGED--KTALLESIVRDPRVDIIKLTPAHLQVL 2017
Cdd:cd17647   135 AYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQLL 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2018 KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEgRIEICNEYGPTETVVGCMIYRYDAA-------KDRRESVPIGTAA 2090
Cdd:cd17647   215 TAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAE-NVRIVNMYGTTETQRAVSYFEVPSRssdptflKNLKDVMPAGRGM 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2091 ANTSIYVLDEN--MKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF-EPGA---------------------KM 2146
Cdd:cd17647   294 LNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvEPDHwnyldkdnnepwrqfwlgprdRL 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2147 YKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAAR-- 2224
Cdd:cd17647   374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDEsf 453
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 2225 ---------------------------LRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAP 2264
Cdd:cd17647   454 aqedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
269-745 5.20e-61

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 217.86  E-value: 5.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  269 FEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYP 348
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  349 KERLQYLLHDADADVLLvqhhlknslafdgpvidlndeasyhadcsllspvaghSHLAYVIYTSGTTGKPKGVMVEHGGI 428
Cdd:cd17631    81 PPEVAYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  429 VNSLQWKKAFFKHSPADRVLVLYPyVFDAFILNFFGP--LISGATLHLLPNEENKETFAiqnAIKQERITHFSTSPRLLK 506
Cdd:cd17631   124 LWNAVNALAALDLGPDDVLLVVAP-LFHIGGLGVFTLptLLRGGTVVILRKFDPETVLD---LIERHRVTSFFLVPTMIQ 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  507 TMI--EQMNREDFIHVQHVVVGGEQLETDTvekLHSLQPR-IRINNEYGPTENSVVSTFHPVQSADEQI-TIGSPVANHQ 582
Cdd:cd17631   200 ALLqhPRFATTDLSSLRAVIYGGAPMPERL---LRALQARgVKFVQGYGMTETSPGVTFLSPEDHRRKLgSAGRPVFFVE 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  583 AYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpGqkMYKTGDLARWLPDGRIEYLGRIDHQVKIR 662
Cdd:cd17631   277 VRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD-----G--WFHTGDLGRLDEDGYLYIVDRKKDMIISG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  663 GYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTS 740
Cdd:cd17631   350 GENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPgaELDEDELIAHCRERLARYKIPKSVEFVDALPRNA 429

                  ....*
gi 166797876  741 NGKID 745
Cdd:cd17631   430 TGKIL 434
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2364-2788 7.14e-61

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 217.28  E-value: 7.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2364 LTPIQ--HWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFrTTENGCEAQ-NEEIAQSglYRLE 2440
Cdd:cd19066     4 LSPMQrgMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQvVLDKTVR--FRIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2441 VMNLKEDPDPGRTIEAKADEIQSSMH-LSDGPLMKAGLFQCAD-GDHLLIAIHHLIIDGISWRILLEDIVSGYKQAENGR 2518
Cdd:cd19066    81 IIDLRNLADPEARLLELIDQIQQTIYdLERGPLVRVALFRLADeRDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2519 VIqLPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTKIEQ--TEVKPLPKDFHETHTTAKDSETAAVEWTKEETElLLKQA 2596
Cdd:cd19066   161 PT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHglPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETK-RLREV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2597 NRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREqiiqDIDISRTVGWFTSLYPVVLHAQPGKEISDYIKTTKEG 2676
Cdd:cd19066   239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP----DEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2677 LRQIPHKGIGYGIARYLSGG----MPSKLNPEISFNYLGQFDQdlqrHGVQLSSYSCGSDSSGHQERPYVLNINGMI-TD 2751
Cdd:cd19066   315 SREAIEHQRVPFIELVRHLGvvpeAPKHPLFEPVFTFKNNQQQ----LGKTGGFIFTTPVYTSSEGTVFDLDLEASEdPD 390
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 166797876 2752 GRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHC 2788
Cdd:cd19066   391 GDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1785-2258 1.85e-60

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 216.32  E-value: 1.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIR 1864
Cdd:cd17631     6 RRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1865 YMLDDSQAgivlmqrdvrkqlayegvTVLLDDessyhqdgsdlapisdvshLAYVIYTSGSTGRPKGVLIEHGGLT-NYI 1943
Cdd:cd17631    86 YILADSGA------------------KVLFDD-------------------LALLMYTSGTTGRPKGAMLTHRNLLwNAV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1944 WW-------AKEVYVkgekANFPLYSSISFDLTVTSIftpLVTGNAIIVYDGEDKTALLESIVRDpRVDIIKLTPAHLQV 2016
Cdd:cd17631   129 NAlaaldlgPDDVLL----VVAPLFHIGGLGVFTLPT---LLRGGTVVILRKFDPETVLDLIERH-RVTSFFLVPTMIQA 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2017 L---KEMNIADQTAVRRMIVGGENLSTRLARsiheQFEGR-IEICNEYGPTETVVGCMIYRYDAAKDRRESVpiGTAAAN 2092
Cdd:cd17631   201 LlqhPRFATTDLSSLRAVIYGGAPMPERLLR----ALQARgVKFVQGYGMTETSPGVTFLSPEDHRRKLGSA--GRPVFF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2093 TSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmyKTGDLAKWLADGNIEYAGRIDEQVK 2172
Cdd:cd17631   275 VEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMII 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2173 IRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPL 2250
Cdd:cd17631   348 SGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVprPGAELDEDELIAHCRERLARYKIPKSVEFVDALPR 427

                  ....*...
gi 166797876 2251 TSNGKINK 2258
Cdd:cd17631   428 NATGKILK 435
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3888-4298 3.37e-60

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 215.01  E-value: 3.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKM--ADGEPVQYVLDHAAFEAEW 3965
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTdpEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3966 YQGE-EDDADLYIRQF-IRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGETLPPLRIQY 4043
Cdd:cd19532    83 VQISdEAEVEEEFERLkNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4044 KDYAVWQTGEARLQQIQKQEAYWLELYSGDVPVL------HLPAdyiRPSARDFAGATMHFTLDKQKSDGLKQLASQTES 4117
Cdd:cd19532   163 LDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLpllpfaKVKS---RPPLTRYDTHTAERRLDAALAARIKEASRKLRV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4118 TLYMVLLASYTLLLSKYSGQEDIIVGspI--AGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQ 4195
Cdd:cd19532   240 TPFHFYLAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4196 DYPFEVLIDQLNIARDLSRNPLFDTMF--VLQNTEQEQL---EINDVTFKPYPNGhtmakFDLTLTAVEEGAG---IQFT 4267
Cdd:cd19532   318 RVPFDVLLDELGVPRSATHSPLFQVFInyRQGVAESRPFgdcELEGEEFEDARTP-----YDLSLDIIDNPDGdclLTLK 392
                         410       420       430
                  ....*....|....*....|....*....|.
gi 166797876 4268 LEylTALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19532   393 VQ--SSLYSEEDAELLLDSYVNLLEAFARDP 421
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1788-2256 3.23e-59

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 216.90  E-value: 3.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKD-----RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDR 1862
Cdd:COG0365    23 GDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 IRYMLDDSQAGIVL---------MQRDVRKQLA----------------YEGVTVLLDDESSYH---QDGSDLAPISDVS 1914
Cdd:COG0365   103 LADRIEDAEAKVLItadgglrggKVIDLKEKVDealeelpslehvivvgRTGADVPMEGDLDWDellAAASAEFEPEPTD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1915 --HLAYVIYTSGSTGRPKGVLIEHGG-LTNYIWWAKEVyvkgekanfplyssisFDLT-------------VT----SIF 1974
Cdd:COG0365   183 adDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYV----------------LDLKpgdvfwctadigwATghsyIVY 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1975 TPLVTGNAIIVYDG----EDKTALLEsIVRDPRVDIIKLTPAHLQVLKEMNIA-----DQTAVRRMIVGGENLSTRLARS 2045
Cdd:COG0365   247 GPLLNGATVVLYEGrpdfPDPGRLWE-LIEKYGVTVFFTAPTAIRALMKAGDEplkkyDLSSLRLLGSAGEPLNPEVWEW 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2046 IHEQFeGrIEICNEYGPTETVvGCMIyrydAAKDRRESVP--IGTAAANTSIYVLDENMKPAPIGVPGEIYISGA--GVA 2121
Cdd:COG0365   326 WYEAV-G-VPIVDGWGQTETG-GIFI----SNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2122 RGYLNRPELTAEKFVDDpfEPGakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAR 2201
Cdd:COG0365   399 RGYWNDPERYRETYFGR--FPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGV 474
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2202 EDVHGFKQLCAYYV-----SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKI 2256
Cdd:COG0365   475 PDEIRGQVVKAFVVlkpgvEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
276-750 6.99e-59

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 214.69  E-value: 6.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  276 TPENAAVKFKNdhLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYL 355
Cdd:cd17647    10 TPSLNSSKTRS--FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  356 LHDADADVLLVqhhLKNSLAFDGPviDLNDEASYhadcsllspvaghshlayviyTSGTTGKPKGVMVEHGGIVNSLQWK 435
Cdd:cd17647    88 LGVAKPRGLIV---IRAAGVVVGP--DSNPTLSF---------------------TSGSEGIPKGVLGRHFSLAYYFPWM 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  436 KAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLhLLPNEENKET---FAIQNAIKQERITHFStsPRLLKTMIEQM 512
Cdd:cd17647   142 AKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTQDDIGTpgrLAEWMAKYGATVTHLT--PAMGQLLTAQA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  513 NrEDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENS-VVSTFH-PVQSADEQ--------ITIGSPVANHQ 582
Cdd:cd17647   219 T-TPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQrAVSYFEvPSRSSDPTflknlkdvMPAGRGMLNVQ 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  583 AYILGAH--HQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHV----------------------PGQKMYKTG 638
Cdd:cd17647   298 LLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlgPRDRLYRTG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  639 DLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQF----- 713
Cdd:cd17647   378 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESfaqed 457
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876  714 ------------------------REELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALP 750
Cdd:cd17647   458 vpkevstdpivkgligyrklikdiREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1319-1741 5.92e-58

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 208.75  E-value: 5.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1319 YPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKKIGFQF 1398
Cdd:cd19531     2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1399 NDLREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQ 1478
Cdd:cd19531    81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1479 KQPEQS--SItpysQYI-------EWLGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSK 1549
Cdd:cd19531   161 RPSPLPplPI----QYAdyavwqrEWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1550 MKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQ 1629
Cdd:cd19531   237 LRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNR--AELEGLIGFFVNTLVLRTDLSGDPTFRELLARVR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1630 ERAVASQK-----FE-------------THPLYDIqarttqkqdlithLMIFENYPVDQymesigrQNGTSITISNVQME 1691
Cdd:cd19531   315 ETALEAYAhqdlpFEklvealqperdlsRSPLFQV-------------MFVLQNAPAAA-------LELPGLTVEPLEVD 374
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166797876 1692 EQT-NYDFNLTVIP-GDEMNISFEYNANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19531   375 SGTaKFDLTLSLTEtDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVAD 426
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
4926-5148 6.95e-58

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 201.81  E-value: 6.95e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4926 VSSVQKMVYLttqIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMER--- 5002
Cdd:COG4908     1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVvdl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5003 ----YEATADEVEECFRAFV-RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGKE----- 5072
Cdd:COG4908    78 salpEPEREAELEELVAEEAsRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 5073 -LAPLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQL 5148
Cdd:COG4908   158 pLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKAL 234
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
3297-3781 4.36e-57

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 206.94  E-value: 4.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQ----FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERI 3372
Cdd:cd17654     1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3373 RYILNDSSISVLLYCGKLqddiGFSGTCIDLMEEHFyhekDSSLALSyqssqLAYAIYTSGTTGKPKGTLIEHRQVIHLI 3452
Cdd:cd17654    81 LTVMKKCHVSYLLQNKEL----DNAPLSFTPEHRHF----NIRTDEC-----LAYVIHTSGTTGTPKIVAVPHKCILPNI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3453 EGLSRQVYSAYDaelNIAMLA-PYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCR-YYRQHSIDITDGTPAHLKLL 3530
Cdd:cd17654   148 QHFRSLFNITSE---DILFLTsPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRF 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3531 IAAGDLQGV-----TLQHLLIGGEALSKTTVNK--LKQLFGEHgaapgITNVYGPTETCVDASLFNIEcssdawaRSQNY 3603
Cdd:cd17654   225 GSQSIKSTVlsatsSLRVLALGGEPFPSLVILSswRGKGNRTR-----IFNIYGITEVSCWALAYKVP-------EEDSP 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3604 VPIGKPLGRNRMYILDskkrLQPKGVQGELYIAgdGVGRGYLNLPELTdekfvadpfVPEDRMYRTGDLARlLPDGNIEY 3683
Cdd:cd17654   293 VQLGSPLLGTVIEVRD----QNGSEGTGQVFLG--GLNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFF 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3684 IGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAalkdaddeyylcgYFAADKTIQI-------SELRKRMARH-LPG 3755
Cdd:cd17654   357 LGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-------------LSDQQRLIAFivgesssSRIHKELQLTlLSS 423
                         490       500
                  ....*....|....*....|....*.
gi 166797876 3756 YMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd17654   424 HAIPDTFVQIDKLPLTSHGKVDKSEL 449
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4924-5335 8.27e-57

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 205.63  E-value: 8.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4924 YPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKS--QVEFSME 5001
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPskPLSFQEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5002 RYEA-TADEVEECFRAFVR-PFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKL----IQLYDGKE--L 5073
Cdd:cd20484    82 DISSlKESEIIAYLREKAKePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLldayQALLQGKQptL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5074 APLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTG 5153
Cdd:cd20484   162 ASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5154 STAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEHQE 5233
Cdd:cd20484   242 INLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5234 YPFEELVEKLGVKRDLSRNPLFDTMFVLQNTEQT-------DIEVDSLAVRPYEQTETAAKFDLQLNFLIDQDEIQGSFD 5306
Cdd:cd20484   322 YPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQStslqqflAEYQDVLSIEFVEGIHQEGEYELVLEVYEQEDRFTLNIK 401
                         410       420
                  ....*....|....*....|....*....
gi 166797876 5307 YCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd20484   402 YNPDLFDASTIERMMEHYVKLAEELIANP 430
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
259-771 1.11e-56

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 209.20  E-value: 1.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  259 FSGSRT--VYQLFEEQAERTPENAAVKFKND-----HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSII 331
Cdd:COG0365     3 FVGGRLniAYNCLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  332 AVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLV---------QHHLKNSLA----------------FDGPVIDLNDE 386
Cdd:COG0365    83 ACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITadgglrggkVIDLKEKVDealeelpslehvivvgRTGADVPMEGD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  387 ASYHAdcsLLSPVAGH--------SHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWK-KAFFKHSPADRVL--------V 449
Cdd:COG0365   163 LDWDE---LLAAASAEfepeptdaDDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTaKYVLDLKPGDVFWctadigwaT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  450 LYPYVFdafilnfFGPLISGATLHLL---PNEENKETFAiqNAIKQERITHFSTSP----RLLKTMIEQMNREDFIHVQH 522
Cdd:COG0365   240 GHSYIV-------YGPLLNGATVVLYegrPDFPDPGRLW--ELIEKYGVTVFFTAPtairALMKAGDEPLKKYDLSSLRL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  523 VVVGGEQLETDTVEKLHSlQPRIRINNEYGPTE-NSVVSTFHPVQsadeQITIGS---PVANHQAYILGAHHQIQPIGIP 598
Cdd:COG0365   311 LGSAGEPLNPEVWEWWYE-AVGVPIVDGWGQTEtGGIFISNLPGL----PVKPGSmgkPVPGYDVAVVDEDGNPVPPGEE 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  599 GELYVGGA--GVARGYLNRPELTEEKFVEHlhVPGqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMF 676
Cdd:COG0365   386 GELVIKGPwpGMFRGYWNDPERYRETYFGR--FPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALV 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  677 NLENVREAAVVAREDADGAKQLYAYYVGEPSLTA-AQFREEL----SRELPNYMIPSRFIPLERIPLTSNGKIDLKALPA 751
Cdd:COG0365   462 SHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPsDELAKELqahvREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
                         570       580
                  ....*....|....*....|
gi 166797876  752 adentRAENEYIAPRNTIEE 771
Cdd:COG0365   542 -----IAEGRPLGDTSTLED 556
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
3297-3784 1.21e-56

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 208.14  E-value: 1.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEG-------KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPS 3369
Cdd:cd17647     2 PERTCVVETPslnssktRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3370 ERIRYILNDSSISVLLYCGKLQDDIGfsgtcidlmeehfyheKDSSLALSYqssqlayaiyTSGTTGKPKGTLIEHRQVI 3449
Cdd:cd17647    82 ARQNIYLGVAKPRGLIVIRAAGVVVG----------------PDSNPTLSF----------TSGSEGIPKGVLGRHFSLA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3450 HLIEGLSRQVYSAYDAELNiaMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKL 3529
Cdd:cd17647   136 YYFPWMAKRFNLSENDKFT--MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3530 LIAAGDLQGVTLQHLLIGGEALSKTTVNKLKQLfgehgaAPG--ITNVYGPTETCVDASLFNI-ECSSD-AWARSQNYV- 3604
Cdd:cd17647   214 LTAQATTPFPKLHHAFFVGDILTKRDCLRLQTL------AENvrIVNMYGTTETQRAVSYFEVpSRSSDpTFLKNLKDVm 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 PIGKPLGRNRMYILDSKKRLQPKGVQ--GELYIAGDGVGRGYLNLPELTDEKFVADPFV--------------------- 3661
Cdd:cd17647   288 PAGRGMLNVQLLVVNRNDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwl 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3662 -PEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAA---- 3736
Cdd:cd17647   368 gPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPrfdk 447
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 3737 ---------DKTIQISE----------------LRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAP 3784
Cdd:cd17647   448 pddesfaqeDVPKEVSTdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
4473-4813 1.41e-56

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 201.74  E-value: 1.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 DLMYVIYTSGTTGQPKGVQLEHKTM-TNLLAYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGneaKRDI 4551
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLlAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4552 RQLNDFVRTHGIQTAFL-PTAFLKLLASEKHYFEPFAeCVDHIIAAGEQLIATRmLRDMLARHQVTLHNHYGPSETHVVT 4630
Cdd:cd04433    78 EAALELIEREKVTILLGvPTLLARLLKAPESAGYDLS-SLRALVSGGAPLPPEL-LERFEEAPGIKLVNGYGLTETGGTV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4631 MYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPhpydsnqRMYKTGD 4710
Cdd:cd04433   156 ATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GWYRTGD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4711 LARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSIS--QLKEKL 4786
Cdd:cd04433   229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHpgVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeELRAHV 308
                         330       340
                  ....*....|....*....|....*..
gi 166797876 4787 AGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:cd04433   309 RERLAPYKVPRRVVFVDALPRTASGKI 335
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1788-2261 2.42e-55

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 201.93  E-value: 2.42e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVID----KDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRI 1863
Cdd:cd17654     1 PDRPALIIdqttSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1864 RYMLDDSQAgivlmqrdvrKQLAYEGvtvLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYI 1943
Cdd:cd17654    81 LTVMKKCHV----------SYLLQNK---ELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1944 WWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTA---LLESIVRDPRVDIIKLTPAHL-----Q 2015
Cdd:cd17654   148 QHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLpskLADILFKRHRITVLQATPTLFrrfgsQ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 VLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCMIYRydaAKDRRESVPIGTAAANTSI 2095
Cdd:cd17654   228 SIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYK---VPEEDSPVQLGSPLLGTVI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2096 YVLDENmkpapiGVPGEIYISGAGVARGYLNRPELTAekfvddpfePGAKMYKTGDLAKwLADGNIEYAGRIDEQVKIRG 2175
Cdd:cd17654   305 EVRDQN------GSEGTGQVFLGGLNRVCILDDEVTV---------PKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRG 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2176 YRIELGEIEAALLQEEVIkEAVVTAREDVhgfKQLCAYYVSGGQTTAARLRKQLSQtLASYMVPAYFIELDEMPLTSNGK 2255
Cdd:cd17654   369 KRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESSSSRIHKELQLTL-LSSHAIPDTFVQIDKLPLTSHGK 443

                  ....*.
gi 166797876 2256 INKKGL 2261
Cdd:cd17654   444 VDKSEL 449
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
4336-4818 4.59e-55

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 201.64  E-value: 4.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4336 QLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPE 4415
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4416 LPEKRRAFMLKDSGADVLLTcaghAIPplFEGEVLLLDDPLLYQGRTdnlnlscsENDLMYVIYTSGTTGQPKGVQLEHK 4495
Cdd:cd05936    83 YTPRELEHILNDSGAKALIV----AVS--FTDLLAAGAPLGERVALT--------PEDVAVLQYTSGTTGVPKGAMLTHR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4496 TMT-NLL---AYEQDHTQLRfDRVLQ----FAAMSFDVCyqeMFSALSSGGILFIIGNeaKRDIRQLNDfVRTHGIqTAF 4567
Cdd:cd05936   149 NLVaNALqikAWLEDLLEGD-DVVLAalplFHVFGLTVA---LLLPLALGATIVLIPR--FRPIGVLKE-IRKHRV-TIF 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4568 --LPTAFLKLLASEKHYFEPFAEcVDHIIAAGEQLiATRMLRDMLARHQVTLHNHYGPSETHVVTmyTVDP-DTDQELQP 4644
Cdd:cd05936   221 pgVPTMYIALLNAPEFKKRDFSS-LRLCISGGAPL-PVEVAERFEELTGVPIVEGYGLTETSPVV--AVNPlDGPRKPGS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4645 IGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpyDSnqrMYKTGDLARYLPEGNIEYAG 4724
Cdd:cd05936   297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV----DG---WLRTGDIGYMDEDGYFFIVD 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4725 RRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA--EQSLSISQLKEKLAGQIPGYMIPSYFI 4800
Cdd:cd05936   370 RKKDMIIVGGFNVYPREVEEVLYEHpaVAEAAVVGVPDPYSGEAVKAFVVLkeGASLTEEEIIAFCREQLAGYKVPRQVE 449
                         490
                  ....*....|....*...
gi 166797876 4801 QLEKLPLTGNGKVNRRAL 4818
Cdd:cd05936   450 FRDELPKSAVGKILRREL 467
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1795-2257 5.27e-55

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 202.06  E-value: 5.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1795 DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGI 1874
Cdd:cd05911     6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1875 VLMQRD----VRKQLAYEGVT---VLLDDESSYHQDGSDL--------------APISDVSHLAYVIYTSGSTGRPKGVL 1933
Cdd:cd05911    86 IFTDPDglekVKEAAKELGPKdkiIVLDDKPDGVLSIEDLlsptlgeededlppPLKDGKDDTAAILYSSGTTGLPKGVC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1934 IEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFD--LTVTSIFTPLVTGNAIIVYDGEDKTALLESIVRDpRVDIIKLTP 2011
Cdd:cd05911   166 LSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKY-KITFLYLVP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2012 AHLQVLKEMNIADQTA---VRRMIVGGENLSTRLARSIHEQFeGRIEICNEYGPTETVVGCMIYRYDAAKdrRESVpiGT 2088
Cdd:cd05911   245 PIAAALAKSPLLDKYDlssLRVILSGGAPLSKELQELLAKRF-PNATIKQGYGMTETGGILTVNPDGDDK--PGSV--GR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2089 AAANTSIYVLDEN-MKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRI 2167
Cdd:cd05911   320 LLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVDRK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2168 DEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASY---MVPAYF 2242
Cdd:cd05911   394 KELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrkPGEKLTEKEVKDYVAKKVASYkqlRGGVVF 473
                         490
                  ....*....|....*
gi 166797876 2243 IelDEMPLTSNGKIN 2257
Cdd:cd05911   474 V--DEIPKSASGKIL 486
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2830-3071 5.36e-55

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 193.72  E-value: 5.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2830 LTPMQKGMLFhslLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVYKTQTPQIHFAD 2909
Cdd:COG4908     1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2910 LRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQEGRE 2989
Cdd:COG4908    77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2990 PE-PLSAVPYSDYIEWLDRQDQG----AAKRYWSGYLEGYKGETTLLHKIAQHEQKEYAYANLICRFDHEQTKQLQQIAN 3064
Cdd:COG4908   157 PPlPELPIQYADYAAWQRAWLQSealeKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236

                  ....*..
gi 166797876 3065 QHQVTLN 3071
Cdd:COG4908   237 AHGATVN 243
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
4333-4820 9.09e-55

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 202.32  E-value: 9.09e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPI 4412
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4413 DPELPEKRRAFMLKDSGADVLLTCA-------------------------GHAIPPLFEGEVLLLDDpLLYQGRTDNLNl 4467
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSerldllhpalpgchdlrtliivgdpAHASEGHPGEEPASWPK-LLALGDADPPH- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4468 SCSENDLMYVIYTSGTTGQPKGVQLEHKTMtnLLAYEQDHTQLRF---DRVLQFAAMSFDVCYQEMFSALSSGGILFIIG 4544
Cdd:TIGR03098  159 PVIDSDMAAILYTSGSTGRPKGVVLSHRNL--VAGAQSVATYLENrpdDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4545 NEAKRDIRQLndfVRTHGIQT-AFLPTAFLKLlaSEKHYFEPFAECVDHIIAAGEQL--IATRMLRDMLARHQVTLhnHY 4621
Cdd:TIGR03098  237 YLLPRDVLKA---LEKHGITGlAAVPPLWAQL--AQLDWPESAAPSLRYLTNSGGAMprATLSRLRSFLPNARLFL--MY 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4622 GPSETHVVTmyTVDPD-TDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYD 4700
Cdd:TIGR03098  310 GLTEAFRST--YLPPEeVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPF 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  4701 SNQRMYK-----TGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAAL--LKHVQEAVVLA-KENTDGQS-DLYAYF 4771
Cdd:TIGR03098  388 PGELHLPelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAyaTGLVAEAVAFGvPDPTLGQAiVLVVTP 467
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 166797876  4772 TAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPM 4820
Cdd:TIGR03098  468 PGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4925-5335 1.52e-54

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 198.83  E-value: 1.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4925 PVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRT--VVEMVREEAVQVIKSQVEFSME- 5001
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTcfFTDPEDGEPMQGVLASSPLRLEh 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5002 RYEATADEVEECFRAFV-RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGKELAPLRIQY 5080
Cdd:cd19532    83 VQISDEAEVEEEFERLKnHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5081 KDFTEWKHQKEQRERIKSQEEYWLGVFH---EELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTA- 5156
Cdd:cd19532   163 LDFAARQRQDYESGALDEDLAYWKSEFStlpEPLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPf 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5157 --YMilfSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEHQEY 5234
Cdd:cd19532   243 hfYL---AALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5235 PFEELVEKLGVKRDLSRNPLFDTMF--VLQNTEQTDIEVDSLAVRPYEQTETAakFDLQLNflIDQDEIQGSF------D 5306
Cdd:cd19532   320 PFDVLLDELGVPRSATHSPLFQVFInyRQGVAESRPFGDCELEGEEFEDARTP--YDLSLD--IIDNPDGDCLltlkvqS 395
                         410       420
                  ....*....|....*....|....*....
gi 166797876 5307 YctkLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19532   396 S---LYSEEDAELLLDSYVNLLEAFARDP 421
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
286-744 2.49e-54

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 200.13  E-value: 2.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  286 NDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLL 365
Cdd:cd05911     8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  366 VQHH----LKNSLAFDGP---VIDLNDEASYHAD-CSLLSPVAG-------------HSHLAYVIYTSGTTGKPKGVMVE 424
Cdd:cd05911    88 TDPDglekVKEAAKELGPkdkIIVLDDKPDGVLSiEDLLSPTLGeededlppplkdgKDDTAAILYSSGTTGLPKGVCLS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  425 HGGIV-NSLQWKKAFFKH-SPADRVLVLYP--YVFDAFILNFFgpLISGATLHLLPNEENkETFAiqNAIKQERITHFST 500
Cdd:cd05911   168 HRNLIaNLSQVQTFLYGNdGSNDVILGFLPlyHIYGLFTTLAS--LLNGATVIIMPKFDS-ELFL--DLIEKYKITFLYL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  501 SPRLLKTMIE--QMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTEnSVVSTFHPVQSADEQITIGSPV 578
Cdd:cd05911   243 VPPIAAALAKspLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE-TGGILTVNPDGDDKPGSVGRLL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  579 ANHQAYILGAH-HQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHlhvpgqKMYKTGDLARWLPDGRIEYLGRIDH 657
Cdd:cd05911   322 PNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED------GWLHTGDIGYFDEDGYLYIVDRKKE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  658 QVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPS--LTAAQFREELSRELPNYM-----IpsRF 730
Cdd:cd05911   396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGekLTEKEVKDYVAKKVASYKqlrggV--VF 473
                         490
                  ....*....|....
gi 166797876  731 IPleRIPLTSNGKI 744
Cdd:cd05911   474 VD--EIPKSASGKI 485
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1776-2263 3.81e-54

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 200.39  E-value: 3.81e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPID 1855
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1856 PEYPQDRIRYMLDDSQAGIVLMQRDVRKQL------AYEGVTVLLDDESSYHQDG---------------SDLAPISDV- 1913
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTSSERLDLLhpalpgCHDLRTLIIVGDPAHASEGhpgeepaswpkllalGDADPPHPVi 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1914 -SHLAYVIYTSGSTGRPKGVLIEHgglTNYIWWAKEV--YVKGEKAN-----FPLyssiSFDLTVTSIFTPLVTGNAIIV 1985
Cdd:TIGR03098  162 dSDMAAILYTSGSTGRPKGVVLSH---RNLVAGAQSVatYLENRPDDrllavLPL----SFDYGFNQLTTAFYVGATVVL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1986 YDGEDKTALLESIVRDPRVDIIKLTPAHLQvLKEMNI--ADQTAVRRMIVGGENLSTRLARSIHEQFEgRIEICNEYGPT 2063
Cdd:TIGR03098  235 HDYLLPRDVLKALEKHGITGLAAVPPLWAQ-LAQLDWpeSAAPSLRYLTNSGGAMPRATLSRLRSFLP-NARLFLMYGLT 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2064 ETVVGcmIYRYDAAKDRRESvPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDP-FEP 2142
Cdd:TIGR03098  313 EAFRS--TYLPPEEVDRRPD-SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpFPG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2143 GAKMYKT----GDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGG 2218
Cdd:TIGR03098  390 ELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPG 469
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 166797876  2219 QTTAAR--LRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPA 2263
Cdd:TIGR03098  470 GEELDRaaLLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
4923-5335 4.74e-54

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 197.43  E-value: 4.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4923 VYPVSSVQK-MVYLTTqIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTV-VEMVREEAVQVIKSQVEFSM 5000
Cdd:cd19543     1 IYPLSPMQEgMLFHSL-LDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSfVWEGLGEPLQVVLKDRKLPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5001 ERY---EATADEVEECFRAFV-----RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGK- 5071
Cdd:cd19543    80 RELdlsHLSEAEQEAELEALAeedreRGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5072 -----ELAPLRiQYKDFTEW--KHQKEQRERiksqeeYW---LGVFHEELPsfeLPKDFARPPVRSFDGKRHNFTLDKTV 5141
Cdd:cd19543   160 egqppSLPPVR-PYRDYIAWlqRQDKEAAEA------YWreyLAGFEEPTP---LPKELPADADGSYEPGEVSFELSAEL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5142 TQGIKQL---EELTGSTaymILFSAYSILLAKYSGQDDIVVGTPIAGRPhADL---EPIIGMFVNTLAIRTAPMAEKTFL 5215
Cdd:cd19543   230 TARLQELarqHGVTLNT---VVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELpgiETMVGLFINTLPVRVRLDPDQTVL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5216 DYITETKETMLKAFEHQEYPFEELveklgVKRDLSRNPLFDTMFVLQN-----TEQTDIEVDSLAVRPyEQTETAAKFDL 5290
Cdd:cd19543   306 ELLKDLQAQQLELREHEYVPLYEI-----QAWSEGKQALFDHLLVFENypvdeSLEEEQDEDGLRITD-VSAEEQTNYPL 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 166797876 5291 QLNFLIDqDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19543   380 TVVAIPG-EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
4331-4818 6.46e-54

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 200.03  E-value: 6.46e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4331 PTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFL 4410
Cdd:PRK06187    5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4411 PIDPELPEKRRAFMLKDSGADVLLTCAGHA-----IPPLFEGE--VLLLDDPLLYQGRTDNLNLS--------------C 4469
Cdd:PRK06187   85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVpllaaILPQLPTVrtVIVEGDGPAAPLAPEVGEYEellaaasdtfdfpdI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4470 SENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF-DRVL----QFAAMSFDVCYQEMFSALSsgGILfiig 4544
Cdd:PRK06187  165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRdDVYLvivpMFHVHAWGLPYLALMAGAK--QVI---- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4545 neAKR-DIRQLNDFVRTHGIQTAFL-PTAFLKLLAsekhyfEPFAECVD----HIIAAGEQLIATRMLRDMLARHQVTLH 4618
Cdd:PRK06187  239 --PRRfDPENLLDLIETERVTFFFAvPTIWQMLLK------APRAYFVDfsslRLVIYGGAALPPALLREFKEKFGIDLV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4619 NHYGPSETH-VVTMYTVDPDTDQELQ---PIGKPISNTEIFILNEAGTLQPV--GIVGELCISGVSLARGYHNRESLTLE 4692
Cdd:PRK06187  311 QGYGMTETSpVVSVLPPEDQLPGQWTkrrSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4693 TFVpHPYdsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRG---YRVELgevEAALLKH--VQEAVVLAKEntDGQSD- 4766
Cdd:PRK06187  391 TID-GGW------LHTGDVGYIDEDGYLYITDRIKDVIISGGeniYPREL---EDALYGHpaVAEVAVIGVP--DEKWGe 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 4767 -LYAYFTAE--QSLSISQLKEKLAGQIPGYMIPS--YFIqlEKLPLTGNGKVNRRAL 4818
Cdd:PRK06187  459 rPVAVVVLKpgATLDAKELRAFLRGRLAKFKLPKriAFV--DELPRTSVGKILKRVL 513
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
3424-3775 1.86e-53

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 192.89  E-value: 1.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3424 QLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYsaYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKeivS 3503
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG--LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---F 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3504 DGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGV---TLQHLLIGGEALSKTTVNKLKQLFGehgaaPGITNVYGPTE 3580
Cdd:cd04433    76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYdlsSLRALVSGGAPLPPELLERFEEAPG-----IKLVNGYGLTE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3581 TCVDASLfnieCSSDAWARSqnYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpf 3660
Cdd:cd04433   151 TGGTVAT----GPPDDDARK--PGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD----- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3661 vpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYF--AADK 3738
Cdd:cd04433   220 --EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVvlRPGA 297
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 166797876 3739 TIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK 3775
Cdd:cd04433   298 DLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
264-749 2.26e-53

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 198.49  E-value: 2.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  264 TVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPL 343
Cdd:PRK06187    7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  344 DPEYPKERLQYLLHDADADVLLVQHHLKNSLA---------------FDGPVIDLNDEA-SYHAdcsLLS--------PV 399
Cdd:PRK06187   87 NIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAailpqlptvrtviveGDGPAAPLAPEVgEYEE---LLAaasdtfdfPD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  400 AGHSHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQwKKAFFKHSPADRVLVLYPyVFDAFILN-FFGPLISGATLhLLPN 477
Cdd:PRK06187  164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLFlHSLA-VCAWLKLSRDDVYLVIVP-MFHVHAWGlPYLALMAGAKQ-VIPR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  478 EenketFAIQNAIKQ---ERITHFSTSPRLLkTMIEQMNRE---DFIHVQHVVVGG----EQLETDTVEKLhslqpRIRI 547
Cdd:PRK06187  241 R-----FDPENLLDLietERVTFFFAVPTIW-QMLLKAPRAyfvDFSSLRLVIYGGaalpPALLREFKEKF-----GIDL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  548 NNEYGPTENS-VVSTFHPVQSADEQITI----GSPVANHQAYILGAHHQIQP--IGIPGELYVGGAGVARGYLNRPELTE 620
Cdd:PRK06187  310 VQGYGMTETSpVVSVLPPEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  621 EKFV-EHLHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLY 699
Cdd:PRK06187  390 ETIDgGWLH--------TGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPV 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166797876  700 AYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK06187  462 AVVVLKPgaTLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1768-2276 4.45e-53

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 197.33  E-value: 4.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1768 AAPFPQTpVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKS 1847
Cdd:PRK06187    1 MQDYPLT-IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1848 GGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAY-----EGV-TVLLDDES----------SYH-----QDGSD 1906
Cdd:PRK06187   80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAilpqlPTVrTVIVEGDGpaaplapevgEYEellaaASDTF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1907 LAPISDVSHLAYVIYTSGSTGRPKGVLIEH--------GGLTNYIWWAKEVYVkgekANFPLYSsiSFDLTVTsiFTPLV 1978
Cdd:PRK06187  160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHrnlflhslAVCAWLKLSRDDVYL----VIVPMFH--VHAWGLP--YLALM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 TGnAIIVYDGE-DKTALLESIVRDpRVDIIKLTPAHLQ-VLKEMNIADQ--TAVRRMIVGGENLSTRLARSIHEQFegRI 2054
Cdd:PRK06187  232 AG-AKQVIPRRfDPENLLDLIETE-RVTFFFAVPTIWQmLLKAPRAYFVdfSSLRLVIYGGAALPPALLREFKEKF--GI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2055 EICNEYGPTETV-VGCMIY---RYDAAKDRRESVpiGTAAANTSIYVLDENMKPAP--IGVPGEIYISGAGVARGYLNRP 2128
Cdd:PRK06187  308 DLVQGYGMTETSpVVSVLPpedQLPGQWTKRRSA--GRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRP 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2129 ELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFK 2208
Cdd:PRK06187  386 EATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGE 458
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 2209 QLCAYYV--SGGQTTAARLRKQLSQTLASYMVPA--YFIelDEMPLTSNGKINKKGLpapdfelqdRAEYKA 2276
Cdd:PRK06187  459 RPVAVVVlkPGATLDAKELRAFLRGRLAKFKLPKriAFV--DELPRTSVGKILKRVL---------REQYAE 519
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
263-744 4.98e-53

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 197.05  E-value: 4.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVP 342
Cdd:PRK07656    5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  343 LDPEYPKERLQYLLHDADADVLLVQHHL-------KNSLAFDGPVIDLNDEASYHADCSLLS---------------PVA 400
Cdd:PRK07656   85 LNTRYTADEAAYILARGDAKALFVLGLFlgvdysaTTRLPALEHVVICETEEDDPHTEKMKTftdflaagdpaerapEVD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  401 GhSHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQWkKAFFKHSPADRVLVLYPYvFDAFILN--FFGPLISGATLHLLPN 477
Cdd:PRK07656  165 P-DDVADILFTSGTTGRPKGAMLTHRQLLsNAADW-AEYLGLTEGDRYLAANPF-FHVFGYKagVNAPLMRGATILPLPV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  478 EENKETFAIqnaIKQERITHFSTSPRLLKTMI--EQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTE 555
Cdd:PRK07656  242 FDPDEVFRL---IETERITVLPGPPTMYNSLLqhPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  556 NSVVSTFHPVQSADEQI--TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpg 631
Cdd:PRK07656  319 ASGVTTFNRLDDDRKTVagTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADgwLH--- 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  632 qkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPS--LT 709
Cdd:PRK07656  396 -----TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGaeLT 470
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 166797876  710 AAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK07656  471 EEELIAYCREHLAKYKVPRSIEFLDELPKNATGKV 505
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1318-1742 7.04e-53

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 192.90  E-value: 7.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1318 IYPLTPMQKGMLFHSLFDPnsGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPLQIIFKTKKIGFQ 1397
Cdd:cd19545     1 IYPCTPLQEGLMALTARQP--GAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1398 FndlremkesqkEAMIQKYAREDKMRGFDLeKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFenyfALLQ 1477
Cdd:cd19545    79 E-----------STSLDEYLEEDRAAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVL----AAYQ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPEQSSitPYSQYIEWLGRQDAKEAAAYWDQYLEGYEeqtglPKDHHAAEDGRYVPE-----KVTCDISSDLTSKmkr 1552
Cdd:cd19545   143 GEPVPQPP--PFSRFVKYLRQLDDEAAAEFWRSYLAGLD-----PAVFPPLPSSRYQPRpdatlEHSISLPSSASSG--- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1553 tagkhhVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERA 1632
Cdd:cd19545   213 ------VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDL 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1633 VASQKFETHPLYDIQARTTQKQdlitHLMIFENYPVDQYMESIGRQNGTSITISNVQMEEQTNYDFNLTV---IPGDEMN 1709
Cdd:cd19545   287 LDMIPFEHTGLQNIRRLGPDAR----AACNFQTLLVVQPALPSSTSESLELGIEEESEDLEDFSSYGLTLecqLSGSGLR 362
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 1710 ISFEYNANVYERASIERVREHFMQILHQVVTDA 1742
Cdd:cd19545   363 VRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1321-1562 3.18e-52

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 185.63  E-value: 3.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1321 LTPMQKGMLFHslfDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKKIGFQFND 1400
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1401 LREMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQKQ 1480
Cdd:COG4908    77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1481 PEQSSIT-PYSQYIEWLGRQ----DAKEAAAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKRTAG 1555
Cdd:COG4908   157 PPLPELPiQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236

                  ....*..
gi 166797876 1556 KHHVTLN 1562
Cdd:COG4908   237 AHGATVN 243
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
4356-4821 3.32e-52

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 195.04  E-value: 3.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFML---KDSGAdV 4432
Cdd:cd17647    19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLgvaKPRGL-I 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4433 LLTCAGHAIPPlfegevlllddpllyqgrTDNLNLScsendlmyviYTSGTTGQPKGVQLEHKTmtnlLAYEQDHTQLRF 4512
Cdd:cd17647    98 VIRAAGVVVGP------------------DSNPTLS----------FTSGSEGIPKGVLGRHFS----LAYYFPWMAKRF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4513 -----DRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEKHyfEPFA 4587
Cdd:cd17647   146 nlsenDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQAT--TPFP 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4588 EcVDHIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETH------VVTMYTVDP---DTDQELQPIGKPISNTEIFILN 4658
Cdd:cd17647   224 K-LHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQravsyfEVPSRSSDPtflKNLKDVMPAGRGMLNVQLLVVN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4659 EAGTLQPVGI--VGELCISGVSLARGYHNRESLTLETFVPHPY-----------DSNQ-----------RMYKTGDLARY 4714
Cdd:cd17647   303 RNDRTQICGIgeVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkDNNEpwrqfwlgprdRLYRTGDLGRY 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4715 LPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA----EQSLSISQ------- 4781
Cdd:cd17647   383 LPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHplVRENITLVRRDKDEEPTLVSYIVPrfdkPDDESFAQedvpkev 462
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4782 ------------------LKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMP 4821
Cdd:cd17647   463 stdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
2665-2814 7.07e-52

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 180.93  E-value: 7.07e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2665 EISDYIKTTKEGLRQIPHKGIGYGIARYLSGGMPS---KLNPEISFNYLGQFDQDLQRHGVQLSSYSCGSDSSGHQERPY 2741
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKlaaSPQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRPY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876  2742 VLNINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITHCVHKEQSELTPSDILLKGISIDELDQL 2814
Cdd:TIGR01720   81 ALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1789-2261 9.00e-51

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 188.27  E-value: 9.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1789 DQAAVIDKDRQLTYGELNKRANRLARTLRAKG-VQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLmqrdvrkqlayegvtvllddessyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIEHGGLTNYI---- 1943
Cdd:cd05941    81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVralv 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1944 --W-WAKE-VYVKGekanFPLYSSISfdlTVTSIFTPLVTGnAIIVYDGEDKTALLESIVRDPRVDI--------IKL-- 2009
Cdd:cd05941   123 daWrWTEDdVLLHV----LPLHHVHG---LVNALLCPLFAG-ASVEFLPKFDPKEVAISRLMPSITVfmgvptiyTRLlq 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2010 TPAHLQVLKEMNIADQTAVRRMIVGGenlSTRLARSIHEQFEGRI--EICNEYGPTETVVGcMIYRYDAakDRRE-SVpi 2086
Cdd:cd05941   195 YYEAHFTDPQFARAAAAERLRLMVSG---SAALPVPTLEEWEAITghTLLERYGMTEIGMA-LSNPLDG--ERRPgTV-- 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2087 GTAAANTSIYVLDEN-MKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAG 2165
Cdd:cd05941   267 GMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILG 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2166 RI-DEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQT-TAARLRKQLSQTLASYMVPAY 2241
Cdd:cd05941   341 RSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVlrAGAAAlSLEELKEWAKQRLAPYKRPRR 420
                         490       500
                  ....*....|....*....|
gi 166797876 2242 FIELDEMPLTSNGKINKKGL 2261
Cdd:cd05941   421 LILVDELPRNAMGKVNKKEL 440
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
281-749 2.53e-50

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 187.11  E-value: 2.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  281 AVKFKNDHLTYRELNEKASRLARTL-RNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDA 359
Cdd:cd05941     4 AIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  360 DAdvllvqhhlknSLAFDGpvidlndeasyhadcsllspvaghshlAYVIYTSGTTGKPKGVMVEHGGI---VNSLQ--W 434
Cdd:cd05941    84 EP-----------SLVLDP---------------------------ALILYTSGTTGRPKGVVLTHANLaanVRALVdaW 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  435 kkaffKHSPADRVL-VLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQnaiKQERITHFSTSP----RLLKT-- 507
Cdd:cd05941   126 -----RWTEDDVLLhVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISR---LMPSITVFMGVPtiytRLLQYye 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  508 -MIEQMN---REDFIHVQHVVVGGEQLETDTVEKLHSLQPRiRINNEYGPTEnSVVSTFHPVQSADEQITIGSPVANHQA 583
Cdd:cd05941   198 aHFTDPQfarAAAAERLRLMVSGSAALPVPTLEEWEAITGH-TLLERYGMTE-IGMALSNPLDGERRPGTVGMPLPGVQA 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  584 YILGAH-HQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYLGRI-DHQVKI 661
Cdd:cd05941   276 RIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD------DGWFKTGDLGVVDEDGYYWILGRSsVDIIKS 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV---GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPL 738
Cdd:cd05941   350 GGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVlraGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPR 429
                         490
                  ....*....|.
gi 166797876  739 TSNGKIDLKAL 749
Cdd:cd05941   430 NAMGKVNKKEL 440
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
4355-4818 3.18e-50

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 186.91  E-value: 3.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4355 NQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLL 4434
Cdd:cd17654    14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4435 TcaghaipplfegEVLLLDDPLLYQGRTDNLNLSCSENdLMYVIYTSGTTGQPKGVQLEHKTMTNLLAyeqdHTQLRF-- 4512
Cdd:cd17654    94 Q------------NKELDNAPLSFTPEHRHFNIRTDEC-LAYVIHTSGTTGTPKIVAVPHKCILPNIQ----HFRSLFni 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4513 --DRVLQFAA-MSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQL--NDFVRtHGIQTAFLPTAFLKLLASEKHYFEPFA 4587
Cdd:cd17654   157 tsEDILFLTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLadILFKR-HRITVLQATPTLFRRFGSQSIKSTVLS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4588 --ECVDHIIAAGE---QLIATRMLRDMLARHQVtlHNHYGPSETHVVTMYTVDPDTDQELQpIGKPISNTEIFILNEAGT 4662
Cdd:cd17654   236 atSSLRVLALGGEpfpSLVILSSWRGKGNRTRI--FNIYGITEVSCWALAYKVPEEDSPVQ-LGSPLLGTVIEVRDQNGS 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4663 LQPvgivGELCISGvsLARGYHNRESLTletfVPhpydsNQRMYKTGDLARyLPEGNIEYAGRRDHQVKIRGYRVELGEV 4742
Cdd:cd17654   313 EGT----GQVFLGG--LNRVCILDDEVT----VP-----KGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLI 376
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 4743 EAALLKHVQ-EAVVLAKENtdgQSDLYAYFTAEQSLSISQlKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd17654   377 QQVIESCLGvESCAVTLSD---QQRLIAFIVGESSSSRIH-KELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
1153-1305 6.84e-50

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 175.54  E-value: 6.84e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1153 NLSQRIKIVKEGLRRIPDKGMNYSIIKYISGHPEADSLQLKPEISFNYLGQFDQDLKHQALRISPFSTGLSMNENQERTA 1232
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKLAASPQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRPY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876  1233 VLDLNGMIAEGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHCVSRQQTSLTPSDILLKDISIDELEQL 1305
Cdd:TIGR01720   81 ALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
298-749 9.08e-50

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 186.11  E-value: 9.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  298 ASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGA----YVPLDPEYPKERLQYLLHDADADVLLVQHHLKNS 373
Cdd:cd05922     3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  374 LAF-------DGPVIDLndEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADR 446
Cdd:cd05922    83 LRDalpaspdPGTVLDA--DGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  447 VLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAiqNAIKQERITHFSTSPrllkTMIEQMNREDFI-----HVQ 521
Cdd:cd05922   161 ALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFW--EDLREHGATGLAGVP----STYAMLTRLGFDpaklpSLR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  522 HVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQIT-IGSPVANHQAYILGAHHQIQPIGIPGE 600
Cdd:cd05922   235 YLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTPTPPGEPGE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  601 LYVGGAGVARGYLNRP--ELTEEKFVEHLHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNL 678
Cdd:cd05922   315 IVHRGPNVMKGYWNDPpyRRKEGRGGGVLH--------TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876  679 ENVREAAVVAREDADGAKqLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05922   387 GLIIEAAAVGLPDPLGEK-LALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2364-2605 1.06e-49

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 178.31  E-value: 1.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2364 LTPIQHWFFEQTTTDQHYyNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEaqnEEIAQSGLYRLEVMN 2443
Cdd:COG4908     1 LSPAQKRFLFLEPGSNAY-NIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPV---QRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2444 LKEDPDPGRTIEAK---ADEIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRV 2519
Cdd:COG4908    77 LSALPEPEREAELEelvAEEASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2520 IQLPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTKI--EQTEVKPLPKDFHETHTTAKDSETAAVEWTKEETELLLKQAn 2597
Cdd:COG4908   157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQlaGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA- 235

                  ....*...
gi 166797876 2598 RAYHTEIN 2605
Cdd:COG4908   236 KAHGATVN 243
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
4338-4813 1.12e-49

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 185.12  E-value: 1.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4338 FEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELP 4417
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4418 EKRRAFMLKDSGADVLLtcaghaipplfegevlllddpllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLEHKtm 4497
Cdd:cd17631    81 PPEVAYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHR-- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4498 tNLLAYEQDHT---QLRFDRVLQFAAMSFDVCYQEMFSA--LSSGGILFIIgneAKRDIRQLNDFVRTHGIQTAFL-PTA 4571
Cdd:cd17631   122 -NLLWNAVNALaalDLGPDDVLLVVAPLFHIGGLGVFTLptLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFLvPTM 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4572 FLKLLASekhyfePFAECVD-----HIIAAGEQLiATRMLRDMLARHqVTLHNHYGPSET-HVVTMYTVDpDTDQELQPI 4645
Cdd:cd17631   198 IQALLQH------PRFATTDlsslrAVIYGGAPM-PERLLRALQARG-VKFVQGYGMTETsPGVTFLSPE-DHRRKLGSA 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4646 GKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpYDSnqrMYKTGDLARYLPEGNIEYAGR 4725
Cdd:cd17631   269 GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF----RDG---WFHTGDLGRLDEDGYLYIVDR 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4726 RDHQVKIRGYRVELGEVEAALLKH--VQE----------------AVVLAKENTdgqsdlyayftaeqSLSISQLKEKLA 4787
Cdd:cd17631   342 KKDMIISGGENVYPAEVEDVLYEHpaVAEvavigvpdekwgeavvAVVVPRPGA--------------ELDEDELIAHCR 407
                         490       500
                  ....*....|....*....|....*.
gi 166797876 4788 GQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:cd17631   408 ERLARYKIPKSVEFVDALPRNATGKI 433
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
4330-4818 2.22e-49

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 186.26  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4330 IPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAF 4409
Cdd:PRK07656    3 EWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4410 LPIDPELPEKRRAFMLKDSGADVLLTC--------AGHAIPPLFEGEVLLLDDP-------------LLYQGRTDNLNLS 4468
Cdd:PRK07656   83 VPLNTRYTADEAAYILARGDAKALFVLglflgvdySATTRLPALEHVVICETEEddphtekmktftdFLAAGDPAERAPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4469 CSENDLMYVIYTSGTTGQPKGVQLEHKtmTNLLAYEQ--DHTQLRF-DRVLQFAAMSFDVCYQE-MFSALSSGGILFIig 4544
Cdd:PRK07656  163 VDPDDVADILFTSGTTGRPKGAMLTHR--QLLSNAADwaEYLGLTEgDRYLAANPFFHVFGYKAgVNAPLMRGATILP-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4545 nEAKRDIRQLNDFVRTHGIqTAF--LPTAFLKLLASEKHYFEPFAE---CVdhiiaAGEQLIATRMLRDMLARHQV-TLH 4618
Cdd:PRK07656  239 -LPVFDPDEVFRLIETERI-TVLpgPPTMYNSLLQHPDRSAEDLSSlrlAV-----TGAASMPVALLERFESELGVdIVL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4619 NHYGPSE-THVVTMytVDPDTDQELQP--IGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFv 4695
Cdd:PRK07656  312 TGYGLSEaSGVTTF--NRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI- 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4696 phpyDSNQRMYkTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLA--KENTdGQSdLYAYF 4771
Cdd:PRK07656  389 ----DADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHpaVAEAAVIGvpDERL-GEV-GKAYV 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 4772 TA-------EQSLsISQLKEKLAgqipGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK07656  462 VLkpgaeltEEEL-IAYCREHLA----KYKVPRSIEFLDELPKNATGKVLKRAL 510
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2829-3250 2.47e-49

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 183.73  E-value: 2.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWNDTPLQIVYKTQTPQIHFA 2908
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2909 DLRDIEEHlREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQEGR 2988
Cdd:cd19539    83 DLSDPDSD-RERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2989 EPE-PLSAVPYSDYIEWLDRQDQG----AAKRYWSGYLEGYkGETTLLHKIAQHEQKEYAYANLICRFDHEQTKQLQQIA 3063
Cdd:cd19539   162 AAPlPELRQQYKEYAAWQREALAApraaELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3064 NQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAeiPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQQNALA 3143
Cdd:cd19539   241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3144 SQSYDTYPLYEIQAQTEQKQNLIDH-----IMIFENYPIGQQAEETGHHGTELNItnfhMQEHSHYDLNVVVIP-GKQLA 3217
Cdd:cd19539   319 AQRHQELPFQQLVAELPVDRDAGRHplvqiVFQVTNAPAGELELAGGLSYTEGSD----IPDGAKFDLNLTVTEeGTGLR 394
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 3218 VHFGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19539   395 GSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1778-2261 4.54e-49

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 185.49  E-value: 4.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:PRK07656    9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDSQAGIVLMQRDVRKQL--AYEGVTVL----------LDDESSYHQDGSDL---------APISDVSHL 1916
Cdd:PRK07656   89 YTADEAAYILARGDAKALFVLGLFLGVDysATTRLPALehvviceteeDDPHTEKMKTFTDFlaagdpaerAPEVDPDDV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1917 AYVIYTSGSTGRPKGVLIEHGGLT-NYIWWAKEV-YVKGEK---ANfPLYSSisFDLTVtSIFTPLVTGNAIIVYDGEDK 1991
Cdd:PRK07656  169 ADILFTSGTTGRPKGAMLTHRQLLsNAADWAEYLgLTEGDRylaAN-PFFHV--FGYKA-GVNAPLMRGATILPLPVFDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1992 TALLEsIVRDPRVDIIKLTPAHLQVL---KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFegRIEICNE-YGPTETV- 2066
Cdd:PRK07656  245 DEVFR-LIETERITVLPGPPTMYNSLlqhPDRSAEDLSSLRLAVTGAASMPVALLERFESEL--GVDIVLTgYGLSEASg 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2067 VGCMIyRYDaakDRRESVP--IGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepga 2144
Cdd:PRK07656  322 VTTFN-RLD---DDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW---- 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2145 kMYkTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTA 2222
Cdd:PRK07656  394 -LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVlkPGAELTE 471
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876 2223 ARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK07656  472 EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
3278-3787 6.55e-49

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 185.01  E-value: 6.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3278 HYPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAG 3357
Cdd:PRK06187    1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3358 GAYLPIDPDSPSERIRYILNDSSISVLLYCG-------KLQDDIGFSGTCIdLMEE----------HFYHEkdsslALSY 3420
Cdd:PRK06187   81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSefvpllaAILPQLPTVRTVI-VEGDgpaaplapevGEYEE-----LLAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3421 QSSQ----------LAYAIYTSGTTGKPKGTLIEHRQ-VIHLIEGLSRQVYSAYDAELNIamlAPYYFDASVQQMYASLL 3489
Cdd:PRK06187  155 ASDTfdfpdidendAAAMLYTSGTTGHPKGVVLSHRNlFLHSLAVCAWLKLSRDDVYLVI---VPMFHVHAWGLPYLALM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3490 SGHTLfIVPKEIvsDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHL---LIGGEALSKTTVNKLKQLFGEh 3566
Cdd:PRK06187  232 AGAKQ-VIPRRF--DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLrlvIYGGAALPPALLREFKEKFGI- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3567 gaapGITNVYGPTETC--VDASLFNIECSSD-AWARSQnyvpiGKPLGRNRMYILDSKKRLQPK--GVQGELYIAGDGVG 3641
Cdd:PRK06187  308 ----DLVQGYGMTETSpvVSVLPPEDQLPGQwTKRRSA-----GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLM 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3642 RGYLNLPELTDEKFVADpfvpedrMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaal 3721
Cdd:PRK06187  379 QGYWNRPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAE------ 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3722 kdaddeyylcgyfAA---------------------DKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQL 3780
Cdd:PRK06187  446 -------------VAvigvpdekwgerpvavvvlkpGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRV 512

                  ....*..
gi 166797876 3781 LPAPVKK 3787
Cdd:PRK06187  513 LREQYAE 519
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1790-2261 7.26e-49

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 182.66  E-value: 7.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1790 QAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDD 1869
Cdd:cd05919     1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1870 SQAGIVlmqrdvrkqlayegvtvllddessyhqdgsdlapISDVSHLAYVIYTSGSTGRPKGVLIEHgglTNYIW----W 1945
Cdd:cd05919    81 CEARLV----------------------------------VTSADDIAYLLYSSGTTGPPKGVMHAH---RDPLLfadaM 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1946 AKEVYvkGEKANFPLYSSISFDLTV---TSIFTPLVTGNAIIVYDG-EDKTALLESIVRDpRVDIIKLTP---AHLQVLK 2018
Cdd:cd05919   124 AREAL--GLTPGDRVFSSAKMFFGYglgNSLWFPLAVGASAVLNPGwPTAERVLATLARF-RPTVLYGVPtfyANLLDSC 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2019 EMNIADQTAVRRMIVGGENLSTRLARSIHEQFEgrIEICNEYGPTETVVGCMIYRYDAAKdrresvpIGTAAANTSIY-- 2096
Cdd:cd05919   201 AGSPDALRSLRLCVSAGEALPRGLGERWMEHFG--GPILDGIGATEVGHIFLSNRPGAWR-------LGSTGRPVPGYei 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2097 -VLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRG 2175
Cdd:cd05919   272 rLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2176 YRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV-----SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPL 2250
Cdd:cd05919   345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlkspaAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPR 424
                         490
                  ....*....|.
gi 166797876 2251 TSNGKINKKGL 2261
Cdd:cd05919   425 TATGKLQRFKL 435
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4925-5333 9.26e-49

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 182.07  E-value: 9.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4925 PVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMERYE 5004
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5005 AT-ADEVEECFRAFVR-----PFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYD----GKELA 5074
Cdd:cd20483    83 LSeAADPEAALDQLVRnlrrqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDalraGRDLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5075 PL---RIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEELPSFE-LPkdFA---RPPVRSFDGKRHNFTLDKTVTQGIKQ 5147
Cdd:cd20483   163 TVpppPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKlLP--FAkaeRPPVKDYERSTVEATLDKELLARMKR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5148 LEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLK 5227
Cdd:cd20483   241 ICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5228 AFEHQEYPFEELVEKLGVKRDLSRNPLFDTMFVLQ-----NTEQTD----IEVDSlavrpyEQTETAAkfDLQLNFLIDQ 5298
Cdd:cd20483   321 AYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvhgkfPEYDTGdfkfTDYDH------YDIPTAC--DIALEAEEDP 392
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 166797876 5299 D-EIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMR 5333
Cdd:cd20483   393 DgGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIR 428
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1788-2261 1.45e-47

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 180.59  E-value: 1.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVI--DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRY 1865
Cdd:cd05926     1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1866 MLDDSQAGIVLMQRDVR--------------KQLAYEGVTVLLDDES---SYHQDGSDLAPISDVSH---LAYVIYTSGS 1925
Cdd:cd05926    81 YLADLGSKLVLTPKGELgpasraasklglaiLELALDVGVLIRAPSAeslSNLLADKKNAKSEGVPLpddLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1926 TGRPKGVLIEHGGLTNYIWWAKEVYVKGEKAN----FPLYSSISFdltVTSIFTPLVTGNAIIVYDGEDKTALLeSIVRD 2001
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRtlvvMPLFHVHGL---VASLLSTLAAGGSVVLPPRFSASTFW-PDVRD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2002 PRVDIIKLTPAHLQVLKEMNIADQTAVR---RMIVGGenlSTRLARSIHEQFEGR-----IEIcneYGPTETVVGCMIYR 2073
Cdd:cd05926   237 YNATWYTAVPTIHQILLNRPEPNPESPPpklRFIRSC---SASLPPAVLEALEATfgapvLEA---YGMTEAAHQMTSNP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2074 YDAAKDRRESVPIGTaaaNTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLA 2153
Cdd:cd05926   311 LPPGPRKPGSVGKPV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2154 KWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV-SGGQT-TAARLRKQLSQ 2231
Cdd:cd05926   382 YLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlREGASvTEEELRAFCRK 461
                         490       500       510
                  ....*....|....*....|....*....|
gi 166797876 2232 TLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05926   462 HLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1320-1742 3.48e-47

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 177.57  E-value: 3.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPLQIIFKTkkiGFQFN 1399
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPP---GPAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1400 DLREMK--ESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQ 1477
Cdd:cd19539    80 EVRDLSdpDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPE-QSSITPYSQYIEWLGRQDAKEAAA----YWDQYLEGYEEqTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKR 1552
Cdd:cd19539   160 GPAAPlPELRQQYKEYAAWQREALAAPRAAelldFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAALRE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1553 TAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERA 1632
Cdd:cd19539   239 LAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1633 VASQKFETHPLYDIQARTTQKQDLITHLMI-----FENYPvDQYMESIGRQNGTSIT-ISNVqmeeqTNYDFNLTVIPGD 1706
Cdd:cd19539   317 VDAQRHQELPFQQLVAELPVDRDAGRHPLVqivfqVTNAP-AGELELAGGLSYTEGSdIPDG-----AKFDLNLTVTEEG 390
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 166797876 1707 E-MNISFEYNANVYERASIERVREHFMQILHQVVTDA 1742
Cdd:cd19539   391 TgLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1797-2262 4.13e-47

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 177.10  E-value: 4.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1797 DRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVl 1876
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 mqrdvrkqlayegvtvllddessyhqdgsdlapisdVSHLAYVIYTSGSTGRPKGVLIEHgglTNYIWWAK---EVYVKG 1953
Cdd:cd05934    80 ------------------------------------VVDPASILYTSGTTGPPKGVVITH---ANLTFAGYysaRRFGLG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1954 EK----ANFPLYSSisfDLTVTSIFTPLVTGNAIIVYDGEDKTALLeSIVRDPRVDIIKLTPAHLQ-VLKEMNIADQTAV 2028
Cdd:cd05934   121 EDdvylTVLPLFHI---NAQAVSVLAALSVGATLVLLPRFSASRFW-SDVRRYGATVTNYLGAMLSyLLAQPPSPDDRAH 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2029 R-RMIVGGENLStrlarSIHEQFEGR--IEICNEYGPTETVVGcmiyrydAAKDRRESVP---IGTAAANTSIYVLDENM 2102
Cdd:cd05934   197 RlRAAYGAPNPP-----ELHEEFEERfgVRLLEGYGMTETIVG-------VIGPRDEPRRpgsIGRPAPGYEVRIVDDDG 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2103 KPAPIGVPGEIYISGA---GVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIE 2179
Cdd:cd05934   265 QELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2180 LGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKIN 2257
Cdd:cd05934   338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlrPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVA 417

                  ....*
gi 166797876 2258 KKGLP 2262
Cdd:cd05934   418 KAQLR 422
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1800-2258 5.35e-47

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 177.19  E-value: 5.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQR 1879
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1880 DVRKQlayegvtvllddesSYHQDGSDlapisdvshLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANF- 1958
Cdd:cd05903    82 RFRQF--------------DPAAMPDA---------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFl 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1959 ---PLYSSISFdltVTSIFTPLVTGNAIIVYDGEDKTALLEsIVRDPRVDIIKLTPAHLQVL---KEMNIADQTAVRRMI 2032
Cdd:cd05903   139 vasPMAHQTGF---VYGFTLPLLLGAPVVLQDIWDPDKALA-LMREHGVTFMMGATPFLTDLlnaVEEAGEPLSRLRTFV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2033 VGGENLSTRLARSIHEQFEGRieICNEYGPTE--TVVGcmiyRYDAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVP 2110
Cdd:cd05903   215 CGGATVPRSLARRAAELLGAK--VCSAYGSTEcpGAVT----SITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVE 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2111 GEIYISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEqVKIR-GYRIELGEIEAALLQ 2189
Cdd:cd05903   289 GELLSRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLG 360
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 2190 EEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLS-QTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:cd05903   361 HPGVIEAAVVALPDERLGERACAVVVtkSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
PRK05691 PRK05691
peptide synthase; Validated
264-1307 7.60e-47

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 188.84  E-value: 7.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  264 TVYQLFEEQAERTPENAAVKFKNDH------LTYRELNEKASRLARTLRNCGVQPDTLVaILADRSLEMIVSIIAVWKAG 337
Cdd:PRK05691   10 TLVQALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  338 GAYVPLDP-----EYPKERLQYLLHDADADVLLVQHHLKNSL-------AFDGP---VIDLNDEASyhADcSLLSPVAGH 402
Cdd:PRK05691   89 VIAVPAYPpesarRHHQERLLSIIADAEPRLLLTVADLRDSLlqmeelaAANAPellCVDTLDPAL--AE-AWQEPALQP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  403 SHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQWKKAFFKHSPADRVLVLY-PYVFD-AFILNFFGPLISGATLHLL-PNE 478
Cdd:PRK05691  166 DDIAFLQYTSGSTALPKGVQVSHGNLVaNEQLIRHGFGIDLNPDDVIVSWlPLYHDmGLIGGLLQPIFSGVPCVLMsPAY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  479 ENKETFAIQNAIKQERIThFSTSP----RLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNE-- 550
Cdd:PRK05691  246 FLERPLRWLEAISEYGGT-ISGGPdfayRLCSERVSEsaLERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPDsf 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  551 ---YGPTENSV-VSTFHPVQS-----ADEQ---------------ITIGSPVANHQAYILGAHHQIQ-PIGIPGELYVGG 605
Cdd:PRK05691  325 fasYGLAEATLfVSGGRRGQGipaleLDAEalarnraepgtgsvlMSCGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  606 AGVARGYLNRPELTEEKFVEHlhvPGQKMYKTGDLArWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAmfnLEnvREAA 685
Cdd:PRK05691  405 PSIAHGYWRNPEASAKTFVEH---DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKT---VE--REVE 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  686 VVARedadgaKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLER---------------------IPLTSNGKI 744
Cdd:PRK05691  476 VVRK------GRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRqavaeacqeapsvvlllnpgaLPKTSSGKL 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  745 DLKA---------------LPAADENTRAENEyiAPRNTIEELLASIWQEVLGAERIGILDNFFDFGGDSIKSIQVSSRL 809
Cdd:PRK05691  550 QRSAcrlrladgsldsyalFPALQAVEAAQTA--ASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARL 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  810 YQA-GYKVDMKHLFKHPSiaeLSQFVAPVSRV-ADQGEVNGGTKLTPIQH-----------WFFEQKMPHAHHYNQAVML 876
Cdd:PRK05691  628 RDElGIDLNLRQLFEAPT---LAAFSAAVARQlAGGGAAQAAIARLPRGQalpqslaqnrlWLLWQLDPQSAAYNIPGGL 704
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  877 YSAEGFKEGPLRRTMERIASHHDALRMIFEKTpDGYA-PRITGTDESELFHLEVMNYKGETDPAQAIADKANEIQSSMVL 955
Cdd:PRK05691  705 HLRGELDEAALRASFQRLVERHESLRTRFYER-DGVAlQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDL 783
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  956 DKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQLPQKTDSFPFWADQLSKYAAETDME 1034
Cdd:PRK05691  784 EKGPLLRVTLVRLDDEEHqLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAA 863
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1035 EEIAYW-TELSSIKPQ-PLPKDTISEGSLLRDSEEVTIQWTKEETEQlLKQANRAYNTDINDLLLTSLGLAVHKWTGTED 1112
Cdd:PRK05691  864 RQLAYWkAQLGDEQPVlELATDHPRSARQAHSAARYSLRVDASLSEA-LRGLAQAHQATLFMVLLAAFQALLHRYSGQGD 942
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1113 IVVNLEGHGRepiiPDADISRTIGWFTSQYPVVLRMEAGKNLSQRIKIVKEG-LRRIPDKGMNYSiiKYISGHPEADSLQ 1191
Cdd:PRK05691  943 IRIGVPNANR----PRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQAtLGAQAHQDLPFE--QLVEALPQAREQG 1016
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1192 LKpEISFNYlgqfdQDLKHQALRISPfstGLSMNEN--QERTAVLDLNGMIAE---GTLSLTLSYSSKQYERSTMAQFAR 1266
Cdd:PRK05691 1017 LF-QVMFNH-----QQRDLSALRRLP---GLLAEELpwHSREAKFDLQLHSEEdrnGRLTLSFDYAAELFDAATIERLAE 1087
                        1130      1140      1150      1160
                  ....*....|....*....|....*....|....*....|.
gi 166797876 1267 GLKESLQEVIahcvsrQQTSLTPSDILLKDisIDELEQLLE 1307
Cdd:PRK05691 1088 HFLALLEQVC------EDPQRALGDVQLLD--AAERAQLAQ 1120
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
3284-3783 7.64e-47

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 178.82  E-value: 7.64e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3284 TIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPI 3363
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3364 DPDSPSERIRYILNDSSISVLL--------------YCGKLQDDIGFsGTCIDLMEEHFYHEK---DSSLALSYQ----- 3421
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVtsserldllhpalpGCHDLRTLIIV-GDPAHASEGHPGEEPaswPKLLALGDAdpphp 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3422 --SSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYDAELnIAMLaPYYFDASVQQMYASLLSGHTL----F 3495
Cdd:TIGR03098  160 viDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRL-LAVL-PLSFDYGFNQLTTAFYVGATVvlhdY 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3496 IVPKEIVsdgaalcRYYRQHSIDITDGTP------AHLKLLIAAGDlqgvTLQHLLIGGEALSKTTVNKLKQLFGEHGAA 3569
Cdd:TIGR03098  238 LLPRDVL-------KALEKHGITGLAAVPplwaqlAQLDWPESAAP----SLRYLTNSGGAMPRATLSRLRSFLPNARLF 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3570 PgitnVYGPTE----TCVDASLFNIECSSdawarsqnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYL 3645
Cdd:TIGR03098  307 L----MYGLTEafrsTYLPPEEVDRRPDS-----------IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYW 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3646 NLPELTDEKF------VADPFVPEDRMYrTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAA 3719
Cdd:TIGR03098  372 NDPEKTAERFrplppfPGELHLPELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAF 450
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3720 ALKDADDEYYLC------GYFAADKtiqiSELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPA 3783
Cdd:TIGR03098  451 GVPDPTLGQAIVlvvtppGGEELDR----AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1788-2256 6.69e-46

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 176.02  E-value: 6.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDVRKQLA--------------------YEGVTVLLDDESSYHQDGSDLAPISDVSHlAYVIYTSGSTG 1927
Cdd:cd05959    98 EDSRARVVVVSGELAPVLAaaltksehtlvvlivsggagPEAGALLLAELVAAEAEQLKPAATHADDP-AFWLYSSGSTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1928 RPKGVLIEHGGLTnyiwWAKEVYVK---GEKANFPLYSS----ISFDLTVTSIFtPLVTGNAIIVYDGEDKTALLESIVR 2000
Cdd:cd05959   177 RPKGVVHLHADIY----WTAELYARnvlGIREDDVCFSAaklfFAYGLGNSLTF-PLSVGATTVLMPERPTPAAVFKRIR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2001 DPRVDIIKLTP---AHLQVLKEMNIADQTAVRRMIVGGENLStrlaRSIHEQFEGR--IEICNEYGPTEtvvgcMIYRYd 2075
Cdd:cd05959   252 RYRPTVFFGVPtlyAAMLAAPNLPSRDLSSLRLCVSAGEALP----AEVGERWKARfgLDILDGIGSTE-----MLHIF- 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2076 aAKDRRESVPIGTAAANT---SIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVddpfepgAKMYKTGDL 2152
Cdd:cd05959   322 -LSNRPGRVRYGTTGKPVpgyEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GEWTRTGDK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2153 AKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAA---RLRK 2227
Cdd:cd05959   394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrPGYEDSEAleeELKE 473
                         490       500
                  ....*....|....*....|....*....
gi 166797876 2228 QLSQTLASYMVPAYFIELDEMPLTSNGKI 2256
Cdd:cd05959   474 FVKDRLAPYKYPRWIVFVDELPKTATGKI 502
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1808-2261 2.59e-45

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 173.01  E-value: 2.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1808 RANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGA----YVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRK 1883
Cdd:cd05922     2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1884 QLAYeGVTVLLDDESSYHQDG----SDLAPISDVSH--LAYVIYTSGSTGRPKGVLIEHgglTNYIWWAKEV-----YVK 1952
Cdd:cd05922    82 RLRD-ALPASPDPGTVLDADGiraaRASAPAHEVSHedLALLLYTSGSTGSPKLVRLSH---QNLLANARSIaeylgITA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1953 GEKANFPLysSISFDLTVTSIFTPLVTGNAIIV-YDGEDKTALLESIvRDPRVDIIKLTPAHLQVLKEMNIAD-QTAVRR 2030
Cdd:cd05922   158 DDRALTVL--PLSYDYGLSVLNTHLLRGATLVLtNDGVLDDAFWEDL-REHGATGLAGVPSTYAMLTRLGFDPaKLPSLR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2031 MI--VGGEnLSTRLARSIHEQFEG-RIEICneYGPTETVVGCMIYRYDAAKDRRESvpIGTAAANTSIYVLDENMKPAPI 2107
Cdd:cd05922   235 YLtqAGGR-LPQETIARLRELLPGaQVYVM--YGQTEATRRMTYLPPERILEKPGS--IGLAIPGGEFEILDDDGTPTPP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2108 GVPGEIYISGAGVARGYLNRPEltaekFVDDPFEPGAKMYkTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAAL 2187
Cdd:cd05922   310 GEPGEIVHRGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA 383
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2188 LQEEVIKEAVVTAREDVHGFKqLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05922   384 RSIGLIIEAAAVGLPDPLGEK-LALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
4335-4818 4.33e-45

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 174.91  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4335 HQLFEQQAERNPDHEAVMFGN-----QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAF 4409
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4410 LPIDPELPEKRRAFMLKDSGADVLLTCAG-------HAIPPLFEGEVLLLDDP---LLYQGRTDNLNL-----------S 4468
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITADGglrggkvIDLKEKVDEALEELPSLehvIVVGRTGADVPMegdldwdellaA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4469 CSE---------NDLMYVIYTSGTTGQPKGVQLEH--------KTMTNLLAYEQDhtqlrfDRVLQFAAMSF-----DVC 4526
Cdd:COG0365   172 ASAefepeptdaDDPLFILYTSGTTGKPKGVVHTHggylvhaaTTAKYVLDLKPG------DVFWCTADIGWatghsYIV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4527 YqemfSALSSGGILFII-GNEAKRDIRQLNDFVRTHGIQTAFL-PTAFLKLLASEKHYFEPFA-ECVDHIIAAGEQL-IA 4602
Cdd:COG0365   246 Y----GPLLNGATVVLYeGRPDFPDPGRLWELIEKYGVTVFFTaPTAIRALMKAGDEPLKKYDlSSLRLLGSAGEPLnPE 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4603 TRM-LRDMLarhQVTLHNHYGPSET--HVVTMYTVDPdtdqeLQP--IGKPISNTEIFILNEAGTLQPVGIVGELCISG- 4676
Cdd:COG0365   322 VWEwWYEAV---GVPIVDGWGQTETggIFISNLPGLP-----VKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGp 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4677 -VSLARGYHNRESLTLETFvphpYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEA 4753
Cdd:COG0365   394 wPGMFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHpaVAEA 469
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 4754 VVLAKENTDGQSDLYAY------FTAEQSLsISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:COG0365   470 AVVGVPDEIRGQVVKAFvvlkpgVEPSDEL-AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
PRK12316 PRK12316
peptide synthase; Provisional
4915-5355 1.17e-44

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 181.69  E-value: 1.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4915 IPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGkLPLNRLLTAFQRLMQGHEPLRT--VVEMVREEAVQVI 4992
Cdd:PRK12316 4094 LPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSgfVWQGELGRPLQVV 4172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4993 KSQVEFSM--------ERYEATADEVEECFRAfvRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKL 5064
Cdd:PRK12316 4173 HKQVSLPFaeldwrgrADLQAALDALAAAERE--RGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEV 4250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5065 IQLYDGKELAPLRIQYKDFTEWKhqkeQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDG-KRHNFTLDKTVTQ 5143
Cdd:PRK12316 4251 LERYSGRPPAQPGGRYRDYIAWL----QRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANGyGEHVRELDATATA 4326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5144 GIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPhADL---EPIIGMFVNTLAIRTAPMAEKTFLDYITE 5220
Cdd:PRK12316 4327 RLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRP-AELpgiEGQIGLFINTLPVIATPRAQQSVVEWLQQ 4405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5221 TKETMLKAFEHQEYPFEELVEKLGvkrdLSRNPLFDTMFVLQNT-------EQTDIEVDSLAVRPYEQTEtaAKFDLQLN 5293
Cdd:PRK12316 4406 VQRQNLALREHEHTPLYEIQRWAG----QGGEALFDSLLVFENYpvsealqQGAPGGLRFGEVTNHEQTN--YPLTLAVG 4479
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 5294 FlidQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQLSEKVNKSKHLA 5355
Cdd:PRK12316 4480 L---GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVA 4538
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
289-744 1.26e-44

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 169.97  E-value: 1.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNslafdgpvidlndeasyhadcsllspvaghshLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd05935    82 ELDD--------------------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVIL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VLYPYVFDA-FILNFFGPLISGATLhLLPNEENKETFAiqNAIKQERITHFSTSPRLLKTMIEQMNRE--DFIHVQHVVV 525
Cdd:cd05935   130 ACLPLFHVTgFVGSLNTAVYVGGTY-VLMARWDRETAL--ELIEKYKVTFWTNIPTMLVDLLATPEFKtrDLSSLKVLTG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  526 GGEQLETDTVEKLHSLQPrIRINNEYGPTENSVVSTFHPVQSADEQiTIGSPVANHQAYILGAHHQIQ-PIGIPGELYVG 604
Cdd:cd05935   207 GGAPMPPAVAEKLLKLTG-LRFVEGYGLTETMSQTHTNPPLRPKLQ-CLGIP*FGVDARVIDIETGRElPPNEVGEIVVR 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  605 GAGVARGYLNRPELTEEKFVEhlhVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREA 684
Cdd:cd05935   285 GPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EV 361
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876  685 AVVAREDADGAKQLYAYYVGEPSLTAAQFREEL---SRE-LPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05935   362 CVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIiewAREqMAAYKYPREVEFVDELPRSASGKI 425
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
4923-5335 1.93e-44

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 168.64  E-value: 1.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4923 VYPVSSVQKMvYLTTQIIGGELPYNMTgILETEGKLPLNRLLTAFQRLMQGHEPLRTV--VEMVREEAVQVIKSQVEFSM 5000
Cdd:cd19542     1 IYPCTPMQEG-MLLSQLRSPGLYFNHF-VFDLDSSVDVERLRNAWRQLVQRHDILRTVfvESSAEGTFLQVVLKSLDPPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5001 ERYEATADEVEECFRAFV-RPFDLSQaPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGKELAPlRIQ 5079
Cdd:cd19542    79 EEVETDEDSLDALTRDLLdDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5080 YKDFTEWKHQKEQRERIksqeEYWLGVFHEELPSFElpkdfarPPVrsfdgkRHNFTLDKTVTQGIKQLEELT------G 5153
Cdd:cd19542   157 FSDYISYLQSQSQEESL----QYWRKYLQGASPCAF-------PSL------SPKRPAERSLSSTRRSLAKLEafcaslG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5154 STAYMILFSAYSILLAKYSGQDDIVVGTPIAGR--PHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEH 5231
Cdd:cd19542   220 VTLASLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPH 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5232 QEYPFEELVEKLGVKRDLsrnPLFDTMFVLQNTEQTDIEVDSLAVRPYEQTETAA-KFDLQLNFLIDQDEIQGSFDYCTK 5310
Cdd:cd19542   300 QHLSLREIQRALGLWPSG---TLFNTLVSYQNFEASPESELSGSSVFELSAAEDPtEYPVAVEVEPSGDSLKVSLAYSTS 376
                         410       420
                  ....*....|....*....|....*
gi 166797876 5311 LFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19542   377 VLSEEQAEELLEQFDDILEALLANP 401
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
286-744 2.05e-44

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 169.39  E-value: 2.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  286 NDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLL 365
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  366 VQhhlknslafdgpvidlndeasyhadcsllspvaghshLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPAD 445
Cdd:cd05934    81 VD-------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  446 RVLVLYPyVF--DAFILNFFGPLISGATLHLLPneenkeTFAIQNAIKQER---ITHFSTSPRLLKTMIEQMNRE-DFIH 519
Cdd:cd05934   124 VYLTVLP-LFhiNAQAVSVLAALSVGATLVLLP------RFSASRFWSDVRrygATVTNYLGAMLSYLLAQPPSPdDRAH 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  520 VQHVVVGGEQLETDtvekLHSLQPR--IRINNEYGPTENSVVSTfHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGI 597
Cdd:cd05934   197 RLRAAYGAPNPPEL----HEEFEERfgVRLLEGYGMTETIVGVI-GPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGE 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  598 PGELYV---GGAGVARGYLNRPELTEEKFvEHLhvpgqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAA 674
Cdd:cd05934   272 PGELVIrglRGWGFFKGYYNMPEATAEAM-RNG------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERA 344
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876  675 MFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPsRFIPL-ERIPLTSNGKI 744
Cdd:cd05934   345 ILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgeTLDPEELFAFCEGQLAYFKVP-RYIRFvDDLPKTPTEKV 416
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
3287-3781 2.07e-44

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 170.44  E-value: 2.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3287 ELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPD 3366
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3367 SPSERIRYILNDSSISVLL----YCGKLQDDIGFSGTCIDlmeehfyHEKDsslalsyqssqLAYAIYTSGTTGKPKGTL 3442
Cdd:cd05936    83 YTPRELEHILNDSGAKALIvavsFTDLLAAGAPLGERVAL-------TPED-----------VAVLQYTSGTTGVPKGAM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3443 IEHRQVIHLIEGLSRQVYSAYDAELNIAMLAPYY--FDASVqQMYASLLSGHTLFIVPKeiVSDGAALcRYYRQHSIDIT 3520
Cdd:cd05936   145 LTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFhvFGLTV-ALLLPLALGATIVLIPR--FRPIGVL-KEIRKHRVTIF 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3521 DGTPAHLKLLIAAGDLQGVTLQHLLI---GGEALSKTTVNKLKQLFGehgaAPgITNVYGPTETC--VDASLFNIEcssd 3595
Cdd:cd05936   221 PGVPTMYIALLNAPEFKKRDFSSLRLcisGGAPLPVEVAERFEELTG----VP-IVEGYGLTETSpvVAVNPLDGP---- 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3596 AWARSqnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpfvpeDRMYRTGDLARL 3675
Cdd:cd05936   292 RKPGS-----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-------DGWLRTGDIGYM 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3676 LPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdaddeyylcgyfAA------------------- 3736
Cdd:cd05936   360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAE-------------------AAvvgvpdpysgeavkafvvl 420
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 3737 --DKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05936   421 keGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
3887-4298 2.35e-44

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 168.25  E-value: 2.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3887 YPVSSAQKrLYILNHLEGGELSYNMLGLMtVEGKLDRDKLQQAFRTLILRHESLRTGF--KMADGEPVQYVLDHAAFEAE 3964
Cdd:cd19542     2 YPCTPMQE-GMLLSQLRSPGLYFNHFVFD-LDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKSLDPPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3965 WYQGEEDDADLYIRQFI-RPFHLDEPPLlRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGETLPPlRIQY 4043
Cdd:cd19542    80 EVETDEDSLDALTRDLLdDPTLFGQPPH-RLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4044 KDYAvwqtgeARLQQIQKQEA--YWLELYSGDVPVLHLPADYIRPSARdfagaTMHFTLDKQKSdgLKQLASQTESTLYM 4121
Cdd:cd19542   158 SDYI------SYLQSQSQEESlqYWRKYLQGASPCAFPSLSPKRPAER-----SLSSTRRSLAK--LEAFCASLGVTLAS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4122 VLLASYTLLLSKYSGQEDIIVGSPIAGR--PHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPF 4199
Cdd:cd19542   225 LFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSL 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4200 EVLIDQLNiarDLSRNPLFDTMFVLQNTEQEQLEinDVTFKPYPNGHTMAK---FDLTLTAVEEGAGIQFTLEYLTALFK 4276
Cdd:cd19542   305 REIQRALG---LWPSGTLFNTLVSYQNFEASPES--ELSGSSVFELSAAEDpteYPVAVEVEPSGDSLKVSLAYSTSVLS 379
                         410       420
                  ....*....|....*....|..
gi 166797876 4277 PETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19542   380 EEQAEELLEQFDDILEALLANP 401
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4359-4818 5.80e-44

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 168.38  E-value: 5.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4359 TYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTcag 4438
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4439 haipplfegevlllDDPllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLEHKTMT-NLLAYEQDHTQLRFDRVLQ 4517
Cdd:cd05971    85 --------------DGS----------------DDPALIIYTSGTTGPPKGALHAHRVLLgHLPGVQFPFNLFPRDGDLY 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4518 FAAMS-------FDVcyqeMFSALSSGgiLFIIGNEAKR-DIRQLNDFVRTHGIQTAFLPTAFLKLLASEKHYFEPFAEC 4589
Cdd:cd05971   135 WTPADwawigglLDV----LLPSLYFG--VPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4590 VDHIIAAGEQLIATRML--RDMLArhqVTLHNHYGPSETHVVT-----MYTVDPDTdqelqpIGKPISNTEIFILNEAGT 4662
Cdd:cd05971   209 LRAIATGGESLGEELLGwaREQFG---VEVNEFYGQTECNLVIgncsaLFPIKPGS------MGKPIPGHRVAIVDDNGT 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4663 LQPVGIVGELCI---SGVSLArGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVEL 4739
Cdd:cd05971   280 PLPPGEVGEIAVelpDPVAFL-GYWNNPSATEKKM-------AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4740 GEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQ-----LKEKLAGQIPGYMIPSYFIQLEKLPLTGNGK 4812
Cdd:cd05971   352 AEIEECLLKHpaVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalareIQELVKTRLAAHEYPREIEFVNELPRTATGK 431

                  ....*.
gi 166797876 4813 VNRRAL 4818
Cdd:cd05971   432 IRRREL 437
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
289-744 8.60e-44

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 167.64  E-value: 8.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVqh 368
Cdd:cd05919    11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 hlknslafdgpvidlndeasyHADcsllspvaghsHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQ-WKKAFFKHSPADRV 447
Cdd:cd05919    89 ---------------------SAD-----------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADaMAREALGLTPGDRV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  448 LVLyPYVFDAFIL--NFFGPLISGATLHLLPNEENKEtfAIQNAIKQERITHFSTSPRLLKTMIEQMN--REDFIHVQHV 523
Cdd:cd05919   137 FSS-AKMFFGYGLgnSLWFPLAVGASAVLNPGWPTAE--RVLATLARFRPTVLYGVPTFYANLLDSCAgsPDALRSLRLC 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  524 VVGGEQLETDTVEKL--HSLQPrirINNEYGPTEnsVVSTFHPVQSADEQI-TIGSPVANHQAYILG-AHHQIQPiGIPG 599
Cdd:cd05919   214 VSAGEALPRGLGERWmeHFGGP---ILDGIGATE--VGHIFLSNRPGAWRLgSTGRPVPGYEIRLVDeEGHTIPP-GEEG 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  600 ELYVGGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLE 679
Cdd:cd05919   288 DLLVRGPSAAVGYWNNPEKSRATFNG-------GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHP 360
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  680 NVREAAVVAREDADGAKQLYAYYVGEPSLT-----AAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05919   361 AVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
3286-3781 8.87e-44

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 171.06  E-value: 8.87e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3286 HELFEEQAHRTPDNTAVVFEG-----KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAY 3360
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3361 LPIDPDSPSERIRYILNDSSISVL------LYCGKLQDD-------------------IGFSGTCIDLMEEHFYHEkdss 3415
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLitadggLRGGKVIDLkekvdealeelpslehvivVGRTGADVPMEGDLDWDE---- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3416 lALSYQSSQLAYA----------IYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYsayD----------AELNIAMLAPY 3475
Cdd:COG0365   168 -LLAAASAEFEPEptdaddplfiLYTSGTTGKPKGVVHTHGGYLVHAATTAKYVL---DlkpgdvfwctADIGWATGHSY 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3476 YFdasvqqmYASLLSGHTLFIVP-KEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQG-----VTLQHLLIGGE 3549
Cdd:COG0365   244 IV-------YGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLkkydlSSLRLLGSAGE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3550 ALSKTTVNKLKQLFGehgaAPgITNVYGPTETCvdASLFNIECSSDAWARSqnyvpIGKPLGRNRMYILDSKKRLQPKGV 3629
Cdd:COG0365   317 PLNPEVWEWWYEAVG----VP-IVDGWGQTETG--GIFISNLPGLPVKPGS-----MGKPVPGYDVAVVDEDGNPVPPGE 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3630 QGELYIAGDGVG--RGYLNLPELTDEKFVADpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVM 3707
Cdd:COG0365   385 EGELVIKGPWPGmfRGYWNDPERYRETYFGR----FPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESAL 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3708 LNVPDIQEaaaaalkdaddeyylC----------------------GYFAADKTIQisELRKRMARHLPGYMIPAHFVQL 3765
Cdd:COG0365   461 VSHPAVAE---------------AavvgvpdeirgqvvkafvvlkpGVEPSDELAK--ELQAHVREELGPYAYPREIEFV 523
                         570
                  ....*....|....*.
gi 166797876 3766 DKMPLTPNGKLNRQLL 3781
Cdd:COG0365   524 DELPKTRSGKIMRRLL 539
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
852-1093 2.50e-43

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 160.20  E-value: 2.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  852 LTPIQHWFFEqKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGTDESELFHLEVMN 931
Cdd:COG4908     1 LSPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDLSA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  932 YKGETDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQL 1010
Cdd:COG4908    80 LPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1011 PQKTDSFPFWADQLSKYAAETDMEEEIAYWTELSS--IKPQPLPKDTISEGSLLRDSEEVTIQWTKEETEQLLKQAnRAY 1088
Cdd:COG4908   160 PELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAgaPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA-KAH 238

                  ....*
gi 166797876 1089 NTDIN 1093
Cdd:COG4908   239 GATVN 243
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
289-749 4.74e-43

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 167.10  E-value: 4.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ- 367
Cdd:cd05926    15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPk 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  368 ----------HHLKNS---LAFDGPVIDLNDEA---SYHADCSLLSPVAGHSH---LAYVIYTSGTTGKPKGVMVEHGGI 428
Cdd:cd05926    95 gelgpasraaSKLGLAileLALDVGVLIRAPSAeslSNLLADKKNAKSEGVPLpddLALILHTSGTTGRPKGVPLTHRNL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  429 VNSLQWKKAFFKHSPADRVLVLYP-YVFDAFILNFFGPLISGATLhLLPNEENKETFaiQNAIKQERITHFSTSPRLLKT 507
Cdd:cd05926   175 AASATNITNTYKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSV-VLPPRFSASTF--WPDVRDYNATWYTAVPTIHQI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  508 MIEQMNRED---FIHVQHVVVGGEQLetdTVEKLHSLQPRIRIN--NEYGPTENSVVSTFHPVQSADEQI-TIGSPVANh 581
Cdd:cd05926   252 LLNRPEPNPespPPKLRFIRSCSASL---PPAVLEALEATFGAPvlEAYGMTEAAHQMTSNPLPPGPRKPgSVGKPVGV- 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  582 QAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFvehLHVPgqkMYKTGDLARWLPDGRIEYLGRIDHQVKI 661
Cdd:cd05926   328 EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA---FKDG---WFRTGDLGYLDADGYLFLTGRIKELINR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV--GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLT 739
Cdd:cd05926   402 GGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlrEGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKT 481
                         490
                  ....*....|
gi 166797876  740 SNGKIDLKAL 749
Cdd:cd05926   482 ATGKIQRRKV 491
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
2827-3144 6.97e-43

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 164.53  E-value: 6.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2827 VYPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYsgWN--DTPLQIVYKtQTP- 2903
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAIL--WEglSEPVQVVWR-QAEl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2904 ---QIHFADLRDIEEHLREDAIAAYQRedkakgFDLARDPLMRIAIfrMEDR---KYHLIWSFHHIVMDGWCLSLITKEV 2977
Cdd:cd19544    78 pveELTLDPGDDALAQLRARFDPRRYR------LDLRQAPLLRAHV--AEDPangRWLLLLLFHHLISDHTSLELLLEEI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2978 fdhySALQEGREPEPLSAVPYSDYIEW-LDRQDQGAAKRYWSGYLEGYKgETTL----------LHKIAQHEQkeyayan 3046
Cdd:cd19544   150 ----QAILAGRAAALPPPVPYRNFVAQaRLGASQAEHEAFFREMLGDVD-EPTApfglldvqgdGSDITEARL------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3047 licRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEIPDVEQMIGLFINTIPVRIRCDE 3126
Cdd:cd19544   218 ---ALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGG 294
                         330
                  ....*....|....*...
gi 166797876 3127 DSTfADTMQMVQQnALAS 3144
Cdd:cd19544   295 RSV-REAVRQTHA-RLAE 310
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
3887-4298 9.09e-43

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 164.46  E-value: 9.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEWY 3966
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3967 Q-GEEDDADLYIRQFIR-----PFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIY----EGETL 4036
Cdd:cd19533    82 DlSGDPDPEGAAQQWMQedlrkPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4037 PP------LRIQYKDYAvWQTGEARlqqiQKQEAYWLELYsGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSdgLKQ 4110
Cdd:cd19533   162 PPapfgsfLDLVEEEQA-YRQSERF----ERDRAFWTEQF-EDLPEPVSLARRAPGRSLAFLRRTAELPPELTRT--LLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4111 LASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALK 4190
Cdd:cd19533   234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRS 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4191 AYEHQDYPFEVLIdqlniaRDL----SRNPLFDTMFVLQnTEQEQLEINDVTFKPYP--NGHTMakfDLTLTAVE--EGA 4262
Cdd:cd19533   314 LLRHQRYRYEDLR------RDLgltgELHPLFGPTVNYM-PFDYGLDFGGVVGLTHNlsSGPTN---DLSIFVYDrdDES 383
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 166797876 4263 GIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19533   384 GLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
289-744 9.31e-43

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 164.06  E-value: 9.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADadvllvqh 368
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 hlknslafdgpvIDLNDEASyhadcsllspvaghshlayVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd05912    74 ------------VKLDDIAT-------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VLYP--YVFDAFILnfFGPLISGATLHLLPN-EENKETFAIQNaikqERITHFSTSPRLLKTMIEQMNREDFIHVQHVVV 525
Cdd:cd05912   123 CALPlfHISGLSIL--MRSVIYGMTVYLVDKfDAEQVLHLINS----GKVTIISVVPTMLQRLLEILGEGYPNNLRCILL 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  526 GGEQLETDTVEKlhSLQPRIRINNEYGPTEN-SVVSTFHPVQSADEQITIGSPVANHQAYIlgaHHQIQPIGIPGELYVG 604
Cdd:cd05912   197 GGGPAPKPLLEQ--CKEKGIPVYQSYGMTETcSQIVTLSPEDALNKIGSAGKPLFPVELKI---EDDGQPPYEVGEILLK 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  605 GAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREA 684
Cdd:cd05912   272 GPNVTKGYLNRPDATEESFEN-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEA 344
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  685 AVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05912   345 GVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKL 404
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
4350-4818 2.22e-42

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 163.79  E-value: 2.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4350 AVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSG 4429
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4430 ADVLLTcaghaipplfegevlllddpllyqgrtdnlnlscSENDLMYVIYTSGTTGQPKGVQLEHK-TMTNLLAYEQDHT 4508
Cdd:cd05919    83 ARLVVT----------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRdPLLFADAMAREAL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4509 QLR-FDRVLqfaamsfdvCYQEMFSALSSGGILF---------IIGNEAKRDIRQLNDFVRtHGIQTAF-LPTAFLKLLA 4577
Cdd:cd05919   129 GLTpGDRVF---------SSAKMFFGYGLGNSLWfplavgasaVLNPGWPTAERVLATLAR-FRPTVLYgVPTFYANLLD 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4578 SEKHYFEPFAEcVDHIIAAGEQLiaTRMLRDMLARH-QVTLHNHYGPSET-HVVTMYTVDpdtDQELQPIGKPISNTEIF 4655
Cdd:cd05919   199 SCAGSPDALRS-LRLCVSAGEAL--PRGLGERWMEHfGGPILDGIGATEVgHIFLSNRPG---AWRLGSTGRPVPGYEIR 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4656 ILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGY 4735
Cdd:cd05919   273 LVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQ 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQ-----LKEKLAGQIPGYMIPSYFIQLEKLPLT 4808
Cdd:cd05919   346 WVSPVEVESLIIQHpaVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAFVDELPRT 425
                         490
                  ....*....|
gi 166797876 4809 GNGKVNRRAL 4818
Cdd:cd05919   426 ATGKLQRFKL 435
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1779-2255 3.42e-42

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 165.44  E-value: 3.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1779 LFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY 1858
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 PQDRIRYMLDDSQAGIVLMQR-------DVRKQLAYEGVTVLLDDESSYHQDGS-----DLAPISDVSHLA--------Y 1918
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYERefaprvaEVLPRLPKLRTLVVVEDGSGNDLLPGavdyeDALAAGSPERDFgerspddlY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKGVLIEHGGltnyIWWA---------------KEVYVKGEKANFPlysSISFDL-------TVTSIFTP 1976
Cdd:PRK07798  168 LLYTGGTTGMPKGVMWRQED----IFRVllggrdfatgepiedEEELAKRAAAGPG---MRRFPApplmhgaGQWAAFAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1977 LVTGNAIIVYDGE--DKTALLESIVRDpRVDIIKLT------PAhLQVLKEMNIADQTAVRRMIVGGENLSTRLARSIHE 2048
Cdd:PRK07798  241 LFSGQTVVLLPDVrfDADEVWRTIERE-KVNVITIVgdamarPL-LDALEARGPYDLSSLFAIASGGALFSPSVKEALLE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2049 QFEGRIeICNEYGPTETvvGCMIYRYDAAKDRRESVPIGTAAANTSiyVLDENMKPAP--IGVPGEIYISGAgVARGYLN 2126
Cdd:PRK07798  319 LLPNVV-LTDSIGSSET--GFGGSGTVAKGAVHTGGPRFTIGPRTV--VLDEDGNPVEpgSGEIGWIARRGH-IPLGYYK 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2127 RPELTAEKF--VDdpfepGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDV 2204
Cdd:PRK07798  393 DPEKTAETFptID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDE 467
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2205 HgFKQLCAYYVS---GGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGK 2255
Cdd:PRK07798  468 R-WGQEVVAVVQlreGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
PRK05691 PRK05691
peptide synthase; Validated
1772-2662 4.27e-42

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 173.05  E-value: 4.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1772 PQTPVHQLfEEQSQRTPDQAAVI------DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVaIITRNSIESVVGILAVL 1845
Cdd:PRK05691    8 PLTLVQAL-QRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1846 KSGGAYVPIDP-----EYPQDRIRYMLDDSQAGIVLMQRDVRKQL----------AYEGVTV-LLDDESSYHQDGSDLAP 1909
Cdd:PRK05691   86 YAGVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTVADLRDSLlqmeelaaanAPELLCVdTLDPALAEAWQEPALQP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1910 isdvSHLAYVIYTSGSTGRPKGVLIEHGGLTnyiwwAKEVYVK---GEKAN--------FPLYSSISFdltVTSIFTPLV 1978
Cdd:PRK05691  166 ----DDIAFLQYTSGSTALPKGVQVSHGNLV-----ANEQLIRhgfGIDLNpddvivswLPLYHDMGL---IGGLLQPIF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 TGNAIIV----YDGEDKTALLESIVR-------DP----RVDIIKLTPAHLQVLkemniaDQTAVRRMIVGGENLSTRLA 2043
Cdd:PRK05691  234 SGVPCVLmspaYFLERPLRWLEAISEyggtisgGPdfayRLCSERVSESALERL------DLSRWRVAYSGSEPIRQDSL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2044 RSIHEQFEGrieiCN--------EYGPTETVV---------GCMIYRYDA---AKDRRES------VPIGTAAANTSIYV 2097
Cdd:PRK05691  308 ERFAEKFAA----CGfdpdsffaSYGLAEATLfvsggrrgqGIPALELDAealARNRAEPgtgsvlMSCGRSQPGHAVLI 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2098 LD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDdpfEPGAKMYKTGDLAkWLADGNIEYAGRIDEQVKIRGY 2176
Cdd:PRK05691  384 VDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGH 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2177 RIELGEIEAALLQE-EVIKEAVVTARE-DVHGFKQL-CAYYVSGG---QTTAARLRKQLSQTLAS--YMVPAYFIELD-- 2246
Cdd:PRK05691  460 NLYPQDIEKTVEREvEVVRKGRVAAFAvNHQGEEGIgIAAEISRSvqkILPPQALIKSIRQAVAEacQEAPSVVLLLNpg 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2247 EMPLTSNGKINKKG---------------LPAPDFELQDRAEykAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDS 2311
Cdd:PRK05691  540 ALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTA--ASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNS 617
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2312 IKSIQVSSRLNQQ-GYKMEIKDLFQYATIAELSPHIKQNLriADQGEVKGKVSLTPIQH-----------WFFEQTTTDQ 2379
Cdd:PRK05691  618 IAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVARQL--AGGGAAQAAIARLPRGQalpqslaqnrlWLLWQLDPQS 695
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2380 HYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFrTTENGCEAQNEEIAQS-GLYRLEVMNLKEDPDPGRTIEAKA 2458
Cdd:PRK05691  696 AAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRF-YERDGVALQRIDAQGEfALQRIDLSDLPEAEREARAAQIRE 774
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2459 DEIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLPQKTDSFQLWAKRLS 2537
Cdd:PRK05691  775 EEARQPFDLEKGPLLRVTLVRLDDEEHqLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQR 854
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2538 EYAQSETIKQEQEYWTKIEQTEVKPL------PKDFHETHTTAKDSETAAVEWTKEetellLKQANRAYHTEINDLLLTS 2611
Cdd:PRK05691  855 QWLAQGEAARQLAYWKAQLGDEQPVLelatdhPRSARQAHSAARYSLRVDASLSEA-----LRGLAQAHQATLFMVLLAA 929
                         970       980       990      1000      1010
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876 2612 LGLSISHWSGLEQIPIHLEGHGREQiiqdIDISRTVGWFTSlyPVVLHAQP 2662
Cdd:PRK05691  930 FQALLHRYSGQGDIRIGVPNANRPR----LETQGLVGFFIN--TQVLRAQL 974
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1799-2261 7.63e-42

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 161.88  E-value: 7.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1799 QLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLmq 1878
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1879 rdvrkqlayegVTVLLDDessyhqdgsdlapisdvshLAYVIYTSGSTGRPKGVLIEHGGL-TNYIWWAKEVYVKGEK-- 1955
Cdd:cd05935    79 -----------VGSELDD-------------------LALIPYTSGTTGLPKGCMHTHFSAaANALQSAVWTGLTPSDvi 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1956 -ANFPLYSSISFdltVTSIFTPLVTGNAIIVYDGEDKTALLESIvRDPRVDI-IKLTPAHLQVLKEMNIA--DQTAVRRM 2031
Cdd:cd05935   129 lACLPLFHVTGF---VGSLNTAVYVGGTYVLMARWDRETALELI-EKYKVTFwTNIPTMLVDLLATPEFKtrDLSSLKVL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2032 IVGGENLSTRLARSIHEQFEGR-IEIcneYGPTETvvgcMIYRYDAAKDRRESVPIGTAAANTSIYVLD-ENMKPAPIGV 2109
Cdd:cd05935   205 TGGGAPMPPAVAEKLLKLTGLRfVEG---YGLTET----MSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNE 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2110 PGEIYISGAGVARGYLNRPELTAEKFVDDpfePGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQ 2189
Cdd:cd05935   278 VGEIVVRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 2190 EEVIKEAVVTAREDVHGFKQLCAYYV----SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05935   355 HPAI*EVCVISVPDERVGEEVKAFIVlrpeYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
3919-4283 8.85e-42

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 160.81  E-value: 8.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3919 GKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHA--AFEAEwyqgeeddaDLYIRQFI-RPFHLDEPPLLRVg 3995
Cdd:cd19537    34 GDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPprVQRVD---------TLDVWKEInRPFDLEREDPIRV- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3996 liELQPDrgILMFDMHHIISDGTSMSVLIKEFIRIYEGETLPPLRIQYKDYAVWQtgearlQQI-QKQEAYWLElYSGDV 4074
Cdd:cd19537   104 --FISPD--TLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWS------RPAsPEDLDFWSE-YLSGL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4075 PVLHLPAdyiRPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPHADL 4154
Cdd:cd19537   173 PLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEED 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4155 EPIIGMFVNTLAMR-NYP-EKGKTFSQYLSEVKENALKAYEHQdYPFEVLIDQLNIARDLSRNPLFDTM--FVLQNTEQE 4230
Cdd:cd19537   250 METVGLFLEPLPIRiRFPsSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVSL 328
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 4231 QLEINDVTFKP-YPNGhtmAKFDLTL--TAVEEGaGIQFTLEYLTALFKPETIERM 4283
Cdd:cd19537   329 ALPIPGVEPLYtWAEG---AKFPLMFefTALSDD-SLLLRLEYDTDCFSEEEIDRI 380
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1775-2261 1.21e-41

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 163.78  E-value: 1.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1775 PVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGayVPI 1854
Cdd:COG1021    26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPeYPQDR---IRYMLDDSQA-GIVL-----------MQRDVRKQLAYEGVTVLLDD-------ESSYHQDGSDLAPISD 1912
Cdd:COG1021   104 FA-LPAHRraeISHFAEQSEAvAYIIpdrhrgfdyraLARELQAEVPSLRHVLVVGDageftslDALLAAPADLSEPRPD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1913 VSHLAYVIYTSGSTGRPKgvLIEHgglTN--YIWWAKE-----------VYVKGEKA--NFPLySSisfdltvTSIFTPL 1977
Cdd:COG1021   183 PDDVAFFQLSGGTTGLPK--LIPR---THddYLYSVRAsaeicgldadtVYLAALPAahNFPL-SS-------PGVLGVL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1978 VTGNAIIVYDGEDKTALLESIVRDpRVDIIKLTPAHLQVL---KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRI 2054
Cdd:COG1021   250 YAGGTVVLAPDPSPDTAFPLIERE-RVTVTALVPPLALLWldaAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2055 eiCNEYG-------------PTETVV---GCMIYRYDaakdrrEsvpigtaaantsIYVLDENMKPAPIGVPGEIYISGA 2118
Cdd:COG1021   329 --QQVFGmaeglvnytrlddPEEVILttqGRPISPDD------E------------VRIVDEDGNPVPPGEVGELLTRGP 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2119 GVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVkIR-GYRIELGEIEAALLQEEVIKEAV 2197
Cdd:COG1021   389 YTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAA 461
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 2198 VTAREDVH-GFKqLCAYYVSGGQT-TAARLRKQL-SQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:COG1021   462 VVAMPDEYlGER-SCAFVVPRGEPlTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
289-744 1.27e-41

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 161.35  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLlvqh 368
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 hlknslafdgpVIDLNDeasyhadcsllspvaghshLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd05972    77 -----------VTDAED-------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VLYPYVFDAFIL-NFFGPLISGAT--LHLLPNEENKETFAIqnaIKQERITHFSTSPRLLKTMIEQ-MNREDFIHVQHVV 524
Cdd:cd05972   127 NIADPGWAKGAWsSFFGPWLLGATvfVYEGPRFDAERILEL---LERYGVTSFCGPPTAYRMLIKQdLSSYKFSHLRLVV 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  525 VGGEQLETDTVEKLHSlQPRIRINNEYGPTE-NSVVSTFH--PVQSAdeqiTIGSPVANHQAYILGAHHQIQPIGIPGEL 601
Cdd:cd05972   204 SAGEPLNPEVIEWWRA-ATGLPIRDGYGQTEtGLTVGNFPdmPVKPG----SMGRPTPGYDVAIIDDDGRELPPGEEGDI 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  602 YV--GGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLE 679
Cdd:cd05972   279 AIklPPPGLFLGYVGDPEKTEASIRG-------DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHP 351
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876  680 NVREAAVVAREDADGAKQLYAYYVgepsLTA-AQFREELSRELPN--------YMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05972   352 AVAEAAVVGSPDPVRGEVVKAFVV----LTSgYEPSEELAEELQGhvkkvlapYKYPREIEFVEELPKTISGKI 421
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1800-2261 1.36e-41

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 160.59  E-value: 1.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGivlmqr 1879
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1880 dvrkqlayegvtvlLDDessyhqdgsdlapisdvshLAYVIYTSGSTGRPKGVLIEHGGltnyIWWAkevyVKGEKANFP 1959
Cdd:cd05912    76 --------------LDD-------------------IATIMYTSGTTGKPKGVQQTFGN----HWWS----AIGSALNLG 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1960 LYSSISFdLTVTSIF---------TPLVTGNAIIVYDGEDKTALLESIvRDPRVDIIKLTPAHLQ-VLKEMNIADQTAVR 2029
Cdd:cd05912   115 LTEDDNW-LCALPLFhisglsilmRSVIYGMTVYLVDKFDAEQVLHLI-NSGKVTIISVVPTMLQrLLEILGEGYPNNLR 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2030 RMIVGGENLSTRLArsihEQFEGR-IEICNEYGPTETVVGCMIYRYDAAKDRRESVpiGTAAANTSIYVLDENMKPAPig 2108
Cdd:cd05912   193 CILLGGGPAPKPLL----EQCKEKgIPVYQSYGMTETCSQIVTLSPEDALNKIGSA--GKPLFPVELKIEDDGQPPYE-- 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2109 vPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmyKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALL 2188
Cdd:cd05912   265 -VGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 2189 QEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05912   337 SHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
289-744 1.40e-41

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 161.39  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNslafdgpvidlndeasyhadcslLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd05903    82 RFRQ-----------------------FDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VLYPYV-FDAFILNFFGPLISGATLHLLPNEENKETFAIqnaIKQERITHFSTSPRLLKTMIEQMNR--EDFIHVQHVVV 525
Cdd:cd05903   139 VASPMAhQTGFVYGFTLPLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNAVEEagEPLSRLRTFVC 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  526 GGEQLETDTVEKLHSLQPRIrINNEYGPTEN-SVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVG 604
Cdd:cd05903   216 GGATVPRSLARRAAELLGAK-VCSAYGSTECpGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSR 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  605 GAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRiDHQVKIR-GYRIEIGEVEAAMFNLENVRE 683
Cdd:cd05903   295 GPSVFLGYLDRPDLTADAAPE-------GWFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVEDLLLGHPGVIE 366
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876  684 AAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRE-LPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05903   367 AAVVALPDERLGERACAVVVTKSgaLLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
1801-2261 1.73e-41

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 161.08  E-value: 1.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1801 TYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQrd 1880
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1881 vrKQLAYEGVTVLLDDESSYhqdgSDLAPISDVSH-----LAYVIYTSGSTGRPKGVLIEHGgltNYIwwakeVYVKGEK 1955
Cdd:TIGR01923   79 --SLLEEKDFQADSLDRIEA----AGRYETSLSASfnmdqIATLMFTSGTTGKPKAVPHTFR---NHY-----ASAVGSK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  1956 ANFPLYSSISFDLT--------VTSIFTPLVTGNAIIVYDGedKTALLESIVRDPrVDIIKLTPAHLQ-VLKEMNiaDQT 2026
Cdd:TIGR01923  145 ENLGFTEDDNWLLSlplyhisgLSILFRWLIEGATLRIVDK--FNQLLEMIANER-VTHISLVPTQLNrLLDEGG--HNE 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2027 AVRRMIVGGENLSTRLARSIHEQfegRIEICNEYGPTETVVGCMIYRYDAAKDRRESvpiGTAAANTSIYVLDENMKPAp 2106
Cdd:TIGR01923  220 NLRKILLGGSAIPAPLIEEAQQY---GLPIYLSYGMTETCSQVTTATPEMLHARPDV---GRPLAGREIKIKVDNKEGH- 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  2107 igvpGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmyKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAA 2186
Cdd:TIGR01923  293 ----GEIMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETV 361
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  2187 LLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:TIGR01923  362 LYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4365-4818 4.22e-41

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 160.30  E-value: 4.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4365 ERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAA----FLPIDPELPE---------KRRAFMLKDSGAD 4431
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKEsvlrylvadAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4432 VLLTCAGHAIPPlfEGEVLLLDDplLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHktmTNLLAYEQDHTQL- 4510
Cdd:cd05922    81 DRLRDALPASPD--PGTVLDADG--IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSH---QNLLANARSIAEYl 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4511 ---RFDRVlqFAAMSFDVCY--QEMFSALSSGGILFIigNEAKRDIRQLNDFVRTHGIqTAF--LPTAFlKLLASEKHYF 4583
Cdd:cd05922   154 gitADDRA--LTVLPLSYDYglSVLNTHLLRGATLVL--TNDGVLDDAFWEDLREHGA-TGLagVPSTY-AMLTRLGFDP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4584 EPFAEcVDHIIAAGEQLIATRM--LRDMLARHQVtlHNHYGPSEThVVTMYTVDPD-TDQELQPIGKPISNTEIFILNEA 4660
Cdd:cd05922   228 AKLPS-LRYLTQAGGRLPQETIarLRELLPGAQV--YVMYGQTEA-TRRMTYLPPErILEKPGSIGLAIPGGEFEILDDD 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4661 GTLQPVGIVGELCISGVSLARGYHNRESltletFVPHPYDSNQRMYkTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELG 4740
Cdd:cd05922   304 GTPTPPGEPGEIVHRGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPT 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4741 EVEAALL--KHVQEAVVLAKENTDGQsDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05922   378 EIEAAARsiGLIIEAAAVGLPDPLGE-KLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
290-749 7.86e-41

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 159.13  E-value: 7.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  290 TYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLlvqhh 369
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL----- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  370 lknslafdgpVIDLNDEasyhadcsllspvaghshLAYVIYTSGTTGKPKGVMVEH----GGIVNsLQWKKAFFKH---- 441
Cdd:cd05971    83 ----------VTDGSDD------------------PALIIYTSGTTGPPKGALHAHrvllGHLPG-VQFPFNLFPRdgdl 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  442 --SPAD------RVLVLYPYVFdafilnfFG-PLISgatlHLLPNEENKETFAIqnaIKQERITHFSTSPRLLKTMIEQ- 511
Cdd:cd05971   134 ywTPADwawiggLLDVLLPSLY-------FGvPVLA----HRMTKFDPKAALDL---MSRYGVTTAFLPPTALKMMRQQg 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  512 MNREDF-IHVQHVVVGGEQLETDTV----EKLhslqpRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYIL 586
Cdd:cd05971   200 EQLKHAqVKLRAIATGGESLGEELLgwarEQF-----GVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIV 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  587 GAHHQIQPIGIPGELyvggaGVAR-------GYLNRPELTEEKFVEHLHvpgqkmyKTGDLARWLPDGRIEYLGRIDHQV 659
Cdd:cd05971   275 DDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVI 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  660 KIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAqfrEELSRELPNYM--------IPSRFI 731
Cdd:cd05971   343 TSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPS---DALAREIQELVktrlaaheYPREIE 419
                         490
                  ....*....|....*...
gi 166797876  732 PLERIPLTSNGKIDLKAL 749
Cdd:cd05971   420 FVNELPRTATGKIRRREL 437
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
254-655 8.80e-41

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 162.58  E-value: 8.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  254 DTVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDH----LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVS 329
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDGiwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  330 IIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH---------------HLKNSLAFDGPVIDLNDEASYHADcs 394
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqeqldkllevrdelpSLRHIVVLDPRGLRDDPRLLSLDE-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  395 LLSPVAGHSH---------------LAYVIYTSGTTGKPKGVMVEHGGIV-NSLQWkKAFFKHSPADRVLVLYP--YVFd 456
Cdd:COG1022   160 LLALGREVADpaelearraavkpddLATIIYTSGTTGRPKGVMLTHRNLLsNARAL-LERLPLGPGDRTLSFLPlaHVF- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  457 AFILNFFGpLISGATLHLLPNEENketfaIQNAIKQERITHFSTSPRLL----KTMIEQMNREDFI-------------- 518
Cdd:COG1022   238 ERTVSYYA-LAAGATVAFAESPDT-----LAEDLREVKPTFMLAVPRVWekvyAGIQAKAEEAGGLkrklfrwalavgrr 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  519 ------------------------------------HVQHVVVGGEQLETDTVEKLHSLqpRIRINNEYGPTENSVVSTF 562
Cdd:COG1022   312 yararlagkspslllrlkhaladklvfsklrealggRLRFAVSGGAALGPELARFFRAL--GIPVLEGYGLTETSPVITV 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  563 HPvqsaDEQI---TIGSPVANhqayilgahHQIQpIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykT 637
Cdd:COG1022   390 NR----PGDNrigTVGPPLPG---------VEVK-IAEDGEILVRGPNVMKGYYKNPEATAEAFDADgwLH--------T 447
                         490
                  ....*....|....*...
gi 166797876  638 GDLARWLPDGRIEYLGRI 655
Cdd:COG1022   448 GDIGELDEDGFLRITGRK 465
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
3289-3776 1.40e-40

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 158.16  E-value: 1.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3289 FEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSP 3368
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3369 SERIRYILNDSSISVLLycgklqDDigfsgtcidlmeehfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQV 3448
Cdd:cd17631    81 PPEVAYILADSGAKVLF------DD-------------------------------LALLMYTSGTTGRPKGAMLTHRNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3449 I-HLIEGLSRQVYSAYDAELNIAMLapYYFDASVQQMYASLLSGHTLFIVPKeivSDGAALCRYYRQHSIDITDGTPAHL 3527
Cdd:cd17631   124 LwNAVNALAALDLGPDDVLLVVAPL--FHIGGLGVFTLPTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPTMI 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3528 KLLIAAGDLQGV---TLQHLLIGGEALSKttvnKLKQLFGEHGAApgITNVYGPTETCVDASLFNIEcssDAWARsqnYV 3604
Cdd:cd17631   199 QALLQHPRFATTdlsSLRAVIYGGAPMPE----RLLRALQARGVK--FVQGYGMTETSPGVTFLSPE---DHRRK---LG 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 PIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYI 3684
Cdd:cd17631   267 SAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-------RDGWFHTGDLGRLDEDGYLYIV 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3685 GRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdaddeyylCGYF-----------------AADKTIQISELRK 3747
Cdd:cd17631   340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAE---------------VAVIgvpdekwgeavvavvvpRPGAELDEDELIA 404
                         490       500
                  ....*....|....*....|....*....
gi 166797876 3748 RMARHLPGYMIPAHFVQLDKMPLTPNGKL 3776
Cdd:cd17631   405 HCRERLARYKIPKSVEFVDALPRNATGKI 433
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1784-2261 1.49e-40

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 159.67  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1784 SQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRI 1863
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1864 RYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLD-----DESSYHQDGSDLAPISDV--SHLAYVIYTSGSTGRPKGVLIEH 1936
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDaaaqaDSRRLAQGGLEIPPQAAVapTDLVRLMYTSGTTDRPKGVMHSY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1937 GgltNYIW-WAKEVYVKGEKANF------PLYSSISFDLTVTSIftpLVTGNAIIVYDGEDKTALLESIVRDpRVDIIKL 2009
Cdd:PRK06145  172 G---NLHWkSIDHVIALGLTASErllvvgPLYHVGAFDLPGIAV---LWVGGTLRIHREFDPEAVLAAIERH-RLTCAWM 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2010 TPAHLQ---VLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEIcNEYGPTETVVGCMIyrYDAAKDRRESVPI 2086
Cdd:PRK06145  245 APVMLSrvlTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYI-DAYGLTETCSGDTL--MEAGREIEKIGST 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2087 GTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmyKTGDLAKWLADGNIEYAGR 2166
Cdd:PRK06145  322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2167 IDEQVKIRGYRIELGEIEAALLQ-EEVIKEAVVTAREDVHGFKQLCAYYVSGGQT-TAARLRKQLSQTLASYMVPAYFIE 2244
Cdd:PRK06145  395 KKDMIISGGENIASSEVERVIYElPEVAEAAVIGVHDDRWGERITAVVVLNPGATlTLEALDRHCRQRLASFKVPRQLKV 474
                         490
                  ....*....|....*..
gi 166797876 2245 LDEMPLTSNGKINKKGL 2261
Cdd:PRK06145  475 RDELPRNPSGKVLKRVL 491
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1783-2261 3.76e-40

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 158.20  E-value: 3.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1783 QSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDR 1862
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 IRYMLDDSQAGIVLMQrDVRKQLAYEGVTVLLDD-ESSYHQDGSDLAPISDvSHLAYVIYTSGSTGRPKGVLIEHGgltN 1941
Cdd:PRK03640   91 LLWQLDDAEVKCLITD-DDFEAKLIPGISVKFAElMNGPKEEAEIQEEFDL-DEVATIMYTSGTTGKPKGVIQTYG---N 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1942 YIWWAkevyvKGEKANFPLYSSISFdLTVTSIF---------TPLVTGNAIIVYDGEDKTALLESIVRDpRVDIIKLTPA 2012
Cdd:PRK03640  166 HWWSA-----VGSALNLGLTEDDCW-LAAVPIFhisglsilmRSVIYGMRVVLVEKFDAEKINKLLQTG-GVTIISVVST 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2013 HLQ----VLKEMNIADqtAVRRMIVGG--ENLSTrlarsiheqfegrIEICNE--------YGPTET---VVGCmiyryd 2075
Cdd:PRK03640  239 MLQrlleRLGEGTYPS--SFRCMLLGGgpAPKPL-------------LEQCKEkgipvyqsYGMTETasqIVTL------ 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2076 AAKDRRESV-PIGTAAANTSIYVLDeNMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmyKTGDLAK 2154
Cdd:PRK03640  298 SPEDALTKLgSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGY 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2155 WLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLA 2234
Cdd:PRK03640  370 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLA 449
                         490       500
                  ....*....|....*....|....*..
gi 166797876 2235 SYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK03640  450 KYKVPKRFYFVEELPRNASGKLLRHEL 476
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
3298-3781 5.55e-40

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 156.68  E-value: 5.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3298 DNTAVVFEGKQFTYEELNRRANQLARTLQAKG-VQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLycgklqddigfsgtcidlmeehfyhekdsslalsyqssQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLS 3456
Cdd:cd05941    81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RQ-VYSAYDAELNI-----------AMLAPYYFDASV--------QQMYASLLSGH-TLFI-VPKeIVSdgaALCRYYRQ 3514
Cdd:cd05941   123 DAwRWTEDDVLLHVlplhhvhglvnALLCPLFAGASVeflpkfdpKEVAISRLMPSiTVFMgVPT-IYT---RLLQYYEA 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3515 HSIDITD---GTPAHLKLLIAagdlqgvtlqhlliGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETcvdasLFNIE 3591
Cdd:cd05941   199 HFTDPQFaraAAAERLRLMVS--------------GSAALPVPTLEEWEAITGHT-----LLERYGMTEI-----GMALS 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3592 CSSDAwARSQNYVpiGKPLGRNRMYILD-SKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTG 3670
Cdd:cd05941   255 NPLDG-ERRPGTV--GMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTG 325
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3671 DLARLLPDGNIEYIGRI-DHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADK---TIQISELR 3746
Cdd:cd05941   326 DLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAgaaALSLEELK 405
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 166797876 3747 KRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05941   406 EWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
3887-4298 5.99e-40

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 156.07  E-value: 5.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3887 YPVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMAD-GEPVQYVLDHAAFEAEW 3965
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3966 YQ---GEEDDADL--YI-RQFIRPFHLDEPPLLRVGLIeLQPDRG--ILMFDMHHIISDGTSMSVLIKEFIRIYEG---- 4033
Cdd:cd19536    82 LDltpLEEQLDPLraYKeETKIRRFDLGRAPLVRAALV-RKDERErfLLVISDHHSILDGWSLYLLVKEILAVYNQlley 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4034 --ETLPPlRIQYKDYAVWqtgeaRLQQIQKQE--AYWLELYSG-DVPVLHLP-----ADYIRPSArdfagatMHFTLDKQ 4103
Cdd:cd19536   161 kpLSLPP-AQPYRDFVAH-----ERASIQQAAseRYWREYLAGaTLATLPALseavgGGPEQDSE-------LLVSVPLP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4104 KSDGlkQLASQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRPH--ADLEPIIGMFVNTLAMR-NYPEkgKTFSQY 4180
Cdd:cd19536   228 VRSR--SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRvTLSE--ETVEDL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4181 LSEVKENALKAYEHQDYPFEvlidqlNIARDLSRNPLFDTMFVLQNTEQEQ---LEINDVTFKPYPNG-HTMAKFDLTLT 4256
Cdd:cd19536   304 LKRAQEQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHFDLDFglpEWGSDEGMRRGLLFsEFKSNYDVNLS 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 166797876 4257 AVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIKQP 4298
Cdd:cd19536   378 VLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
3305-3715 7.79e-40

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 157.37  E-value: 7.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3305 EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVL 3384
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3385 LYCGKLQDDI------GFSGTCIDLM--EEHFYHEKDSSL------ALSYQ-------SSQLAYAIYTSGTTGKPKGTLI 3443
Cdd:cd05911    87 FTDPDGLEKVkeaakeLGPKDKIIVLddKPDGVLSIEDLLsptlgeEDEDLppplkdgKDDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3444 EHRqviHLIEGLSrQVYSAYDAELN----IAMLAPYYFDASVQQMYASLLSGHTLFIVPKeivSDGAALCRYYRQHSIDI 3519
Cdd:cd05911   167 SHR---NLIANLS-QVQTFLYGNDGsndvILGFLPLYHIYGLFTTLASLLNGATVIIMPK---FDSELFLDLIEKYKITF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3520 TDGTPAHLKLLIA-----AGDLQgvTLQHLLIGGEALSKTTVNKLKQLFGehgaAPGITNVYGPTETCVDASLfNIEcsS 3594
Cdd:cd05911   240 LYLVPPIAAALAKsplldKYDLS--SLRVILSGGAPLSKELQELLAKRFP----NATIKQGYGMTETGGILTV-NPD--G 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3595 DAWARSqnyvpIGKPLGRNRMYILDSK-KRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvPEDRMYRTGDLA 3673
Cdd:cd05911   311 DDKPGS-----VGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF------DEDGWLHTGDIG 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 166797876 3674 RLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05911   380 YFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVAD 421
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
280-749 1.16e-39

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 157.53  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  280 AAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDA 359
Cdd:cd05959    21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  360 DADVLLVQHHL----KNSLAFDGP----VIDLNDEASYHADCSLLSPVAGHSHL-----------AYVIYTSGTTGKPKG 420
Cdd:cd05959   101 RARVVVVSGELapvlAAALTKSEHtlvvLIVSGGAGPEAGALLLAELVAAEAEQlkpaathaddpAFWLYSSGSTGRPKG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  421 VMVEHGGIVNSLQ-WKKAFFKHSPADRVLVLyPYVFDAFILN---FFgPLISGATLHLLPneENKETFAIQNAIKQERIT 496
Cdd:cd05959   181 VVHLHADIYWTAElYARNVLGIREDDVCFSA-AKLFFAYGLGnslTF-PLSVGATTVLMP--ERPTPAAVFKRIRRYRPT 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  497 HFSTSPRLLKTMI--EQMNREDFIHVQHVVVGGEQLETDTVEklhSLQPR--IRINNEYGPTEnsvvsTFHPVQS----A 568
Cdd:cd05959   257 VFFGVPTLYAAMLaaPNLPSRDLSSLRLCVSAGEALPAEVGE---RWKARfgLDILDGIGSTE-----MLHIFLSnrpgR 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  569 DEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVehlhvpGQkMYKTGDLARWLPDGR 648
Cdd:cd05959   329 VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDDGF 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  649 IEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV-----GEPSLTAAQFREELSRELPN 723
Cdd:cd05959   402 YTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALEEELKEFVKDRLAP 481
                         490       500
                  ....*....|....*....|....*.
gi 166797876  724 YMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05959   482 YKYPRWIVFVDELPKTATGKIQRFKL 507
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
4925-5335 1.61e-39

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 155.33  E-value: 1.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4925 PVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVV----EMVREEAVQVIKSQVEfsM 5000
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFpgdgGDVHQRILDADAARPE--L 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5001 ERYEATADEVEECFRAFV-RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGK------EL 5073
Cdd:cd19546    84 PVVPATEEELPALLADRAaHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrapER 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5074 APLRIQYKDFTEWKHQ-----KEQRERIKSQEEYWLGVFHEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQL 5148
Cdd:cd19546   164 APLPLQFADYALWEREllageDDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5149 EELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRP-HADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLK 5227
Cdd:cd19546   244 AESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVRE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5228 AFEHQEYPFEELVEKLGVKRDLSRNPLFDTmfVLQNTEQTDIEVDS-----LAVRPYEQTETAAKFDLQLNFLI------ 5296
Cdd:cd19546   324 ARRHQDVPFERLAELLALPPSADRHPVFQV--ALDVRDDDNDPWDApelpgLRTSPVPLGTEAMELDLSLALTErrnddg 401
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 166797876 5297 DQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19546   402 DPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
3888-4292 1.81e-39

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 155.33  E-value: 1.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3888 PVSSAQKRLYILNHLEGGELSYNMLGLMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAFEAEWY- 3966
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPv 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3967 --QGEEDDADLYIRQFIRPFHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIY----EGETlP--- 4037
Cdd:cd19546    86 vpATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarrEGRA-Pera 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4038 PLRIQYKDYAVWQ----TGE-ARLQQIQKQEAYWLELYSGDVPVLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLA 4112
Cdd:cd19546   165 PLPLQFADYALWErellAGEdDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4113 SQTESTLYMVLLASYTLLLSKYSGQEDIIVGSPIAGRP-HADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKA 4191
Cdd:cd19546   245 ESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4192 YEHQDYPFEVLIDQLNIARDLSRNPLFDTMFVLQ---NTEQEQLEINDVTFKPYPNGHTMAKFDLTLTAVE----EGA-- 4262
Cdd:cd19546   325 RRHQDVPFERLAELLALPPSADRHPVFQVALDVRdddNDPWDAPELPGLRTSPVPLGTEAMELDLSLALTErrndDGDpd 404
                         410       420       430
                  ....*....|....*....|....*....|....
gi 166797876 4263 GIQFTLEYLTALFKPETIE----RMMGHFEQLVD 4292
Cdd:cd19546   405 GLDGSLRYAADLFDRATAAalarRLVRVLEQVAA 438
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
4924-5335 2.55e-39

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 154.06  E-value: 2.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4924 YPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMERY 5003
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5004 EATADEVEECF------RAFVRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLY----DGKEL 5073
Cdd:cd19533    82 DLSGDPDPEGAaqqwmqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5074 AP------LRIQYKDfTEWKhQKEQRERIKSqeeYWLGVFHEELPsfelPKDFA-RPPVRSFDGKRHNFTLDKTVTQGIK 5146
Cdd:cd19533   162 PPapfgsfLDLVEEE-QAYR-QSERFERDRA---FWTEQFEDLPE----PVSLArRAPGRSLAFLRRTAELPPELTRTLL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5147 QLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETML 5226
Cdd:cd19533   233 EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5227 KAFEHQEYPFEELVEKLGVKRDLsrNPLFDTmfvlqnteqtdievdSLAVRPYE--------QTETAAKF-----DLQLN 5293
Cdd:cd19533   313 SLLRHQRYRYEDLRRDLGLTGEL--HPLFGP---------------TVNYMPFDygldfggvVGLTHNLSsgptnDLSIF 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 166797876 5294 FL--IDQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19533   376 VYdrDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1319-1741 3.30e-39

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 154.01  E-value: 3.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1319 YPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKKIGFQF 1398
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEE-DGVPFQKIEPSKPLSFQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1399 NDLREMKESQKEAMIQKYAREDkmrgFDLEKGALMRLFIL-RTDEKTYRFIwSFHHILMDGWCLPLITKEIFENYFALLQ 1477
Cdd:cd20484    81 EDISSLKESEIIAYLREKAKEP----FVLENGPLMRVHLFsRSEQEHFVLI-TIHHIIFDGSSSLTLIHSLLDAYQALLQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPE-QSSITPYSQYIEW----LGRQDAKEAAAYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKR 1552
Cdd:cd20484   156 GKQPTlASSPASYYDFVAWeqdmLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1553 TAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQ--- 1629
Cdd:cd20484   236 FARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPE--ERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQltv 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1630 --------------------ERAVA-SQKFETHPLYDIQARTTQKQDLITHLMifENYPVDqYMESIgRQNGtsitisnv 1688
Cdd:cd20484   314 ldgldhaaypfpamvrdlniPRSQAnSPVFQVAFFYQNFLQSTSLQQFLAEYQ--DVLSIE-FVEGI-HQEG-------- 381
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 1689 qmeeqtNYDFNLTVIPG-DEMNISFEYNANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd20484   382 ------EYELVLEVYEQeDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIAN 429
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1775-2261 5.15e-39

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 154.79  E-value: 5.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1775 PVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI 1854
Cdd:cd05920    16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPEYPQDRIRYMLDDSQAgivlmqrdvrKQLAYEGVTVLLDDESSYHQDGSDLAPIsdvshlAYVIYTSGSTGRPKGVLI 1934
Cdd:cd05920    96 LPSHRRSELSAFCAHAEA----------VAYIVPDRHAGFDHRALARELAESIPEV------ALFLLSGGTTGTPKLIPR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1935 EHGGLTNYIWWAKE--------VYVKGEKA--NFPLYSSISFDltvtsifTPLVTGNAIIVYDGEDKTALleSIVRDPRV 2004
Cdd:cd05920   160 THNDYAYNVRASAEvcgldqdtVYLAVLPAahNFPLACPGVLG-------TLLAGGRVVLAPDPSPDAAF--PLIEREGV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2005 DIIKLTPAHLQVLKEMNI---ADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEICneYGPTEtvvGCMIY-RYDAAKDR 2080
Cdd:cd05920   231 TVTALVPALVSLWLDAAAsrrADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQV--FGMAE---GLLNYtRLDDPDEV 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2081 RESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGN 2160
Cdd:cd05920   306 IIHTQGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGY 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2161 IEYAGRIDEQVKIRGYRIELGEIEAALLQE-EVIKEAVVTAREDVHGfKQLCAYYV-SGGQTTAARLRKQLSQT-LASYM 2237
Cdd:cd05920   380 LVVEGRIKDQINRGGEKIAAEEVENLLLRHpAVHDAAVVAMPDELLG-ERSCAFVVlRDPPPSAAQLRRFLRERgLAAYK 458
                         490       500
                  ....*....|....*....|....
gi 166797876 2238 VPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05920   459 LPDRIEFVDSLPLTAVGKIDKKAL 482
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
263-749 5.19e-39

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 154.97  E-value: 5.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPE-NAAVKFKNDH-LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAY 340
Cdd:cd05923     1 QTVFEMLRRAASRAPDaCAIADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  341 VPLDPEYPKERLQYLLHDADADVLLVQHH---LKNSLAFDGPVIDLNDEASYHADCS----LLSPVAGHSHLAYVIYTSG 413
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVIAVDaqvMDAIFQSGVRVLALSDLVGLGEPESagplIEDPPREPEQPAFVFYTSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  414 TTGKPKGVMVEHGGIVNSLQW--KKAFFKHSPADRVLVLYP-YVFDAFILNFFGPLISGATLHLLpneenkETFAIQNA- 489
Cdd:cd05923   161 TTGLPKGAVIPQRAAESRVLFmsTQAGLRHGRHNVVLGLMPlYHVIGFFAVLVAALALDGTYVVV------EEFDPADAl 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  490 --IKQERITHFSTSPRLLKTMI--EQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPrIRINNEYGPTEnSVVSTFHPv 565
Cdd:cd05923   235 klIEQERVTSLFATPTHLDALAaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP-GEKVNIYGTTE-AMNSLYMR- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  566 qsADEQITIGSPVANHQ---AYILGAHHQIQPIGIPGELYVGGAGVA--RGYLNRPELTEEKFVEhlhvpgqKMYKTGDL 640
Cdd:cd05923   312 --DARTGTEMRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTGDV 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  641 ARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSR- 719
Cdd:cd05923   383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRa 462
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876  720 -ELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05923   463 sELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
4358-4818 1.02e-38

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 152.49  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4358 LTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLtca 4437
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4438 ghaipplfegevlllddpllyqgrtdnlnlsCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLR-FDRVL 4516
Cdd:cd05972    78 -------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRpDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4517 QFAAMSFDVC-YQEMFSALSSGGILFIIgNEAKRDIRQLNDFVRTHGIQTAFL-PTAFLKLLASEKHYFEPfaECVDHII 4594
Cdd:cd05972   127 NIADPGWAKGaWSSFFGPWLLGATVFVY-EGPRFDAERILELLERYGVTSFCGpPTAYRMLIKQDLSSYKF--SHLRLVV 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4595 AAGEQLI--ATRMLRDMLArhqVTLHNHYGPSETHVVTMYTvdpdTDQELQP--IGKPISNTEIFILNEAGTLQPVGIVG 4670
Cdd:cd05972   204 SAGEPLNpeVIEWWRAATG---LPIRDGYGQTETGLTVGNF----PDMPVKPgsMGRPTPGYDVAIIDDDGRELPPGEEG 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4671 ELCI--SGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLK 4748
Cdd:cd05972   277 DIAIklPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLE 349
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4749 H--VQEAVVLAKENTDGQSDLYAY------FTAEQSLsISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05972   350 HpaVAEAAVVGSPDPVRGEVVKAFvvltsgYEPSEEL-AEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
PRK07638 PRK07638
acyl-CoA synthetase; Validated
273-755 1.09e-38

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 154.17  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTlVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:PRK07638   11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVQHHLKNSLA-FDGPVIDL--------NDEASYHADCSLlspvaGHSHLaYVIYTSGTTGKPKGVMV 423
Cdd:PRK07638   90 KERLAISNADMIVTERYKLNDLPdEEGRVIEIdewkrmieKYLPTYAPIENV-----QNAPF-YMGFTSGSTGKPKAFLR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  424 EHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNeenKETFAIQNAIKQERITHFSTSPr 503
Cdd:PRK07638  164 AQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVP- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  504 llkTMIEQMNRED-FI-HVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANH 581
Cdd:PRK07638  240 ---TMLESLYKENrVIeNKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  582 QAYIL-GAHHQIQPiGIPGELYVGGAGVARGYLNRPELTEEkfvehlhvPGQKMYKT-GDLARWLPDGRIEYLGRIDHQV 659
Cdd:PRK07638  317 QVRICnEAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE--------LNADGWMTvRDVGYEDEEGFIYIVGREKNMI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  660 KIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGepSLTAAQFREELSRELPNYMIPSRFIPLERIPLT 739
Cdd:PRK07638  388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKG--SATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYT 465
                         490
                  ....*....|....*.
gi 166797876  740 SNGKIDLKALPAADEN 755
Cdd:PRK07638  466 NSGKIARMEAKSWIEN 481
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1801-2261 1.13e-38

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 152.97  E-value: 1.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1801 TYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAgivlmqrd 1880
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA-------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1881 vrkqlayegvTVLLDDESSyhqdgsdlapisdvsHLAYVIYTSGSTGRPKGVLIEHGGLTNYIwwakeVYVKGEKANFP- 1959
Cdd:cd05971    80 ----------SALVTDGSD---------------DPALIIYTSGTTGPPKGALHAHRVLLGHL-----PGVQFPFNLFPr 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1960 ---LYSSIS--------FDLTVTSIF--TPLVTGNAiivyDGEDKTALLEsIVRDPRVDIIKLTPAHLQVLKEMNIADQT 2026
Cdd:cd05971   130 dgdLYWTPAdwawigglLDVLLPSLYfgVPVLAHRM----TKFDPKAALD-LMSRYGVTTAFLPPTALKMMRQQGEQLKH 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2027 AVRRM---IVGGENLSTRLARSIHEQFegRIEICNEYGPTET--VVG-CMIYrydaAKDRRESvpIGTAAANTSIYVLDE 2100
Cdd:cd05971   205 AQVKLraiATGGESLGEELLGWAREQF--GVEVNEFYGQTECnlVIGnCSAL----FPIKPGS--MGKPIPGHRVAIVDD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2101 NMKPAPIGVPGEIYIS--GAGVARGYLNRPELTAEKFVDDPFepgakmyKTGDLAKWLADGNIEYAGRIDEQVKIRGYRI 2178
Cdd:cd05971   277 NGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2179 ELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV-----SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSN 2253
Cdd:cd05971   350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTAT 429

                  ....*...
gi 166797876 2254 GKINKKGL 2261
Cdd:cd05971   430 GKIRRREL 437
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1318-1740 1.43e-38

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 151.82  E-value: 1.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1318 IYPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYrgWK--DQPLQIIFKTKKIg 1395
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAIL--WEglSEPVQVVWRQAEL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1396 fQFNDLREMKESQKEAMIQKYAREDKMRgFDLEKGALMRLFILRtDEKTYRF--IWSFHHILMDGWCLPLITKEIFenyf 1473
Cdd:cd19544    78 -PVEELTLDPGDDALAQLRARFDPRRYR-LDLRQAPLLRAHVAE-DPANGRWllLLLFHHLISDHTSLELLLEEIQ---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1474 ALLQQKQPEQSSITPYSQYIE--WLGRQDAkEAAAYWDQYLEGYEEQT---GLpkdHHAAEDGRYVPEkVTCDISSDLTS 1548
Cdd:cd19544   151 AILAGRAAALPPPVPYRNFVAqaRLGASQA-EHEAFFREMLGDVDEPTapfGL---LDVQGDGSDITE-ARLALDAELAQ 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1549 KMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAGIPNVETMIGLFINTIPVRFRCeAGTTFAELMKEA 1628
Cdd:cd19544   226 RLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRL-GGRSVREAVRQT 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1629 QERAVASQKFETHPLYDIQ------ARTTqkqdLITHLMifeNY----PVDQYMESIGRQNgtsitISNVQMEEQTNYDF 1698
Cdd:cd19544   305 HARLAELLRHEHASLALAQrcsgvpAPTP----LFSALL---NYrhsaAAAAAAALAAWEG-----IELLGGEERTNYPL 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 166797876 1699 NLTVipgDEMNISFEYNANVYERASIERVREHFMQILHQVVT 1740
Cdd:cd19544   373 TLSV---DDLGDGFSLTAQVVAPIDAERVCAYMETALEQLVD 411
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4359-4819 1.68e-38

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 151.68  E-value: 1.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4359 TYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTcag 4438
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4439 haipplfegevlllddpllyqgrtdnlnlscsenDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLqF 4518
Cdd:cd05934    82 ----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY-L 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4519 AAMSF----DVCYQeMFSALSSGGILFIIGN-EAKRDIRQlndfVRTHGIQTAFLPTAFLKLLASEkhyfEPFAECVDHI 4593
Cdd:cd05934   127 TVLPLfhinAQAVS-VLAALSVGATLVLLPRfSASRFWSD----VRRYGATVTNYLGAMLSYLLAQ----PPSPDDRAHR 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4594 I-AAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTmyTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGEL 4672
Cdd:cd05934   198 LrAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGV--IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGEL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4673 CISGV---SLARGYHNRESLTLETFvPHpydsnqRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH 4749
Cdd:cd05934   276 VIRGLrgwGFFKGYYNMPEATAEAM-RN------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRH 348
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 4750 --VQEAVVLAKENTDGQSDLYAYFTAE--QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALP 4819
Cdd:cd05934   349 paVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
289-744 2.02e-38

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 152.36  E-value: 2.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQh 368
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 hlknslafdgpviDLNDeasyhadcsllspvaghshLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd05907    85 -------------DPDD-------------------LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VLYP--YVFdAFILNFFGPLISGATLHLLPNEEnketfAIQNAIKQERITHFSTSPRLLKTMIEQMNRE----------D 516
Cdd:cd05907   133 SFLPlaHVF-ERRAGLYVPLLAGARIYFASSAE-----TLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKavpglkrklfD 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  517 FIH---VQHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTENSVVSTFHPVQsaDEQI-TIGSPVAnhqayilGAHHQI 592
Cdd:cd05907   207 LAVggrLRFAASGGAPLPAELLHFFRALG--IPVYEGYGLTETSAVVTLNPPG--DNRIgTVGKPLP-------GVEVRI 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  593 QPigiPGELYVGGAGVARGYLNRPELTEEKFVEhlhvPGqkMYKTGDLARWLPDGRIEYLGRI-DHQVKIRGYRIEIGEV 671
Cdd:cd05907   276 AD---DGEILVRGPNVMLGYYKNPEATAEALDA----DG--WLHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPI 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  672 EAAMFNLENVREAAVVA--------------------REDADGAKQLYAYYVGEPSLTAA--QFREELSRELPNYMIPSR 729
Cdd:cd05907   347 ENALKASPLISQAVVIGdgrpflvalivpdpealeawAEEHGIAYTDVAELAANPAVRAEieAAVEAANARLSRYEQIKK 426
                         490       500
                  ....*....|....*....|.
gi 166797876  730 FIPLERIP------LTSNGKI 744
Cdd:cd05907   427 FLLLPEPFtiengeLTPTLKL 447
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2828-3250 2.27e-38

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 151.37  E-value: 2.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2828 YPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVYKTQTPQIHF 2907
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTPVPIRH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2908 ADLRDIEEhlREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQEG 2987
Cdd:cd19533    81 IDLSGDPD--PEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2988 REPEPLSAVPYSDYIEwlDRQDQGAAKR------YWSGYLEGYKGETTLLHKIAQheqkeyAYANLICR---FDHEQTKQ 3058
Cdd:cd19533   159 RPAPPAPFGSFLDLVE--EEQAYRQSERferdraFWTEQFEDLPEPVSLARRAPG------RSLAFLRRtaeLPPELTRT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3059 LQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGR--PAEIpdveQMIGLFINTIPVRIRCDEDSTFADTMQM 3136
Cdd:cd19533   231 LLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAAR----QTPGMVANTLPLRLTVDPQQTFAELVAQ 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3137 V---QQNALASQSYDTYPLYEIQAQTEQKQNLIDHIMIFENYPIGQqaEETGHHGTELNITNFHMQehshyDLNVVV--- 3210
Cdd:cd19533   307 VsreLRSLLRHQRYRYEDLRRDLGLTGELHPLFGPTVNYMPFDYGL--DFGGVVGLTHNLSSGPTN-----DLSIFVydr 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 166797876 3211 IPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19533   380 DDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK06145 PRK06145
acyl-CoA synthetase; Validated
273-744 4.37e-38

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 152.35  E-value: 4.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASY--------HADCSLLSPVAgHSHLAYVIYTSGTTGKPKGVMVE 424
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQAdsrrlaqgGLEIPPQAAVA-PTDLVRLMYTSGTTDRPKGVMHS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  425 HGgivnSLQWKKafFKHSPA------DRVLVLYP-YVFDAFILNFFGPLISGATLHLlpnEENKETFAIQNAIKQERITH 497
Cdd:PRK06145  171 YG----NLHWKS--IDHVIAlgltasERLLVVGPlYHVGAFDLPGIAVLWVGGTLRI---HREFDPEAVLAAIERHRLTC 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  498 FSTSPRLLKTMIE--QMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQI-TI 574
Cdd:PRK06145  242 AWMAPVMLSRVLTvpDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIgST 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  575 GSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGR 654
Cdd:PRK06145  322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG-------DWFRSGDVGYLDEEGFLYLTDR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  655 IDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIP 732
Cdd:PRK06145  395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgaTLTLEALDRHCRQRLASFKVPRQLKV 474
                         490
                  ....*....|..
gi 166797876  733 LERIPLTSNGKI 744
Cdd:PRK06145  475 RDELPRNPSGKV 486
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
4355-4814 4.96e-38

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 151.98  E-value: 4.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4355 NQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLL 4434
Cdd:cd05911     8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4435 tCAGHAIPPL--------FEGEVLLLDDPLLYQGRTDNLNLSCSE--------------NDLMYVIYTSGTTGQPKGVQL 4492
Cdd:cd05911    88 -TDPDGLEKVkeaakelgPKDKIIVLDDKPDGVLSIEDLLSPTLGeededlppplkdgkDDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4493 EHKTMTNLLAYEQDHTQLRF---DRVLQFAamSFDVCYQeMFSALSSG--GILFIIGNeaKRDIRQLNDFVRTHGIQTAF 4567
Cdd:cd05911   167 SHRNLIANLSQVQTFLYGNDgsnDVILGFL--PLYHIYG-LFTTLASLlnGATVIIMP--KFDSELFLDLIEKYKITFLY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4568 L-PTAFLKLLASEKHYFEPFAeCVDHIIAAGEQLiaTRMLRDMLA--RHQVTLHNHYGPSETHVVTMYTvdPDTDQELQP 4644
Cdd:cd05911   242 LvPPIAAALAKSPLLDKYDLS-SLRVILSGGAPL--SKELQELLAkrFPNATIKQGYGMTETGGILTVN--PDGDDKPGS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4645 IGKPISNTEIFILNEAG-TLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPEGNIEYA 4723
Cdd:cd05911   317 VGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIV 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4724 GRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGqSDL-YAYFTAEQSLSIS--QLKEKLAGQIPGYmipsY 4798
Cdd:cd05911   391 DRKKELIKYKGFQVAPAELEAVLLEHpgVADAAVIGIPDEVS-GELpRAYVVRKPGEKLTekEVKDYVAKKVASY----K 465
                         490       500
                  ....*....|....*....|.
gi 166797876 4799 FIQ-----LEKLPLTGNGKVN 4814
Cdd:cd05911   466 QLRggvvfVDEIPKSASGKIL 486
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1776-2261 5.50e-38

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 151.89  E-value: 5.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQ--LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVP 1853
Cdd:cd05923     3 VFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1854 IDPEYPQDRIRYMLD-DSQAGIVL------MQRDVRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGST 1926
Cdd:cd05923    83 INPRLKAAELAELIErGEMTAAVIavdaqvMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1927 GRPKGVLIEHGGLTNYIWWAKEV--YVKGEKAN----FPLYSSISFdltvTSIFTPLVTGNAIIVYDGEDKTALLESIVR 2000
Cdd:cd05923   163 GLPKGAVIPQRAAESRVLFMSTQagLRHGRHNVvlglMPLYHVIGF----FAVLVAALALDGTYVVVEEFDPADALKLIE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2001 DPRVDIIKLTPAHLQVL---KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGriEICNEYGPTETvvgcMIYRYDAA 2077
Cdd:cd05923   239 QERVTSLFATPTHLDALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG--EKVNIYGTTEA----MNSLYMRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2078 KdRRESVpiGTAAANTSIYVLDENMKP---APIGVPGEIYISGAGVA--RGYLNRPELTAEKFVDdpfepgaKMYKTGDL 2152
Cdd:cd05923   313 A-RTGTE--MRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTGDV 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2153 AKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV-SGGQTTAARLRK-QLS 2230
Cdd:cd05923   383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVpREGTLSADELDQfCRA 462
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876 2231 QTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05923   463 SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1783-2261 7.63e-38

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 151.50  E-value: 7.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1783 QSQRTPDQAAVID--KDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQ 1860
Cdd:PRK09088    4 HARLQPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1861 DRIRYMLDDSQAGIVLmqRDVRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLI-EHGGL 1939
Cdd:PRK09088   84 SELDALLQDAEPRLLL--GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLsERNLQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1940 TNYIWWAKEVYVKGEKA---NFPLYSSISFdltVTSIFTPLVTGNAIIVYDGEDKTALLESIVrDPRVDIIKL--TPAHL 2014
Cdd:PRK09088  162 QTAHNFGVLGRVDAHSSflcDAPMFHIIGL---ITSVRPVLAVGGSILVSNGFEPKRTLGRLG-DPALGITHYfcVPQMA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2015 QVLKEMNIADQTAVRRM---IVGGenlSTRLARSIHEQFEGRIEICNEYGPTE--TVVGCMIyryDAAKDRRESVPIGTA 2089
Cdd:PRK09088  238 QAFRAQPGFDAAALRHLtalFTGG---APHAAEDILGWLDDGIPMVDGFGMSEagTVFGMSV---DCDVIRAKAGAAGIP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2090 AANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDE 2169
Cdd:PRK09088  312 TPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGFFWVVDRKKD 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2170 QVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVH-GFKQLCAYYVSGGQTT-AARLRKQLSQTLASYMVPAYFIELDE 2247
Cdd:PRK09088  386 MFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPADGAPLdLERIRSHLSTRLAKYKVPKHLRLVDA 465
                         490
                  ....*....|....
gi 166797876 2248 MPLTSNGKINKKGL 2261
Cdd:PRK09088  466 LPRTASGKLQKARL 479
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1781-2261 1.08e-37

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 151.17  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1781 EEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAK-GVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYP 1859
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1860 QDRIRYMLDDS-----------QAGIVLMQR--DVRKQLAYEGVTVLLDDESSYHQDGSDLAPisdvshlaYVI-YTSGS 1925
Cdd:PRK06839   89 ENELIFQLKDSgttvlfvektfQNMALSMQKvsYVQRVISITSLKEIEDRKIDNFVEKNESAS--------FIIcYTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1926 TGRPKGVLIEHgglTNYIWWAkevyvkgekanfpLYSSISFDLTVTSI-----------------FTPLVTGNAIIVYDG 1988
Cdd:PRK06839  161 TGKPKGAVLTQ---ENMFWNA-------------LNNTFAIDLTMHDRsivllplfhiggiglfaFPTLFAGGVIIVPRK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1989 EDKTALLeSIVRDPRVDIIKLTPAHLQVLKEMNIADQT---AVRRMIVGGENLSTRLARSIHEQfegRIEICNEYGPTET 2065
Cdd:PRK06839  225 FEPTKAL-SMIEKHKVTVVMGVPTIHQALINCSKFETTnlqSVRWFYNGGAPCPEELMREFIDR---GFLFGQGFGMTET 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2066 VVGC-MIYRYDAakdRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEpga 2144
Cdd:PRK06839  301 SPTVfMLSEEDA---RRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC--- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2145 kmykTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTA 2222
Cdd:PRK06839  375 ----TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVkkSSSVLIE 450
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876 2223 ARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK06839  451 KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
405-749 1.31e-37

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 150.94  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  405 LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyVFDAFILN--FFGPLISGATLHLLPNEENKE 482
Cdd:cd05909   149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALP-FFHSFGLTgcLWLPLLSGIKVVFHPNPLDYK 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  483 TfaIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQpRIRINNEYGPTENSVVSTF 562
Cdd:cd05909   228 K--IPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISV 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  563 HPVQSADEQITIGSPVANHQAYILG-AHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVpgqkmykTGDLA 641
Cdd:cd05909   305 NTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYD-------TGDIG 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  642 RWLPDGRIEYLGRIDHQVKIRGYRIEIGEVE-AAMFNLENVREAAVVAREDADGAKQLYAYYVGEpSLTAAQFREELSR- 719
Cdd:cd05909   378 KIDGEGFLTITGRLSRFAKIAGEMVSLEAIEdILSEILPEDNEVAVVSVPDGRKGEKIVLLTTTT-DTDPSSLNDILKNa 456
                         330       340       350
                  ....*....|....*....|....*....|
gi 166797876  720 ELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05909   457 GISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK06188 PRK06188
acyl-CoA synthetase; Validated
274-752 2.32e-37

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 150.91  E-value: 2.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  274 ERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQ 353
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  354 YLLHDADADVLLVQH---------------HLKNSLAFdGPV---IDLNDEASYHADCSLlSPVAGHSHLAYVIYTSGTT 415
Cdd:PRK06188  103 YVLEDAGISTLIVDPapfveralallarvpSLKHVLTL-GPVpdgVDLLAAAAKFGPAPL-VAAALPPDIAGLAYTGGTT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  416 GKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYP--YVFDAFILnffgP-LISGATLHLLPNEENKETFAiqnAIKQ 492
Cdd:PRK06188  181 GKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPlsHAGGAFFL----PtLLRGGTVIVLAKFDPAEVLR---AIEE 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  493 ERIthfsTSPRLLKTMI------EQMNREDFIHVQHVVVGGEQLETDtveklhSLQPRIRI-----NNEYGPTE-NSVVS 560
Cdd:PRK06188  254 QRI----TATFLVPTMIyalldhPDLRTRDLSSLETVYYGASPMSPV------RLAEAIERfgpifAQYYGQTEaPMVIT 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  561 TF----HPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH-LHvpgqkmy 635
Cdd:PRK06188  324 YLrkrdHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGwLH------- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  636 kTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQF 713
Cdd:PRK06188  397 -TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPgaAVDAAEL 475
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876  714 REELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAA 752
Cdd:PRK06188  476 QAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
270-749 2.95e-37

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 150.01  E-value: 2.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  270 EEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYP 348
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  349 KERLQYLLHDADADVLLVQHHLKNSL------AFDGPVIDLNDEASYhADCSLLSPVAGHSHLAYVI-YTSGTTGKPKG- 420
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTFQNMAlsmqkvSYVQRVISITSLKEI-EDRKIDNFVEKNESASFIIcYTSGTTGKPKGa 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  421 VMVEHGGIVNSLQwKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETfAIQnAIKQERITHFST 500
Cdd:PRK06839  168 VLTQENMFWNALN-NTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTK-ALS-MIEKHKVTVVMG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  501 SPRLLKTMIEQMNRE--DFIHVQHVVVGGEQLetdTVEKLHSLQPR-IRINNEYGPTENS-VVSTFHPVQSADEQITIGS 576
Cdd:PRK06839  245 VPTIHQALINCSKFEttNLQSVRWFYNGGAPC---PEELMREFIDRgFLFGQGFGMTETSpTVFMLSEEDARRKVGSIGK 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  577 PVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRID 656
Cdd:PRK06839  322 PVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQD-------GWLCTGDLARVDEDGFVYIVGRKK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  657 HQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPS--LTAAQFREELSRELPNYMIPSRFIPLE 734
Cdd:PRK06839  395 EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHCRLFLAKYKIPKEIVFLK 474
                         490
                  ....*....|....*
gi 166797876  735 RIPLTSNGKIDLKAL 749
Cdd:PRK06839  475 ELPKNATGKIQKAQL 489
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
4340-4818 3.07e-37

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 149.73  E-value: 3.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4340 QQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEK 4419
Cdd:PRK03640   10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4420 RRAFMLKDSGADVLLTcAGHAIPPLFEGEVLLLDDplLYQGRTDNLNL--SCSENDLMYVIYTSGTTGQPKGVQLEHK-- 4495
Cdd:PRK03640   90 ELLWQLDDAEVKCLIT-DDDFEAKLIPGISVKFAE--LMNGPKEEAEIqeEFDLDEVATIMYTSGTTGKPKGVIQTYGnh 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4496 ------TMTNLLAYEQdhtqlrfDRVLqfAAMSfdvcyqeMF--SALSsggILF---IIGN----EAKRDIRQLNDFVRT 4560
Cdd:PRK03640  167 wwsavgSALNLGLTED-------DCWL--AAVP-------IFhiSGLS---ILMrsvIYGMrvvlVEKFDAEKINKLLQT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4561 HGIQTAFLPTAFLK-LLA--SEKHYFEPFaECVdhIIAAGEqliATRMLRDMLARHQVTLHNHYGPSET--HVVTMytvD 4635
Cdd:PRK03640  228 GGVTIISVVSTMLQrLLErlGEGTYPSSF-RCM--LLGGGP---APKPLLEQCKEKGIPVYQSYGMTETasQIVTL---S 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4636 P-DTDQELQPIGKPISNTEIFILNEaGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDLArY 4714
Cdd:PRK03640  299 PeDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-------DGWFKTGDIG-Y 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4715 LPEGNIEYA-GRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLK----EKLA 4787
Cdd:PRK03640  370 LDEEGFLYVlDRRSDLIISGGENIYPAEIEEVLLSHpgVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRhfceEKLA 449
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876 4788 gqipGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK03640  450 ----KYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1786-2261 3.40e-37

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 150.47  E-value: 3.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1786 RTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRY 1865
Cdd:PRK08316   23 RYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1866 MLDDSQAGIVL------------MQRDVRKQLAYEGVTVLLDDESSYH--------QDGSDLAPISDVSHLAYVIYTSGS 1925
Cdd:PRK08316  103 ILDHSGARAFLvdpalaptaeaaLALLPVDTLILSLVLGGREAPGGWLdfadwaeaGSVAEPDVELADDDLAQILYTSGT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1926 TGRPKGVLIEHGGLT-NYI-------WWAKEVYVkgekANFPLYSSISFDLTVTSIFtpLVTGNAIIVyDGEDKTALLES 1997
Cdd:PRK08316  183 ESLPKGAMLTHRALIaEYVscivagdMSADDIPL----HALPLYHCAQLDVFLGPYL--YVGATNVIL-DAPDPELILRT 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1998 IVRDpRVDIIKLTPA-------HlqvlKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGrIEICNEYGPTETVVGCM 2070
Cdd:PRK08316  256 IEAE-RITSFFAPPTvwisllrH----PDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPG-LRFYNCYGQTEIAPLAT 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2071 IYRYDAAKDRRESVpiGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEpgakmykTG 2150
Cdd:PRK08316  330 VLGPEEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFH-------SG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2151 DLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQ 2228
Cdd:PRK08316  401 DLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVpkAGATVTEDELIAH 480
                         490       500       510
                  ....*....|....*....|....*....|...
gi 166797876 2229 LSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK08316  481 CRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1742-2273 4.79e-37

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 150.58  E-value: 4.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1742 ADIRVDQAELLTEGERRTllqtlndTAAPFPQTPVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGV 1821
Cdd:PRK06178    8 AELRALQQAAWPAGIPRE-------PEYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1822 QTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVL-------MQRDVRKQLAYEGVTV-- 1892
Cdd:PRK06178   81 GAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVts 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1893 ---------------LLDDESSYHQDGSDL------------APISDVSHLAYVIYTSGSTGRPKGVLIEHGGL-----T 1940
Cdd:PRK06178  161 ladvlpaeptlplpdSLRAPRLAAAGAIDLlpalractapvpLPPPALDALAALNYTGGTTGMPKGCEHTQRDMvytaaA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1941 NY-----------------IWWakevyVKGEKAN--FPLYSSISFDL--------TVTSIFTPLVTgNAIIVYDGEDKta 1993
Cdd:PRK06178  241 AYavavvggedsvflsflpEFW-----IAGENFGllFPLFSGATLVLlarwdavaFMAAVERYRVT-RTVMLVDNAVE-- 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1994 LLE---------SIVRDPRVD--IIKLTPAHLQVLKEmniadqtavrrmivggenlstrLARSIheQFEGrieicnEYGP 2062
Cdd:PRK06178  313 LMDhprfaeydlSSLRQVRVVsfVKKLNPDYRQRWRA----------------------LTGSV--LAEA------AWGM 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2063 TET------VVGCMIYRYDAakdRRESVPIGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKF 2135
Cdd:PRK06178  363 TEThtcdtfTAGFQDDDFDL---LSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2136 VDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVH------GFKQ 2209
Cdd:PRK06178  440 RDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDkgqvpvAFVQ 512
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2210 LcayyVSGGQTTAARLRKQLSQTLASYMVPAYFIeLDEMPLTSNGKINKKglpapdfELQDRAE 2273
Cdd:PRK06178  513 L----KPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQ-------DLQALAE 564
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1800-2258 6.41e-37

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 147.48  E-value: 6.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVlmqr 1879
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1880 dvrkqlayegvtvllddessyhqdgsdlapISDVSHLAYVIYTSGSTGRPKGVLIEHG-----GLTNYIW---------- 1944
Cdd:cd05972    77 ------------------------------VTDAEDPALIYFTSGTTGLPKGVLHTHSyplghIPTAAYWlglrpddihw 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1945 ------WAKEVYvkgekanfplyssisfdltvTSIFTPLVTGNAIIVYDGEDKTAL--LESIVRDPrVDIIKLTPAHLQV 2016
Cdd:cd05972   127 niadpgWAKGAW--------------------SSFFGPWLLGATVFVYEGPRFDAEriLELLERYG-VTSFCGPPTAYRM 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2017 LKEMNIA--DQTAVRRMIVGGENLSTRLARSIHEQFegRIEICNEYGPTETVVGCMIYRYDAAKdrresvP--IGTAAAN 2092
Cdd:cd05972   186 LIKQDLSsyKFSHLRLVVSAGEPLNPEVIEWWRAAT--GLPIRDGYGQTETGLTVGNFPDMPVK------PgsMGRPTPG 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2093 TSIYVLDENMKPAPIGVPGEIYI--SGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQ 2170
Cdd:cd05972   258 YDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDI 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2171 VKIRGYRIELGEIEAALLQEEVIKEAVVTARED-VHGfkQLCAYYVS------GGQTTAARLRKQLSQTLASYMVPaYFI 2243
Cdd:cd05972   331 IKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDpVRG--EVVKAFVVltsgyePSEELAEELQGHVKKVLAPYKYP-REI 407
                         490
                  ....*....|....*.
gi 166797876 2244 EL-DEMPLTSNGKINK 2258
Cdd:cd05972   408 EFvEELPKTISGKIRR 423
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1784-2203 6.86e-37

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 148.92  E-value: 6.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1784 SQRTPDQAAVIDKD--RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQD 1861
Cdd:cd05904    15 ASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1862 RIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLL----DDESSYHQDGSDLAPISDV-------SHLAYVIYTSGSTGRPK 1930
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVLldsaEFDSLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1931 GVLIEHGGLTNyiwwAKEVYVKGEKANF----------PLYSSISFDLTVTsifTPLVTGNAIIVYDGEDKTALLESIVR 2000
Cdd:cd05904   175 GVMLTHRNLIA----MVAQFVAGEGSNSdsedvflcvlPMFHIYGLSSFAL---GLLRLGATVVVMPRFDLEELLAAIER 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2001 DpRVDIIKLTPAHLQVLKEMNIADQ---TAVRRMIVGGENLSTRLARSIHEQFeGRIEICNEYGPTE-TVVGCMIyrYDA 2076
Cdd:cd05904   248 Y-KVTHLPVVPPIVLALVKSPIVDKydlSSLRQIMSGAAPLGKELIEAFRAKF-PNVDLGQGYGMTEsTGVVAMC--FAP 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2077 AKDRRESVPIGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKW 2155
Cdd:cd05904   324 EKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW------LHTGDLCYI 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 2156 LADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED 2203
Cdd:cd05904   398 DEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPD 445
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3316-3778 7.86e-37

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 147.97  E-value: 7.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3316 RRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA----YLPIDPDSPSERIRYILNDSSISVLLYCGKLQ 3391
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3392 D--DIGFSGTCIDLM---EEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRqvYSAYDAE 3466
Cdd:cd05922    81 DrlRDALPASPDPGTvldADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAE--YLGITAD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3467 LNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVsdGAALCRYYRQHSIDITDGTPAHLKLLIAAG--DLQGVTLQHL 3544
Cdd:cd05922   159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTYAMLTRLGfdPAKLPSLRYL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3545 LIGGEALSKTTVNKLKQLFgehgaaPG--ITNVYGPTEtcvdaslfniecssdAWARSqNYVP----------IGKPLGR 3612
Cdd:cd05922   237 TQAGGRLPQETIARLRELL------PGaqVYVMYGQTE---------------ATRRM-TYLPperilekpgsIGLAIPG 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3613 NRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNlpeltDEKFVADPFVPEDRMYrTGDLARLLPDGNIEYIGRIDHQVK 3692
Cdd:cd05922   295 GEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWN-----DPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIK 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3693 IQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEyYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTP 3772
Cdd:cd05922   369 LFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE-KLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTA 447

                  ....*.
gi 166797876 3773 NGKLNR 3778
Cdd:cd05922   448 SGKVDY 453
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
3280-3780 1.41e-36

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 148.13  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3280 PREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA 3359
Cdd:PRK07656    2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3360 YLPIDPDSPSERIRYILNDSSISVLLYCGKL--------------------QDDIGFSGTCIDLMEEHFYHEKDSSL-AL 3418
Cdd:PRK07656   82 VVPLNTRYTADEAAYILARGDAKALFVLGLFlgvdysattrlpalehvvicETEEDDPHTEKMKTFTDFLAAGDPAErAP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3419 SYQSSQLAYAIYTSGTTGKPKGTLIEHrqvihlieglsRQVYSAYDAELNIA-------MLA--PYY--FDASVqQMYAS 3487
Cdd:PRK07656  162 EVDPDDVADILFTSGTTGRPKGAMLTH-----------RQLLSNAADWAEYLgltegdrYLAanPFFhvFGYKA-GVNAP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3488 LLSGHTLFIVPKEIVSDGAALCryyRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLI---GGEALSKTTVNKLKQLFG 3564
Cdd:PRK07656  230 LMRGATILPLPVFDPDEVFRLI---ETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLavtGAASMPVALLERFESELG 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3565 ehgaAPGITNVYGPTETCVDASLfnieCSSDawaRSQNYVP--IGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGR 3642
Cdd:PRK07656  307 ----VDIVLTGYGLSEASGVTTF----NRLD---DDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMK 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3643 GYLNLPELTDEKFVADPFVpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALK 3722
Cdd:PRK07656  376 GYYDDPEATAAAIDADGWL------HTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVP 449
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 3723 DADDEYYLCGYFAADKTIQISE--LRKRMARHLPGYMIPAHFVQLDKMPLTPNGK-LNRQL 3780
Cdd:PRK07656  450 DERLGEVGKAYVVLKPGAELTEeeLIAYCREHLAKYKVPRSIEFLDELPKNATGKvLKRAL 510
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
4358-4818 1.69e-36

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 146.08  E-value: 1.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4358 LTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCA 4437
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4438 ghaipplfegevlllddpllyqgrtdnlnlscSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQ 4517
Cdd:cd05935    82 --------------------------------ELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVIL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4518 FAAMSFDVC--YQEMFSALSSGGILFIIgneAKRDIRQLNDFVRTHGIQ--TAfLPTAFLKLLASEKHYFEPFAECVdhI 4593
Cdd:cd05935   130 ACLPLFHVTgfVGSLNTAVYVGGTYVLM---ARWDRETALELIEKYKVTfwTN-IPTMLVDLLATPEFKTRDLSSLK--V 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4594 IAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTmyTVDPDTDQELQPIGKPISNTEIFILN-EAGTLQPVGIVGEL 4672
Cdd:cd05935   204 LTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQT--HTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4673 CISGVSLARGYHNRESLTLETFVphpYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--V 4750
Cdd:cd05935   282 VVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHpaI 358
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 4751 QEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKL----AGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05935   359 *EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIiewaREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK07798 PRK07798
acyl-CoA synthetase; Validated
268-745 1.91e-36

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 148.11  E-value: 1.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  268 LFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEY 347
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  348 PKERLQYLLHDADADVLLVQH--------------HLK--------NSLAFDGPVIDLND-EASYHADCSLL--SPVAGh 402
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYERefaprvaevlprlpKLRtlvvvedgSGNDLLPGAVDYEDaLAAGSPERDFGerSPDDL- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  403 shlaYVIYTSGTTGKPKGVMVEH--------GGI-------VNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLI 467
Cdd:PRK07798  167 ----YLLYTGGTTGMPKGVMWRQedifrvllGGRdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWAAFAALF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  468 SGATLHLLPNEEnketF---AIQNAIKQERITH-FSTSPRLLKTMIE---QMNREDFIHVQHVVVGGEQLETDTVEKLHS 540
Cdd:PRK07798  243 SGQTVVLLPDVR----FdadEVWRTIEREKVNViTIVGDAMARPLLDaleARGPYDLSSLFAIASGGALFSPSVKEALLE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  541 LQPRIRINNEYGPTEN----SVVSTFHPVQSADEQITIGSPVAnhqayILGAHHQIQPigiPGElyvGGAG-VAR----- 610
Cdd:PRK07798  319 LLPNVVLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIGPRTV-----VLDEDGNPVE---PGS---GEIGwIARrghip 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  611 -GYLNRPELTEEKFVEhlhVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAR 689
Cdd:PRK07798  388 lGYYKDPEKTAETFPT---IDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGV 464
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876  690 ED-------------ADGAkqlyayyvgepSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:PRK07798  465 PDerwgqevvavvqlREGA-----------RPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
4924-5335 2.08e-36

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 145.67  E-value: 2.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4924 YPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVRE-EAVQVIKSQVEFSMER 5002
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLgQPVQVVHRQAQVPVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5003 YEATADE-----VEECF-RAFVRPFDLSQAPLLRAGLIELEQDLHIFM-FDMHHIITDGASMNIFVEKLIQLY----DGK 5071
Cdd:cd19536    82 LDLTPLEeqldpLRAYKeETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYnqllEYK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5072 ELAPLRIQ-YKDFTEWKHQKEQRErikSQEEYWLgvfhEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQ-GIKQLE 5149
Cdd:cd19536   162 PLSLPPAQpYRDFVAHERASIQQA---ASERYWR----EYLAGATLATLPALSEAVGGGPEQDSELLVSVPLPvRSRSLA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5150 ELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPH--ADLEPIIGMFVNTLAIRTApMAEKTFLDYITETKETMLK 5227
Cdd:cd19536   235 KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVT-LSEETVEDLLKRAQEQELE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5228 AFEHQEYPFEELveklgvKRDLSRNPLFDTMFVLQNTEQTD---IEVDSLAVRPYEQtETAAKFDLQLNFLID--QDEIQ 5302
Cdd:cd19536   314 SLSHEQVPLADI------QRCSEGEPLFDSIVNFRHFDLDFglpEWGSDEGMRRGLL-FSEFKSNYDVNLSVLpkQDRLE 386
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 5303 GSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19536   387 LKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1788-2258 2.35e-36

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 148.36  E-value: 2.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVID-KDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYM 1866
Cdd:PRK06087   37 PDKIAVVDnHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1867 LDDSQAGI------------VLMQRDVRKQLAYEGVTVLLDDES------SYHQDGSDLAPISDV-----SHLAYVIYTS 1923
Cdd:PRK06087  117 LNKCQAKMffaptlfkqtrpVDLILPLQNQLPQLQQIVGVDKLApatsslSLSQIIADYEPLTTAitthgDELAAVLFTS 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1924 GSTGRPKGVLIEHggltNYIWWAKEVYVKGEKANF--------PLYSSISFDLTVTSiftPLVTGNAIIVYDGEDKTALL 1995
Cdd:PRK06087  197 GTEGLPKGVMLTH----NNILASERAYCARLNLTWqdvfmmpaPLGHATGFLHGVTA---PFLIGARSVLLDIFTPDACL 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1996 ESIVRDPRVDIIKLTPAHLQVLK--EMNIADQTAVRRMIVGGENLSTRLARSIHEQfegRIEICNEYGPTETVVGCMIyR 2073
Cdd:PRK06087  270 ALLEQQRCTCMLGATPFIYDLLNllEKQPADLSALRFFLCGGTTIPKKVARECQQR---GIKLLSVYGSTESSPHAVV-N 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2074 YDAAKDRRESVPiGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLA 2153
Cdd:PRK06087  346 LDDPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW------YYSGDLC 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2154 KWLADGNIEYAGRIDEqVKIR-GYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLS-- 2230
Cdd:PRK06087  419 RMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAff 497
                         490       500       510
                  ....*....|....*....|....*....|
gi 166797876 2231 --QTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:PRK06087  498 srKRVAKYKYPEHIVVIDKLPRTASGKIQK 527
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1778-2198 3.55e-36

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 148.71  E-value: 3.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKD----RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVP 1853
Cdd:COG1022    15 DLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1854 IDPEYPQDRIRYMLDDSQAGIVLMQ--------RDVRKQLAYEGVTVLLDDESSYHQD-----------GSDLAPISDV- 1913
Cdd:COG1022    95 IYPTSSAEEVAYILNDSGAKVLFVEdqeqldklLEVRDELPSLRHIVVLDPRGLRDDPrllsldellalGREVADPAELe 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1914 --------SHLAYVIYTSGSTGRPKGVLIEHGgltNYIWWAK---EVYVKGEKANF----PLysSISFDLTVTSIFtpLV 1978
Cdd:COG1022   175 arraavkpDDLATIIYTSGTTGRPKGVMLTHR---NLLSNARallERLPLGPGDRTlsflPL--AHVFERTVSYYA--LA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 TGNAII-----------------------------VYDG-----EDKTALLESIVR---------DPRVDIIKLTPAHLQ 2015
Cdd:COG1022   248 AGATVAfaespdtlaedlrevkptfmlavprvwekVYAGiqakaEEAGGLKRKLFRwalavgrryARARLAGKSPSLLLR 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2016 VLKemNIADQTA-----------VRRMIVGGENLSTRLARSiheqFEG-RIEICNEYGPTETVVGCMIYRYDAAkdRRES 2083
Cdd:COG1022   328 LKH--ALADKLVfsklrealggrLRFAVSGGAALGPELARF----FRAlGIPVLEGYGLTETSPVITVNRPGDN--RIGT 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2084 VpiGTAAANTSIyvldenmKpapIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEY 2163
Cdd:COG1022   400 V--GPPLPGVEV-------K---IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDEDGFLRI 461
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 166797876 2164 AGRIDEQVKIR-GYRIELGEIEAALLQEEVIKEAVV 2198
Cdd:COG1022   462 TGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
4337-4818 3.63e-36

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 146.74  E-value: 3.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4337 LFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPEL 4416
Cdd:cd05959     9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4417 PEKRRAFMLKDSGADVLltCAGHAIPPLFEgEVLLLDDPLLYQ-----------GRTDNLNL-----------SCSENDL 4474
Cdd:cd05959    89 TPDDYAYYLEDSRARVV--VVSGELAPVLA-AALTKSEHTLVVlivsggagpeaGALLLAELvaaeaeqlkpaATHADDP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4475 MYVIYTSGTTGQPKGVQLEHKTMTNLL-AYEQDHTQLRFDRVLQFAAMSFdVCY---QEMFSALSSGGILFIIGNEAKRD 4550
Cdd:cd05959   166 AFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLF-FAYglgNSLTFPLSVGATTVLMPERPTPA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4551 irQLNDFVRTHGiQTAF--LPTAFLKLLASE---KHYFEPFAECVdhiiAAGEQLIATRMLRdMLARHQVTLHNHYGPSE 4625
Cdd:cd05959   245 --AVFKRIRRYR-PTVFfgVPTLYAAMLAAPnlpSRDLSSLRLCV----SAGEALPAEVGER-WKARFGLDILDGIGSTE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4626 thVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHpydsnqrM 4705
Cdd:cd05959   317 --MLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-------W 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4706 YKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYF-----TAEQSLS 4778
Cdd:cd05959   388 TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHpaVLEAAVVGVEDEDGLTKPKAFVvlrpgYEDSEAL 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 166797876 4779 ISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05959   468 EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1786-2272 3.65e-36

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 147.05  E-value: 3.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1786 RTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRY 1865
Cdd:PRK06188   24 RYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1866 MLDDsqAGI-VLMQRDV----RKQLAYEGVT----VLLDDESSYHQDGSDLAPISDVSHL---------AYVIYTSGSTG 1927
Cdd:PRK06188  104 VLED--AGIsTLIVDPApfveRALALLARVPslkhVLTLGPVPDGVDLLAAAAKFGPAPLvaaalppdiAGLAYTGGTTG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1928 RPKGVLIEHGGLTNYIWWAKevyvkgekANFPLYSSISFdLTVTSI-------FTP-LVTGNAIIVYDGEDKTALLESIV 1999
Cdd:PRK06188  182 KPKGVMGTHRSIATMAQIQL--------AEWEWPADPRF-LMCTPLshaggafFLPtLLRGGTVIVLAKFDPAEVLRAIE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2000 RDpRVDIIKLTPAHLQVLKE---MNIADQTAVRRMIVGGENLS-TRLARSIhEQFeGRIeICNEYGPTETVvgcMIYRYD 2075
Cdd:PRK06188  253 EQ-RITATFLVPTMIYALLDhpdLRTRDLSSLETVYYGASPMSpVRLAEAI-ERF-GPI-FAQYYGQTEAP---MVITYL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2076 AAKDRRESVP-----IGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTG 2150
Cdd:PRK06188  326 RKRDHDPDDPkrltsCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WLHTG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2151 DLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQE-EVIKEAVVTARED-----VHGFKQLCayyvSGGQTTAAR 2224
Cdd:PRK06188  399 DVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHpAVAQVAVIGVPDEkwgeaVTAVVVLR----PGAAVDAAE 474
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 2225 LRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFELQDRA 2272
Cdd:PRK06188  475 LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRGRA 522
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
273-749 6.28e-36

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 147.03  E-value: 6.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKER 351
Cdd:PRK08314   20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  352 LQYLLHDADADVL---------------------LVQHHLKNSLAFDGPV-----------IDLNDEASYHA-----DCS 394
Cdd:PRK08314  100 LAHYVTDSGARVAivgselapkvapavgnlrlrhVIVAQYSDYLPAEPEIavpawlraeppLQALAPGGVVAwkealAAG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  395 LLSP--VAGHSHLAYVIYTSGTTGKPKGVMVEHGGI----VNSLQWKKAffkhSPADRVLVLYPYvFD--AFILNFFGPL 466
Cdd:PRK08314  180 LAPPphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmanaVGSVLWSNS----TPESVVLAVLPL-FHvtGMVHSMNAPI 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  467 ISGATLHLLPNEEnKETFAiqNAIKQERITHFSTSPrllkTMI------EQMNREDFIHVQHVVVGGEQLETDTVEKLHS 540
Cdd:PRK08314  255 YAGATVVLMPRWD-REAAA--RLIERYRVTHWTNIP----TMVvdflasPGLAERDLSSLRYIGGGGAAMPEAVAERLKE 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  541 lQPRIRINNEYGPTENSVVSTFHPVQSADEQiTIGSPVANHQAYILG-AHHQIQPIGIPGELYVGGAGVARGYLNRPELT 619
Cdd:PRK08314  328 -LTGLDYVEGYGLTETMAQTHSNPPDRPKLQ-CLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEAT 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  620 EEKFVEhlhVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLY 699
Cdd:PRK08314  406 AEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVK 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876  700 AYYVGEPSLTAAQFREEL---SRE-LPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK08314  483 AVVVLRPEARGKTTEEEIiawAREhMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2828-3250 1.29e-35

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 143.61  E-value: 1.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2828 YPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVYKTQTPQIHF 2907
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEE-DGVPFQKIEPSKPLSFQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2908 ADLrdieEHLREDAIAAYQREDKAKGFDLARDPLMRIAIF-RMEDRKYHLIwSFHHIVMDGWCLSLITKEVFDHYSALQE 2986
Cdd:cd20484    81 EDI----SSLKESEIIAYLREKAKEPFVLENGPLMRVHLFsRSEQEHFVLI-TIHHIIFDGSSSLTLIHSLLDAYQALLQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2987 GREPEPLSAVP-YSDYIEW----LDRQDQGAAKRYW----SGYLEGYKGETTLLHKIAQhEQKEYAYANlicRFDHEQTK 3057
Cdd:cd20484   156 GKQPTLASSPAsYYDFVAWeqdmLAGAEGEEHRAYWkqqlSGTLPILELPADRPRSSAP-SFEGQTYTR---RLPSELSN 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3058 QLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEipDVEQMIGLFINTIPVRIRCDEDSTFADTMQMV 3137
Cdd:cd20484   232 QIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3138 QQNALASQSYDTYPlYEIQAQTEQKQNLIDHIMIFENYPIGQ-----------QAEETGHHGTELnITNFHmQEhSHYDL 3206
Cdd:cd20484   310 QLTVLDGLDHAAYP-FPAMVRDLNIPRSQANSPVFQVAFFYQnflqstslqqfLAEYQDVLSIEF-VEGIH-QE-GEYEL 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 166797876 3207 NVVVIPGK-QLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd20484   386 VLEVYEQEdRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1800-2265 1.49e-35

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 143.80  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAgivlmqr 1879
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEA------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1880 dvrkqlayegvTVLLDDESSYHQdgsdlapiSDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVyvkgekanfp 1959
Cdd:cd05969    74 -----------KVLITTEELYER--------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYV---------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1960 lyssisFDL-----------------TVTSIFTPLVTGNAIIVYDGEDKTALLESIVRDPRVDIIKLTPAHLQVLKEMNI 2022
Cdd:cd05969   125 ------LDLhpddiywctadpgwvtgTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGD 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2023 A-----DQTAVRRMIVGGENLSTRLARSIHEQFEGRIEicNEYGPTETVvGCMIYRYDAAKDRRESV--PI-GTAAAnts 2094
Cdd:cd05969   199 ElarkyDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIH--DTWWQTETG-SIMIANYPCMPIKPGSMgkPLpGVKAA--- 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2095 iyVLDENMKPAPIGVPGEIYISGA--GVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVK 2172
Cdd:cd05969   273 --VVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIK 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2173 IRGYRIELGEIEAALLQEEVIKEAVVTARED-VHGFKQLCAYYVSGGQTTAARLRKQL----SQTLASYMVPAYFIELDE 2247
Cdd:cd05969   344 TSGHRVGPFEVESALMEHPAVAEAGVIGKPDpLRGEIIKAFISLKEGFEPSDELKEEIinfvRQKLGAHVAPREIEFVDN 423
                         490
                  ....*....|....*...
gi 166797876 2248 MPLTSNGKINKKGLPAPD 2265
Cdd:cd05969   424 LPKTRSGKIMRRVLKAKE 441
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
272-744 1.57e-35

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 144.33  E-value: 1.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  272 QAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKER 351
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  352 LQYLLHDADADVLLVQHHLKNSLaFDGPVIDLND-EASYHADCSLLSPvaghSHL---AYVIYTSGTTGKPKGVMVEHGG 427
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKL-IPGISVKFAElMNGPKEEAEIQEE----FDLdevATIMYTSGTTGKPKGVIQTYGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  428 ivnslQWKKAFfkhSPA--------DRVLVLYP--YVFDAFILnfFGPLISGATLHLLPNEENKEtfaIQNAIKQERITH 497
Cdd:PRK03640  166 -----HWWSAV---GSAlnlgltedDCWLAAVPifHISGLSIL--MRSVIYGMRVVLVEKFDAEK---INKLLQTGGVTI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  498 FSTSPRLLKTMIEQMNREDF-IHVQHVVVGGEQLETDTVEKlhSLQPRIRINNEYGPTEN-SVVSTFHPVQSADEQITIG 575
Cdd:PRK03640  233 ISVVSTMLQRLLERLGEGTYpSSFRCMLLGGGPAPKPLLEQ--CKEKGIPVYQSYGMTETaSQIVTLSPEDALTKLGSAG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  576 SPVANHQAYILgAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVehlhvpgQKMYKTGDLARWLPDGRIEYLGRI 655
Cdd:PRK03640  311 KPLFPCELKIE-KDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-------DGWFKTGDIGYLDEEGFLYVLDRR 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  656 DHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYMIPSRFIPLER 735
Cdd:PRK03640  383 SDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEE 462

                  ....*....
gi 166797876  736 IPLTSNGKI 744
Cdd:PRK03640  463 LPRNASGKL 471
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
3310-3781 1.70e-35

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 143.36  E-value: 1.70e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3310 TYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISvLLYCGK 3389
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQ-LLLTDS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3390 LQDDIGFsgTCIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGlSRQVYSAYDAELNI 3469
Cdd:TIGR01923   80 LLEEKDF--QADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVG-SKENLGFTEDDNWL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3470 AMLaPYYFDASVQQMYASLLSGHTLFIVPKEivsdgAALCRYYRQHSIDITDGTPAHLKLLIAAgDLQGVTLQHLLIGGE 3549
Cdd:TIGR01923  157 LSL-PLYHISGLSILFRWLIEGATLRIVDKF-----NQLLEMIANERVTHISLVPTQLNRLLDE-GGHNENLRKILLGGS 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3550 ALSKTTVNKLKQLfgehgaapGIT--NVYGPTETCVDASLFNIECSSDAwarsqnyVPIGKPL-GRnrmyilDSKKRLQP 3626
Cdd:TIGR01923  230 AIPAPLIEEAQQY--------GLPiyLSYGMTETCSQVTTATPEMLHAR-------PDVGRPLaGR------EIKIKVDN 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  3627 KGVQGELYIAGDGVGRGYLNLPELTdekfvadPFVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESV 3706
Cdd:TIGR01923  289 KEGHGEIMVKGANLMKGYLYQGELT-------PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETV 361
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  3707 MLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:TIGR01923  362 LYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
PRK06178 PRK06178
acyl-CoA synthetase; Validated
4342-4818 2.14e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 145.57  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRR 4421
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4422 AFMLKDSGADVLLT-----------CAGHAIPPLFE---GEVL----------LLDDP-LLYQGRTDNLNL--SCSENDL 4474
Cdd:PRK06178  123 SYELNDAGAEVLLAldqlapvveqvRAETSLRHVIVtslADVLpaeptlplpdSLRAPrLAAAGAIDLLPAlrACTAPVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4475 MYVI---------YTSGTTGQPKGVQLEHKTM-----TNL---LAYEQDHTQLRFDRVLQFAAMSFDVCYqemfsALSSG 4537
Cdd:PRK06178  203 LPPPaldalaalnYTGGTTGMPKGCEHTQRDMvytaaAAYavaVVGGEDSVFLSFLPEFWIAGENFGLLF-----PLFSG 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4538 GILFIIgneAKRDIRQLNDFVRTHGIQTAFLPTaflkllasekhyfEPFAECVDHIIAAGEQLiatRMLRDMLA------ 4611
Cdd:PRK06178  278 ATLVLL---ARWDAVAFMAAVERYRVTRTVMLV-------------DNAVELMDHPRFAEYDL---SSLRQVRVvsfvkk 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4612 -----RHQ-------VTLHNHYGPSETHVVTMYTV---DPDTDQELQPI--GKPISNTEIFILN-EAGTLQPVGIVGELC 4673
Cdd:PRK06178  339 lnpdyRQRwraltgsVLAEAAWGMTETHTCDTFTAgfqDDDFDLLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIV 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4674 ISGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQ 4751
Cdd:PRK06178  419 VRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHpaVL 491
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4752 EAVVLAKENTD-GQSDLyAYFT--AEQSLSISQLKEKLAGQIPGYMIPSYFIqLEKLPLTGNGKVNRRAL 4818
Cdd:PRK06178  492 GSAVVGRPDPDkGQVPV-AFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
289-753 2.57e-35

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 143.03  E-value: 2.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNSLAFDGPvidlndeasyhadcsllspvaghshlAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADrvl 448
Cdd:cd05969    81 ELYERTDPEDP--------------------------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD--- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 vLYPYVFD-AFILN----FFGPLISGATLHLLPNEENKETFaiQNAIKQERITHFSTSP----RLLKTMIEQMNREDFIH 519
Cdd:cd05969   132 -IYWCTADpGWVTGtvygIWAPWLNGVTNVVYEGRFDAESW--YGIIERVKVTVWYTAPtairMLMKEGDELARKYDLSS 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  520 VQHVVVGGEQLETDTV----EKLhslqpRIRINNEYGPTEN-SVVSTFHPVQSADEQiTIGSPVANHQAYILGAHHQIQP 594
Cdd:cd05969   209 LRFIHSVGEPLNPEAIrwgmEVF-----GVPIHDTWWQTETgSIMIANYPCMPIKPG-SMGKPLPGVKAAVVDENGNELP 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  595 IGIPGELYV--GGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVE 672
Cdd:cd05969   283 PGTKGILALkpGWPSMFRGIWNDEERYKNSFID-------GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  673 AAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAqfrEELSRELPNY--------MIPSRFIPLERIPLTSNGKI 744
Cdd:cd05969   356 SALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPS---DELKEEIINFvrqklgahVAPREIEFVDNLPKTRSGKI 432

                  ....*....
gi 166797876  745 DLKALPAAD 753
Cdd:cd05969   433 MRRVLKAKE 441
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
4350-4818 2.71e-35

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 142.81  E-value: 2.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4350 AVMFGNQTLTYRQLNERSNQLARVLQDKGA-CTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDS 4428
Cdd:cd05941     4 AIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4429 GADvlltcaghaipplfegevLLLDDPLlyqgrtdnlnlscsendlmyVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHT 4508
Cdd:cd05941    84 EPS------------------LVLDPAL--------------------ILYTSGTTGRPKGVVLTHANLAANVRALVDAW 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4509 QLRFDRVLQFAAMSFDV--CYQEMFSALSSGGILFIIGN-EAKRDIRqlndfVRTHGIQTAFL--PTAFLKLLAS-EKHY 4582
Cdd:cd05941   126 RWTEDDVLLHVLPLHHVhgLVNALLCPLFAGASVEFLPKfDPKEVAI-----SRLMPSITVFMgvPTIYTRLLQYyEAHF 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4583 FEPFAECVDH-----IIAAGEQLIATRMLRDMLARHQVTLHNHYGPSEThvvTMYTVDPdTDQELQP--IGKPISNTEIF 4655
Cdd:cd05941   201 TDPQFARAAAaerlrLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEI---GMALSNP-LDGERRPgtVGMPLPGVQAR 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4656 IL-NEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPEGNIEYAGR-RDHQVKIR 4733
Cdd:cd05941   277 IVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRsSVDIIKSG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4734 GYRVELGEVEAALLKH--VQEAVVLAKENTD-GQSdLYAYFTAE---QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPL 4807
Cdd:cd05941   351 GYKVSALEIERVLLAHpgVSECAVIGVPDPDwGER-VVAVVVLRagaAALSLEELKEWAKQRLAPYKRPRRLILVDELPR 429
                         490
                  ....*....|.
gi 166797876 4808 TGNGKVNRRAL 4818
Cdd:cd05941   430 NAMGKVNKKEL 440
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
263-749 3.08e-35

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 143.62  E-value: 3.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQP-DTLVAILADrSLEMIVSIIAVWKAGGAYV 341
Cdd:cd05920    15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPgDRVVVQLPN-VAEFVVLFFALLRLGAVPV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  342 PLDPEYPKERLQYLLHDADADVLLVqhhlKNSLAFDGPVIDLNDEASYHADcsllspvaghshLAYVIYTSGTTGKPKGV 421
Cdd:cd05920    94 LALPSHRRSELSAFCAHAEAVAYIV----PDRHAGFDHRALARELAESIPE------------VALFLLSGGTTGTPKLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  422 MVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDaFILN---FFGPLISGATLHLLPNEENKETFAIqnaIKQERITHF 498
Cdd:cd05920   158 PRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHN-FPLAcpgVLGTLLAGGRVVLAPDPSPDAAFPL---IEREGVTVT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  499 STSPRLLKTMIEQMNRE--DFIHVQHVVVGGEQLETDTVEKLHS-LQPRIRinNEYGPTENSVvsTFHPVQSADEQI--T 573
Cdd:cd05920   234 ALVPALVSLWLDAAASRraDLSSLRLLQVGGARLSPALARRVPPvLGCTLQ--QVFGMAEGLL--NYTRLDDPDEVIihT 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  574 IGSPVANH-QAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYL 652
Cdd:cd05920   310 QGRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP------DGFYRTGDLVRRTPDGYLVVE 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  653 GRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV-GEPSLTAAQFREEL-SRELPNYMIPSRF 730
Cdd:cd05920   384 GRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVlRDPPPSAAQLRRFLrERGLAAYKLPDRI 463
                         490
                  ....*....|....*....
gi 166797876  731 IPLERIPLTSNGKIDLKAL 749
Cdd:cd05920   464 EFVDSLPLTAVGKIDKKAL 482
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
264-744 4.26e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 144.76  E-value: 4.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  264 TVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPL 343
Cdd:PRK05605   33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  344 DPEYPKERLQYLLHDADADVLLVQ-------HHLKNSLAFDGPV-IDLNDE--------------------ASYHA---- 391
Cdd:PRK05605  113 NPLYTAHELEHPFEDHGARVAIVWdkvaptvERLRRTTPLETIVsVNMIAAmpllqrlalrlpipalrkarAALTGpapg 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  392 --------DCSLLSPVAGHSH-------LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSP--ADRVLVLYPyV 454
Cdd:PRK05605  193 tvpwetlvDAAIGGDGSDVSHprptpddVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGdgPERVLAALP-M 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  455 FDAFILNF---FGPLIsGATLHLLPNEENKEtfaIQNAIKQERITHFSTSPRLLKTMIEQMNRE--DFIHVQHVVVGGEQ 529
Cdd:PRK05605  272 FHAYGLTLcltLAVSI-GGELVLLPAPDIDL---ILDAMKKHPPTWLPGVPPLYEKIAEAAEERgvDLSGVRNAFSGAMA 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  530 LETDTVEKLHSLQPRiRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHH--QIQPIGIPGELYVGGAG 607
Cdd:PRK05605  348 LPVSTVELWEKLTGG-LLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDpdETMPDGEEGELLVRGPQ 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  608 VARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVV 687
Cdd:PRK05605  427 VFKGYWNRPEETAKSFLD-------GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVV 499
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876  688 AREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK05605  500 GLPREDGSEEVVAAVVLEPgaALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
287-712 6.88e-35

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 143.14  E-value: 6.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  287 DHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLV 366
Cdd:cd05904    31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  367 Q-HHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGH----------SHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWK 435
Cdd:cd05904   111 TaELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEaeppvvvikqDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  436 KAFF--KHSPADRVLVLYPYvFDAFILNFF--GPLISGATLHLLPNEENKETFAiqnAIKQERITHFSTSPRLLKTMIEQ 511
Cdd:cd05904   191 VAGEgsNSDSEDVFLCVLPM-FHIYGLSSFalGLLRLGATVVVMPRFDLEELLA---AIERYKVTHLPVVPPIVLALVKS 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  512 --MNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSADEQ--ITIGSPVANHQAYIL- 586
Cdd:cd05904   267 piVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAkyGSVGRLVPNVEAKIVd 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  587 ---GAHhqiQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKI 661
Cdd:cd05904   347 petGES---LPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEgwLH--------TGDLCYIDEDGYLFIVDRLKELIKY 415
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV--GEPSLTAAQ 712
Cdd:cd05904   416 KGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkPGSSLTEDE 468
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1319-1741 7.26e-35

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 140.97  E-value: 7.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1319 YPLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKKIGFQF 1398
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTPVPIRH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1399 NDLREmkESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKtyRFIW--SFHHILMDGWCLPLITKEIFENYFALL 1476
Cdd:cd19533    81 IDLSG--DPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDN--RHFWyqRVHHIVMDGFSFALFGQRVAEIYTALL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1477 QQKQPEQSSITPYSQYIEwlGRQDAKEA------AAYWDQYLEGYEEQTGLPKdhhAAEDGRYVPEKVTCDISSDLTSKM 1550
Cdd:cd19533   157 KGRPAPPAPFGSFLDLVE--EEQAYRQSerferdRAFWTEQFEDLPEPVSLAR---RAPGRSLAFLRRTAELPPELTRTL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1551 KRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRpAGiPNVETMIGLFINTIPVRFRCEAGTTFAELMK---E 1627
Cdd:cd19533   232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR-LG-AAARQTPGMVANTLPLRLTVDPQQTFAELVAqvsR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1628 AQERAVASQKFETHPLYDIQARTTQKQDLITHLMifeNYPVDQYMESIGRQNGTSITISNVQMEeqtnyDFNLTV---IP 1704
Cdd:cd19533   310 ELRSLLRHQRYRYEDLRRDLGLTGELHPLFGPTV---NYMPFDYGLDFGGVVGLTHNLSSGPTN-----DLSIFVydrDD 381
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 166797876 1705 GDEMNISFEYNANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19533   382 ESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
3297-3781 7.74e-35

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 142.45  E-value: 7.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEG--KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRY 3374
Cdd:cd05926     1 PDAPALVVPGstPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3375 ILNDSSISVLL--YCGKLQDD---IGFSGTCIDLMEEHF-YHEKDSSLALSY--------------QSSQLAYAIYTSGT 3434
Cdd:cd05926    81 YLADLGSKLVLtpKGELGPASraaSKLGLAILELALDVGvLIRAPSAESLSNlladkknaksegvpLPDDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3435 TGKPKGTLIEHRQVIHLIEGLSRqVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKeivSDGAALCRYYRQ 3514
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITN-TYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPR---FSASTFWPDVRD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3515 HSIDITDGTPA-HLKLLIAAGDLQGVTLQHL-LI--GGEALSKTTVNKLKQLFGehgaAPGItNVYGPTETCVDASLFNI 3590
Cdd:cd05926   237 YNATWYTAVPTiHQILLNRPEPNPESPPPKLrFIrsCSASLPPAVLEALEATFG----APVL-EAYGMTEAAHQMTSNPL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3591 EcssdawARSQNYVPIGKPLGrNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTG 3670
Cdd:cd05926   312 P------PGPRKPGSVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTG 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3671 DLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdaddeyylCGYFA--------------- 3735
Cdd:cd05926   379 DLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLE---------------AVAFGvpdekygeevaaavv 443
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 3736 --ADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05926   444 lrEGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1798-2261 9.73e-35

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 142.77  E-value: 9.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLM 1877
Cdd:cd12119    24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1878 QRD-------VRKQLA-YEGVTVLLDDES----------SYHQ---DGSDLAPISDVS-HLAYVI-YTSGSTGRPKGVLI 1934
Cdd:cd12119   104 DRDflplleaIAPRLPtVEHVVVMTDDAAmpepagvgvlAYEEllaAESPEYDWPDFDeNTAAAIcYTSGTTGNPKGVVY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1935 EHggltnyiwwaKEVYVKGEKANfplySSISFDLTVTSIFTPLV----------------TGnAIIVYDG-EDKTALLES 1997
Cdd:cd12119   184 SH----------RSLVLHAMAAL----LTDGLGLSESDVVLPVVpmfhvnawglpyaaamVG-AKLVLPGpYLDPASLAE 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1998 IVRDPRVDIIKLTPAHLQ-VLKEM--NIADQTAVRRMIVGGENLStrlaRSIHEQFEGR-IEICNEYGPTETV-VGCMIY 2072
Cdd:cd12119   249 LIEREGVTFAAGVPTVWQgLLDHLeaNGRDLSSLRRVVIGGSAVP----RSLIEAFEERgVRVIHAWGMTETSpLGTVAR 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2073 R--------YDAAKDRRESvpIGTAAANTSIYVLDENMKPAPI-GVP-GEIYISGAGVARGYLNRPELTAEKFVDDPFep 2142
Cdd:cd12119   325 PpsehsnlsEDEQLALRAK--QGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTEDGWL-- 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2143 gakmyKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQT 2220
Cdd:cd12119   401 -----RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVlkEGATV 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 166797876 2221 TAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd12119   476 TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
3283-3715 2.91e-34

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 141.11  E-value: 2.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3283 KTIHELFEEQAHRTPDNTAVVF--EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAY 3360
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3361 LPIDPDSPSERIRY-ILNDSSISVLLYCGKL-QDDIGFSGTCIDLMEEhfyhEKDSSLALSYQSS---------QLAYAI 3429
Cdd:cd05923    81 ALINPRLKAAELAElIERGEMTAAVIAVDAQvMDAIFQSGVRVLALSD----LVGLGEPESAGPLiedpprepeQPAFVF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3430 YTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIvsDGAALC 3509
Cdd:cd05923   157 YTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADAL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3510 RYYRQHSIDITDGTPAHLKLLIAAGDLQGV---TLQHLLIGGEALSKTTVNKLkqlfgeHGAAPG-ITNVYGPTETCvdA 3585
Cdd:cd05923   235 KLIEQERVTSLFATPTHLDALAAAAEFAGLklsSLRHVTFAGATMPDAVLERV------NQHLPGeKVNIYGTTEAM--N 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3586 SLFNIECSSDAWARSQNY-----VPIGkplgrnrmyilDSKKRLQPKGVQGELYIA--GDGVGRGYLNLPELTDEKFVad 3658
Cdd:cd05923   307 SLYMRDARTGTEMRPGFFsevriVRIG-----------GSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQ-- 373
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3659 pfvpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05923   374 -----DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTE 425
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2829-3249 4.00e-34

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 138.93  E-value: 4.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLF-HSLLDEaSSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWNDTPLQIVyktQTPQIHF 2907
Cdd:cd20483     3 PMSTFQRRLWFlHNFLED-KTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVL---DDPSFHL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2908 aDLRDI-EEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQE 2986
Cdd:cd20483    79 -IVIDLsEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2987 GREPEPLSAVP--YSDYIEWLDRQDQGAAKR----YWSGYLEGYKGETTLL--HKIAQHEQKEYAYANLICRFDHEQTKQ 3058
Cdd:cd20483   158 GRDLATVPPPPvqYIDFTLWHNALLQSPLVQplldFWKEKLEGIPDASKLLpfAKAERPPVKDYERSTVEATLDKELLAR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3059 LQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAeiPDVEQMIGLFINTIPVRIRCDEDSTFADTMQMVQ 3138
Cdd:cd20483   238 MKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3139 QNALASQSYDTYPLYEIQAQTEQKQNLiDHimifenYPIGQQAEETGHHGT--ELNITNFHMQEHSHYD--------LNV 3208
Cdd:cd20483   316 TTCLEAYEHSAVPFDYIVDALDVPRST-SH------FPIGQIAVNYQVHGKfpEYDTGDFKFTDYDHYDiptacdiaLEA 388
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 166797876 3209 VVIPGKQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVLRQ 3249
Cdd:cd20483   389 EEDPDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
PRK06178 PRK06178
acyl-CoA synthetase; Validated
261-754 7.65e-34

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 140.95  E-value: 7.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  261 GSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAY 340
Cdd:PRK06178   31 GERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVH 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  341 VPLDPEYPKERLQYLLHDADADVLLVQ-----------------HHLKNSLA--------------FDGPVI---DLNDE 386
Cdd:PRK06178  111 VPVSPLFREHELSYELNDAGAEVLLALdqlapvveqvraetslrHVIVTSLAdvlpaeptlplpdsLRAPRLaaaGAIDL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  387 ASYHADCS--LLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRV-LVLYPYVFDA---FIL 460
Cdd:PRK06178  191 LPALRACTapVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVfLSFLPEFWIAgenFGL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  461 NFfgPLISGATLHLLpNEENKETFAiqNAIKQERITHFSTsprLLKTMIEQMN-----REDFIHVQHVVVGG--EQLETD 533
Cdd:PRK06178  271 LF--PLFSGATLVLL-ARWDAVAFM--AAVERYRVTRTVM---LVDNAVELMDhprfaEYDLSSLRQVRVVSfvKKLNPD 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  534 TVEKLHSLQPRIRINNEYGPTENSVVSTFHPVQSAD------EQITIGSPVANHQAYILG-AHHQIQPIGIPGELYVGGA 606
Cdd:PRK06178  343 YRQRWRALTGSVLAEAAWGMTETHTCDTFTAGFQDDdfdllsQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTP 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  607 GVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAV 686
Cdd:PRK06178  423 SLLKGYWNKPEATAEALRD-------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAV 495
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876  687 VAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIpLERIPLTSNGKI---DLKALPAADE 754
Cdd:PRK06178  496 VGRPDPDKGQVPVAFVQLKPgaDLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVrkqDLQALAEELK 567
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1797-2264 1.21e-33

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 138.58  E-value: 1.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1797 DRQLTYGELNKRANRLARTLRAKGvqtdqPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVL 1876
Cdd:PRK07787   23 GRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 MQRDvRKQLAYEGVTVLLddessyHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYI--------WWAKE 1948
Cdd:PRK07787   98 GPAP-DDPAGLPHVPVRL------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLdalaeawqWTADD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1949 VYVKGekanFPLYSSISFdltVTSIFTPLVTGNAII--------VYDGE--DKTALL-------ESIVRDPrvdiikltp 2011
Cdd:PRK07787  171 VLVHG----LPLFHVHGL---VLGVLGPLRIGNRFVhtgrptpeAYAQAlsEGGTLYfgvptvwSRIAADP--------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2012 ahlqvlkemNIADQTAVRRMIVGGenlSTRLARSIHEQFEGRI--EICNEYGPTETVVGCMIyRYDAakDRResvP--IG 2087
Cdd:PRK07787  235 ---------EAARALRGARLLVSG---SAALPVPVFDRLAALTghRPVERYGMTETLITLST-RADG--ERR---PgwVG 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2088 TAAANTSIYVLDENMKPAPIGVP--GEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAG 2165
Cdd:PRK07787  297 LPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVG 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2166 R--IDeQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFI 2243
Cdd:PRK07787  371 ResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPREVR 449
                         490       500
                  ....*....|....*....|.
gi 166797876 2244 ELDEMPLTSNGKINKKGLPAP 2264
Cdd:PRK07787  450 FVDALPRNAMGKVLKKQLLSE 470
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1320-1741 1.27e-33

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 137.20  E-value: 1.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLF--HSLFDPNsgAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFY-RGWKDQPLQIIFKTKKIGF 1396
Cdd:cd19532     3 PMSFGQSRFWFlqQYLEDPT--TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFtDPEDGEPMQGVLASSPLRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1397 qfndlrEMKESQKEAMIQKYAREDKMRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYfall 1476
Cdd:cd19532    81 ------EHVQISDEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1477 qQKQPEQSSItpySQYIEWLGRQDAKEAAAYWDQYLEGYEEQ-TGLPK-------------------DHHaaedgryvpe 1536
Cdd:cd19532   151 -NGQPLLPPP---LQYLDFAARQRQDYESGALDEDLAYWKSEfSTLPEplpllpfakvksrppltryDTH---------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1537 KVTCDISSDLTSKMKRTAGKHHVT-----LntllqTAWAVLLQKYNRSRDVVFGSVVSGRpagiPNVETM--IGLFINTI 1609
Cdd:cd19532   217 TAERRLDAALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDDICIGIADANR----TDEDFMetIGFFLNLL 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1610 PVRFRCEAGTTFAELMKEAQERAVASQK-----FE------------TH-PLYdiQArttqkqdlithlmiFENYpvdqy 1671
Cdd:cd19532   288 PLRFRRDPSQTFADVLKETRDKAYAALAhsrvpFDvlldelgvprsaTHsPLF--QV--------------FINY----- 346
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 1672 mesigRQNGT-SITISNVQMEE------QTNYDFNLTVI--PGDEMNISFEYNANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19532   347 -----RQGVAeSRPFGDCELEGeefedaRTPYDLSLDIIdnPDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARD 420
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1798-2198 1.59e-33

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 137.73  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAgivlm 1877
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1878 qrdvrkqlayegvtvllddessyhqdgsDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGgltNYIWWAK---EVYVKGE 1954
Cdd:cd05907    79 ----------------------------KALFVEDPDDLATIIYTSGTTGRPKGVMLSHR---NILSNALalaERLPATE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1955 KANF----PLysSISFDlTVTSIFTPLVTGnAIIVYDGEDKTALLES-------IVRDPRV-------DIIKLTPAHLQV 2016
Cdd:cd05907   128 GDRHlsflPL--AHVFE-RRAGLYVPLLAG-ARIYFASSAETLLDDLsevrptvFLAVPRVwekvyaaIKVKAVPGLKRK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2017 LKEMNIADQtaVRRMIVGGENLSTRLARsiheQFEGR-IEICNEYGPTET--VVGCMiyryDAAKDRRESVpiGTAAANT 2093
Cdd:cd05907   204 LFDLAVGGR--LRFAASGGAPLPAELLH----FFRALgIPVYEGYGLTETsaVVTLN----PPGDNRIGTV--GKPLPGV 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2094 SIYVLDEnmkpapigvpGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRI-DEQVK 2172
Cdd:cd05907   272 EVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKkDLIIT 335
                         410       420
                  ....*....|....*....|....*.
gi 166797876 2173 IRGYRIELGEIEAALLQEEVIKEAVV 2198
Cdd:cd05907   336 SGGKNISPEPIENALKASPLISQAVV 361
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
273-744 1.70e-33

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 139.68  E-value: 1.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKF------KNDHLTYRELNEKASRLARTLRNCGVQPDTlVAILADRSLEMIVSIIAVWKAGGAYVPL-DP 345
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  346 EYPK--ERLQYLLHDADADVLL-----------VQHHLKNSLAFDGPVIDLNDEASyhADcSLLSPVAGHSHLAYVIYTS 412
Cdd:cd05931    82 TPGRhaERLAAILADAGPRVVLttaaalaavraFAASRPAAGTPRLLVVDLLPDTS--AA-DWPPPSPDPDDIAYLQYTS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  413 GTTGKPKGVMVEHGGIV-NSLQWKKAFFkHSPADRVLVLYPYVFD-AFILNFFGPLISGATLHLLPneenKETFaIQN-- 488
Cdd:cd05931   159 GSTGTPKGVVVTHRNLLaNVRQIRRAYG-LDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGPSVLMS----PAAF-LRRpl 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  489 ----AIKQERITHfSTSP----RLL--KTMIEQMNREDFIHVQHVVVGGEQLETDTVEKL-----------HSLQPriri 547
Cdd:cd05931   233 rwlrLISRYRATI-SAAPnfayDLCvrRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFaeafapfgfrpEAFRP---- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  548 nnEYGPTENSVVSTFHPV-------------------------QSADEQITIGSPVANHQAYIL-GAHHQIQPIGIPGEL 601
Cdd:cd05931   308 --SYGLAEATLFVSGGPPgtgpvvlrvdrdalagravavaaddPAARELVSCGRPLPDQEVRIVdPETGRELPDGEVGEI 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  602 YVGGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGDLARwLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNL-EN 680
Cdd:cd05931   386 WVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAhPA 464
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876  681 VREAAVVA-REDADGAKQLYA-------YYVGEPSLTAAQFREELSRE--LPNYMIpsRFIPLERIPLTSNGKI 744
Cdd:cd05931   465 LRPGCVAAfSVPDDGEERLVVvaevergADPADLAAIAAAIRAAVAREhgVAPADV--VLVRPGSIPRTSSGKI 536
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1772-2278 5.57e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 138.17  E-value: 5.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1772 PQTPVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAK-GVQTDQPVAIITRNSIESVVGILAVLKSGGA 1850
Cdd:PRK08314    8 PETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1851 YVPIDPEYPQDRIRYMLDDSQAGIVLMQRD----VRKQLAYEGVT-VLLDDESSYHQDGSDLA---------PISDVSH- 1915
Cdd:PRK08314   88 VVPVNPMNREEELAHYVTDSGARVAIVGSElapkVAPAVGNLRLRhVIVAQYSDYLPAEPEIAvpawlraepPLQALAPg 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1916 ------------------------LAYVIYTSGSTGRPKGVLIEHGGLT-----NYIWwakevyVKGEKANFPLYSSISF 1966
Cdd:PRK08314  168 gvvawkealaaglappphtagpddLAVLPYTSGTTGVPKGCMHTHRTVManavgSVLW------SNSTPESVVLAVLPLF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1967 DLT--VTSIFTPLVTGNAIIVYDGEDKTALLESIVRDpRVDIIKLTPAHL-QVLKEMNIA--DQTAVRRMIVGGENLSTR 2041
Cdd:PRK08314  242 HVTgmVHSMNAPIYAGATVVLMPRWDREAAARLIERY-RVTHWTNIPTMVvDFLASPGLAerDLSSLRYIGGGGAAMPEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2042 LARSIHEQF-----EGrieicneYGPTETVVGCMIYRYDAAKDRRESVPIgtaaANTSIYVLD-ENMKPAPIGVPGEIYI 2115
Cdd:PRK08314  321 VAERLKELTgldyvEG-------YGLTETMAQTHSNPPDRPKLQCLGIPT----FGVDARVIDpETLEELPPGEVGEIVV 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2116 SGAGVARGYLNRPELTAEKFVDdpFEpGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKE 2195
Cdd:PRK08314  390 HGPQVFKGYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQE 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2196 AVVTAREDVHGFKQLCAYYV----SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKglpapdfELQDR 2271
Cdd:PRK08314  467 ACVIATPDPRRGETVKAVVVlrpeARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWR-------QLQEQ 539

                  ....*..
gi 166797876 2272 AEYKAPR 2278
Cdd:PRK08314  540 EKARAAK 546
PRK12467 PRK12467
peptide synthase; Provisional
4915-5335 5.99e-33

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 142.61  E-value: 5.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4915 IPKAKAKDVYPVSSVQK-MVYLTTQIIGGELPYNMTgILETEGkLPLNRLLTAFQRLMQGHEPLRT--VVEMVREEAVQV 4991
Cdd:PRK12467 2638 VAVGDIEDIYPLSPMQQgMLFHTLYEGGAGDYINQM-RVDVEG-LDVERFRTAWQAVIDRHEILRSgfLWDGELEEPLQV 2715
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4992 IKSQVEFSMERY--------EATADEVEECFRAfvRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEK 5063
Cdd:PRK12467 2716 VYKQARLPFSRLdwrdradlEQALDALAAADRQ--QGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGE 2793
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5064 LIQLYDGKELAPLRIQYKDFTEWKhqkeQRERIKSQEEYWlgvfHEELPSFELPKDFAR----PPVRSFDGK-RHNFTLD 5138
Cdd:PRK12467 2794 VLQRYFGQPPPAREGRYRDYIAWL----QAQDAEASEAFW----KEQLAALEEPTRLARalypAPAEAVAGHgAHYLHLD 2865
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5139 KTVTQGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPhADL---EPIIGMFVNTLAIRTAPMAEKTFL 5215
Cdd:PRK12467 2866 ATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRP-AQLrgaEQQLGLFINTLPVIASPRAEQTVS 2944
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5216 DYITETKETMLKAFEHQEYPFEELVEKLGvkrdLSRNPLFDTMFV---------LQNTEQTDIEVDSLAVRpyEQTETAA 5286
Cdd:PRK12467 2945 DWLQQVQAQNLALREFEHTPLADIQRWAG----QGGEALFDSILVfenypiseaLKQGAPSGLRFGAVSSR--EQTNYPL 3018
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876 5287 KFDLQLNfliDQDEIQgsFDYCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:PRK12467 3019 TLAVGLG---DTLELE--FSYDRQHFDAAAIERLAESFDRLLQAMLNNP 3062
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
284-744 6.37e-33

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 136.42  E-value: 6.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  284 FKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADV 363
Cdd:cd05914     3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  364 LLVQHhlknslafdgpvidlNDEasyhadcsllspvaghshLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSP 443
Cdd:cd05914    83 IFVSD---------------EDD------------------VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGK 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  444 ADRVLVL------YPYVFDaFILnffgPLISGATLHLLpneeNKETFAIQNAIKQERITHFSTSPRLL-------KTMIE 510
Cdd:cd05914   130 GDKILSIlplhhiYPLTFT-LLL----PLLNGAHVVFL----DKIPSAKIIALAFAQVTPTLGVPVPLviekifkMDIIP 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  511 QMNREDFI--------------------------HVQHVVVGGEQLETDTVEKLHSLQPRIRINneYGPTENSVVSTFHP 564
Cdd:cd05914   201 KLTLKKFKfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLRTIGFPYTIG--YGMTETAPIISYSP 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  565 vqsaDEQITIGS---PVANHQAYIlgahHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGD 639
Cdd:cd05914   279 ----PNRIRLGSagkVIDGVEVRI----DSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDgwFH--------TGD 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  640 LARWLPDGRIEYLGRIDHQ-VKIRGYRIEIGEVEAAMFNLENVREAAVVAREDaDGAKQLYAYYVGEPSLTAAQ------ 712
Cdd:cd05914   343 LGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK-KLVALAYIDPDFLDVKALKQrniida 421
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 166797876  713 ----FREELSRELPNYMIPSRF-IPLERIPLTSNGKI 744
Cdd:cd05914   422 ikweVRDKVNQKVPNYKKISKVkIVKEEFEKTPKGKI 458
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
261-744 1.74e-32

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 136.42  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  261 GSRTVYQLFEEQAERTPENAAVKfkNDH---LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAG 337
Cdd:PRK06087   21 GDASLADYWQQTARAMPDKIAVV--DNHgasYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  338 GAYVPLDPEYPKERLQYLLHDADADVLLVQ------------HHLKNSLAFDGPVIDLNDEASYHADCS----------L 395
Cdd:PRK06087   99 AVSVPLLPSWREAELVWVLNKCQAKMFFAPtlfkqtrpvdliLPLQNQLPQLQQIVGVDKLAPATSSLSlsqiiadyepL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  396 LSPVAGHS-HLAYVIYTSGTTGKPKGVMVEHGGIVNS---------LQWKKAFFKHSPADRVlvlypyvfDAFILNFFGP 465
Cdd:PRK06087  179 TTAITTHGdELAAVLFTSGTEGLPKGVMLTHNNILASeraycarlnLTWQDVFMMPAPLGHA--------TGFLHGVTAP 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  466 LISGATLHLLpnEENKETFAIQnAIKQERIT-HFSTSP---RLLKTMIEQmnREDFIHVQHVVVGGEQLETDTVEklHSL 541
Cdd:PRK06087  251 FLIGARSVLL--DIFTPDACLA-LLEQQRCTcMLGATPfiyDLLNLLEKQ--PADLSALRFFLCGGTTIPKKVAR--ECQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  542 QPRIRINNEYGPTEnsvvSTFHPVQSADEQI-----TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRP 616
Cdd:PRK06087  324 QRGIKLLSVYGSTE----SSPHAVVNLDDPLsrfmhTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  617 ELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYLGRiDHQVKIR-GYRIEIGEVEAAMFNLENVREAAVVAREDADGA 695
Cdd:PRK06087  400 ELTARALDE------EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLG 472
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876  696 KQLYAYYV---GEPSLTAAQFREELSRE-LPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK06087  473 ERSCAYVVlkaPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKI 525
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
289-744 1.76e-32

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 135.50  E-value: 1.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:cd12118    30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 hlknslAFDGpvIDLNDEASyhADCSLLSPVAGHSHLAyVIYTSGTTGKPKGVMVEHGG-----IVNSLQWKkafFKHSP 443
Cdd:cd12118   110 ------EFEY--EDLLAEGD--PDFEWIPPADEWDPIA-LNYTSGTTGRPKGVVYHHRGaylnaLANILEWE---MKQHP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  444 adrvlvLYPYVFDAFILN---F-FGPLISGATLHLLPNEENKETFAiqnAIKQERITHFSTSPRLLKTMIEQM--NREDF 517
Cdd:cd12118   176 ------VYLWTLPMFHCNgwcFpWTVAAVGGTNVCLRKVDAKAIYD---LIEKHKVTHFCGAPTVLNMLANAPpsDARPL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  518 IHVQHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTENSVVSTFHPVQ------SADEQITI----GSPVANHQAYILG 587
Cdd:cd12118   247 PHRVHVMTAGAPPPAAVLAKMEELG--FDVTHVYGLTETYGPATVCAWKpewdelPTEERARLkarqGVRYVGLEEVDVL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  588 AHHQIQPIgiP------GELYVGGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKI 661
Cdd:cd12118   325 DPETMKPV--PrdgktiGEIVFRGNIVMKGYLKNPEATAEAFRG-------GWFHSGDLAVIHPDGYIEIKDRSKDIIIS 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLErIPLT 739
Cdd:cd12118   396 GGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEgaKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKT 474

                  ....*
gi 166797876  740 SNGKI 744
Cdd:cd12118   475 STGKI 479
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3307-3781 2.09e-32

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 134.10  E-value: 2.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3307 KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLy 3386
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3387 cgklqddigfsgtcIDLmeehfyhekdsslalsyqSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGlsrqVYSAYDae 3466
Cdd:cd05971    84 --------------TDG------------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPG----VQFPFN-- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3467 lniamLAP-----YYFDAS-------VQQMYASLLSGhtlfiVPkeIVS------DGAALCRYYRQHSIDITDGTPAHLK 3528
Cdd:cd05971   126 -----LFPrdgdlYWTPADwawigglLDVLLPSLYFG-----VP--VLAhrmtkfDPKAALDLMSRYGVTTAFLPPTALK 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3529 LLIAAG---DLQGVTLQHLLIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTET------CvdASLFNIECSSdawar 3599
Cdd:cd05971   194 MMRQQGeqlKHAQVKLRAIATGGESLGEELLGWAREQFGVE-----VNEFYGQTECnlvignC--SALFPIKPGS----- 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3600 sqnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIA-GDGVGR-GYLNLPELTDEKFVADPFvpedrmyRTGDLARLLP 3677
Cdd:cd05971   262 ------MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGDWL-------LTGDLGRKDS 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3678 DGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS-----ELRKRMARH 3752
Cdd:cd05971   329 DGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdalarEIQELVKTR 408
                         490       500
                  ....*....|....*....|....*....
gi 166797876 3753 LPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05971   409 LAAHEYPREIEFVNELPRTATGKIRRREL 437
PRK08316 PRK08316
acyl-CoA synthetase; Validated
273-747 3.50e-32

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 135.06  E-value: 3.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVQ----------HHLKNSLAF-----------DGPVIDLNDEASYHADCSLLSPVAGhSHLAYVIYT 411
Cdd:PRK08316  101 AYILDHSGARAFLVDpalaptaeaaLALLPVDTLilslvlggreaPGGWLDFADWAEAGSVAEPDVELAD-DDLAQILYT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  412 SGTTGKPKGVMVEHGGIVNslQWKKAFF--KHSPADRVLVLYPYVFDAFILNFFGPLIS-GATLHLLPNEENKETFAIqn 488
Cdd:PRK08316  180 SGTESLPKGAMLTHRALIA--EYVSCIVagDMSADDIPLHALPLYHCAQLDVFLGPYLYvGATNVILDAPDPELILRT-- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  489 aIKQERITHFSTSPrllkTM-IEQMNREDFihvqhvvvGGEQLETDT----------VEKLHSLQ---PRIRINNEYGPT 554
Cdd:PRK08316  256 -IEAERITSFFAPP----TVwISLLRHPDF--------DTRDLSSLRkgyygasimpVEVLKELRerlPGLRFYNCYGQT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  555 EnsvVSTFHPVQSADEQI----TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVE---Hl 627
Cdd:PRK08316  323 E---IAPLATVLGPEEHLrrpgSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGgwfH- 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  628 hvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV--GE 705
Cdd:PRK08316  399 ---------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVpkAG 469
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 166797876  706 PSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIdLK 747
Cdd:PRK08316  470 ATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI-LK 510
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3306-3780 3.62e-32

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 133.19  E-value: 3.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3306 GKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL 3385
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3386 ycgklqddigfsgtcIDLmeehfyhekdsslalsyqssqlAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQvYSAYDA 3465
Cdd:cd05934    81 ---------------VDP----------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARR-FGLGED 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3466 ELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSdgaalcRYYRQ---HSIDITDGTPAHLKLLIAAGDLQGVTlQ 3542
Cdd:cd05934   123 DVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSAS------RFWSDvrrYGATVTNYLGAMLSYLLAQPPSPDDR-A 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3543 HLLigGEALSKTTVNKLKQLFGEHGAAPGItNVYGPTETCVdaslfnieCSSDAWARSQNYVPIGKPLGRNRMYILDSKK 3622
Cdd:cd05934   196 HRL--RAAYGAPNPPELHEEFEERFGVRLL-EGYGMTETIV--------GVIGPRDEPRRPGSIGRPAPGYEVRIVDDDG 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3623 RLQPKGVQGELYI---AGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIE 3699
Cdd:cd05934   265 QELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3700 LGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADK--TIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK-L 3776
Cdd:cd05934   338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgeTLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKvA 417

                  ....
gi 166797876 3777 NRQL 3780
Cdd:cd05934   418 KAQL 421
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1779-2258 3.80e-32

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 135.26  E-value: 3.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1779 LFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY 1858
Cdd:PRK06164   15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 PQDRIRYMLDDSQAGIVLMQRDVRK--------------QLAYEGVTVLLDDESS--------YHQ--DGSDLAPI---- 1910
Cdd:PRK06164   95 RSHEVAHILGRGRARWLVVWPGFKGidfaailaavppdaLPPLRAIAVVDDAADAtpapapgaRVQlfALPDPAPPaaag 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1911 ---SDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYD 1987
Cdd:PRK06164  175 eraADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEP 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1988 GEDkTALLESIVRDPRVdiikltpAHLQVLKEM--NIADQTAVRR-----MIVGGENLSTRLARSIHEQFEGRIEICNEY 2060
Cdd:PRK06164  255 VFD-AARTARALRRHRV-------THTFGNDEMlrRILDTAGERAdfpsaRLFGFASFAPALGELAALARARGVPLTGLY 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2061 GPTETVVGCMIYRY-DAAKDRRES--VPIGTAAANTSIYVLDENMKPApiGVPGEIYISGAGVARGYLNRPELTAEKFVD 2137
Cdd:PRK06164  327 GSSEVQALVALQPAtDPVSVRIEGggRPASPEARVRARDPQDGALLPD--GESGEIEIRAPSLMRGYLDNPDATARALTD 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2138 DPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREdvHGFKQLCAYYV-- 2215
Cdd:PRK06164  405 DGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT--RDGKTVPVAFVip 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 2216 -SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLT--SNG-KINK 2258
Cdd:PRK06164  477 tDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQK 523
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
239-744 3.90e-32

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 136.17  E-value: 3.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  239 ILPEAQKQKLLFDF-NDTVRDFSGSR--TVYQLFEEQAERTPENAAVKFKND------HLTYRELNEKASRLARTLRNCG 309
Cdd:cd17634    26 ITPYQKVKNTSFAPgAPSIKWFEDATlnLAANALDRHLRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLDLG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  310 VQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLL-------------VQHHLKNSLAF 376
Cdd:cd17634   106 VKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrsvpLKKNVDDALNP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  377 DGP----VIDLNDEAS-----------YHADCSLLSPVAGHSHLA-----YVIYTSGTTGKPKGVMVEHGGIVNSLQWKK 436
Cdd:cd17634   186 NVTsvehVIVLKRTGSdidwqegrdlwWRDLIAKASPEHQPEAMNaedplFILYTSGTTGKPKGVLHTTGGYLVYAATTM 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  437 AF-FKHSPADRV--------LVLYPYVFdafilnfFGPLISGATLHLLPNEENKET-FAIQNAIKQERITHFSTSPRLLK 506
Cdd:cd17634   266 KYvFDYGPGDIYwctadvgwVTGHSYLL-------YGPLACGATTLLYEGVPNWPTpARMWQVVDKHGVNILYTAPTAIR 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  507 TMI----EQMNREDFIHVQHVVVGGEQLETDTVEKL--HSLQPRIRINNEYGPTENSvvSTFHPVQSADEQITIGS---P 577
Cdd:cd17634   339 ALMaagdDAIEGTDRSSLRILGSVGEPINPEAYEWYwkKIGKEKCPVVDTWWQTETG--GFMITPLPGAIELKAGSatrP 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  578 VANHQAYILGAHHQIQPIGIPGELYVGGA--GVARGYLNRPELTEEKFVEHLhvpgQKMYKTGDLARWLPDGRIEYLGRI 655
Cdd:cd17634   417 VFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFSTF----KGMYFSGDGARRDEDGYYWITGRS 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  656 DHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLT-----AAQFREELSRELPNYMIPSRF 730
Cdd:cd17634   493 DDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEpspelYAELRNWVRKEIGPLATPDVV 572
                         570
                  ....*....|....
gi 166797876  731 IPLERIPLTSNGKI 744
Cdd:cd17634   573 HWVDSLPKTRSGKI 586
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
3307-3715 6.81e-32

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 133.10  E-value: 6.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3307 KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLy 3386
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3387 CGKLQDdigfsgtcidlmeehfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVySAYDAE 3466
Cdd:cd05907    83 VEDPDD--------------------------------LATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3467 LNIAML--APYYFDASVQqmYASLLSGHTL-FIVPKEIVSDG---------AALCRYYRQHS--IDITDGTPAHLKLL-I 3531
Cdd:cd05907   130 RHLSFLplAHVFERRAGL--YVPLLAGARIyFASSAETLLDDlsevrptvfLAVPRVWEKVYaaIKVKAVPGLKRKLFdL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3532 AAGDlqgvTLQHLLIGGEALSKTTVNKLKQLfgehgaapGIT--NVYGPTETCVDASLfniecssdawARSQNYVP--IG 3607
Cdd:cd05907   208 AVGG----RLRFAASGGAPLPAELLHFFRAL--------GIPvyEGYGLTETSAVVTL----------NPPGDNRIgtVG 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3608 KPLGRNRMYIldskkrlqpkGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEYIGRI 3687
Cdd:cd05907   266 KPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRK 329
                         410       420
                  ....*....|....*....|....*....
gi 166797876 3688 -DHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05907   330 kDLIITSGGKNISPEPIENALKASPLISQ 358
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
4357-4818 7.67e-32

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 131.70  E-value: 7.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4357 TLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVlltc 4436
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4437 aghaipplfegevlllddpllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLEHK--------TMTNLLAYEQDHT 4508
Cdd:cd05912    77 -----------------------------------DDIATIMYTSGTTGKPKGVQQTFGnhwwsaigSALNLGLTEDDNW 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4509 qlrfdrvlqfaamsfdVCYQEMF--SALSsggILF---IIGNEA----KRDIRQLNDFVRTHGIQTAFLPTAFLKLLASE 4579
Cdd:cd05912   122 ----------------LCALPLFhiSGLS---ILMrsvIYGMTVylvdKFDAEQVLHLINSGKVTIISVVPTMLQRLLEI 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4580 KHyfEPFAECVDHIIAAGEQLIATrMLRDMLARHqVTLHNHYGPSET--HVVTMYTVDPDTdqELQPIGKPISNTEIFIL 4657
Cdd:cd05912   183 LG--EGYPNNLRCILLGGGPAPKP-LLEQCKEKG-IPVYQSYGMTETcsQIVTLSPEDALN--KIGSAGKPLFPVELKIE 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4658 NEagtLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDLArYL-PEGNIEYAGRRDHQVKIRGYR 4736
Cdd:cd05912   257 DD---GQPPYEVGEILLKGPNVTKGYLNRPDATEESFE-------NGWFKTGDIG-YLdEEGFLYVLDRRSDLIISGGEN 325
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4737 VELGEVEAALLKH--VQEAVVLAKEN-TDGQSDLyAYFTAEQSLS----ISQLKEKLAGqipgYMIPSYFIQLEKLPLTG 4809
Cdd:cd05912   326 IYPAEIEEVLLSHpaIKEAGVVGIPDdKWGQVPV-AFVVSERPISeeelIAYCSEKLAK----YKVPKKIYFVDELPRTA 400

                  ....*....
gi 166797876 4810 NGKVNRRAL 4818
Cdd:cd05912   401 SGKLLRHEL 409
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
3279-3687 9.66e-32

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 135.23  E-value: 9.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3279 YPREKTIHELFEEQAHRTPDNTAVVF----EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVL 3354
Cdd:COG1022     7 VPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAIL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3355 KAGGAYLPIDPDSPSERIRYILNDSSISVL------LY---------CGKLQ-----DDIGFSGTCI-----DLME---E 3406
Cdd:COG1022    87 AAGAVTVPIYPTSSAEEVAYILNDSGAKVLfvedqeQLdkllevrdeLPSLRhivvlDPRGLRDDPRllsldELLAlgrE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3407 HFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLsRQVYSAYDAELNIAMLaPyyFDASVQQM-- 3484
Cdd:COG1022   167 VADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARAL-LERLPLGPGDRTLSFL-P--LAHVFERTvs 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3485 YASLLSGHTLFIV--PKEIVSDGAA-----LC-------RYYRQHSIDITDGTPAHLKLLIAAGDLqGVTLQHLLIGGEA 3550
Cdd:COG1022   243 YYALAAGATVAFAesPDTLAEDLREvkptfMLavprvweKVYAGIQAKAEEAGGLKRKLFRWALAV-GRRYARARLAGKS 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3551 LS-----------KTTVNKLKQLFGEH------GAAP------------GIT--NVYGPTETCVDASlFNiecssdawaR 3599
Cdd:COG1022   322 PSlllrlkhaladKLVFSKLREALGGRlrfavsGGAAlgpelarffralGIPvlEGYGLTETSPVIT-VN---------R 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3600 SQNYVP--IGKPLgrnrmyildskkrlqpKGVQ------GELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGD 3671
Cdd:COG1022   392 PGDNRIgtVGPPL----------------PGVEvkiaedGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGD 449
                         490
                  ....*....|....*.
gi 166797876 3672 LARLLPDGNIEYIGRI 3687
Cdd:COG1022   450 IGELDEDGFLRITGRK 465
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
3300-3778 1.02e-31

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 132.20  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3300 TAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDS 3379
Cdd:cd05919     2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3380 SISVLLycgKLQDDIgfsgtcidlmeehfyhekdsslalsyqssqlAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQV 3459
Cdd:cd05919    82 EARLVV---TSADDI-------------------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3460 Y--SAYDAELNIAMLapyYFDASV-QQMYASLLSGHTLFIVPKEIVSDgAALCRYYRqHSIDITDGTPAHLKLLIAAGDL 3536
Cdd:cd05919   128 LglTPGDRVFSSAKM---FFGYGLgNSLWFPLAVGASAVLNPGWPTAE-RVLATLAR-FRPTVLYGVPTFYANLLDSCAG 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3537 QG---VTLQHLLIGGEALSKttvnKLKQLFGEHGAAPgITNVYGPTETcvdASLFnIECSSDAWarsqNYVPIGKPLGRN 3613
Cdd:cd05919   203 SPdalRSLRLCVSAGEALPR----GLGERWMEHFGGP-ILDGIGATEV---GHIF-LSNRPGAW----RLGSTGRPVPGY 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3614 RMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKI 3693
Cdd:cd05919   270 EIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-------NGGWYRTGDKFCRDADGWYTHAGRADDMLKV 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3694 QGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISE-LRKRMARH----LPGYMIPAHFVQLDKM 3768
Cdd:cd05919   343 GGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEsLARDIHRHllerLSAHKVPRRIAFVDEL 422
                         490
                  ....*....|
gi 166797876 3769 PLTPNGKLNR 3778
Cdd:cd05919   423 PRTATGKLQR 432
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
3309-3781 1.15e-31

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 132.12  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3309 FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYCG 3388
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3389 KlqddigFSGTCIDLMeehfyhekdsslalsyqSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIeglsrqvySAYDAELN 3468
Cdd:cd05903    82 R------FRQFDPAAM-----------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASI--------RQYAERLG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3469 iamlapyyFDASVQQMYASLLSGHTLFIVPKEIVS------------DGAALCRYYRQHSIDITDGTPAHLKLLIAAGDL 3536
Cdd:cd05903   131 --------LGPGDVFLVASPMAHQTGFVYGFTLPLllgapvvlqdiwDPDKALALMREHGVTFMMGATPFLTDLLNAVEE 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3537 QGVTLQHL---LIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETCvdASLFNIEcSSDAWARSqnyVPIGKPLGRN 3613
Cdd:cd05903   203 AGEPLSRLrtfVCGGATVPRSLARRAAELLGAK-----VCSAYGSTECP--GAVTSIT-PAPEDRRL---YTDGRPLPGV 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3614 RMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTdekFVADPfvpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKI 3693
Cdd:cd05903   272 EIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLT---ADAAP----EGWFRTGDLARLDEDGYLRITGRSKDIIIR 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3694 QGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFA--ADKTIQISELRKRMARH-LPGYMIPAHFVQLDKMPL 3770
Cdd:cd05903   345 GGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVtkSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPR 424
                         490
                  ....*....|.
gi 166797876 3771 TPNGKLNRQLL 3781
Cdd:cd05903   425 TPSGKVQKFRL 435
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1320-1741 1.59e-31

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 131.23  E-value: 1.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLF-HSLFDPNSgAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKKIGFQF 1398
Cdd:cd19538     3 PLSFAQRRLWFlHQLEGPSA-TYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEE-DGVPYQLILEEDEATPKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1399 NdLREMKESQKEAMIQKYARedkmRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQ 1478
Cdd:cd19538    81 E-IKEVDEEELESEINEAVR----YPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1479 KQPEQSSIT-PYSQYI----EWLGRQDAKEAA-----AYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSDLTS 1548
Cdd:cd19538   156 EAPELAPLPvQYADYAlwqqELLGDESDPDSLiarqlAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1549 KMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELM--- 1625
Cdd:cd19538   236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRTDTSGNPSFRELLerv 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1626 KEAQERAVASQK--FE-------------THPLYDIqarttqkqdlithLMIFENYPVDQY-MEsigrQNGTSITISNVQ 1689
Cdd:cd19538   314 KETNLEAYEHQDipFErlvealnptrsrsRHPLFQI-------------MLALQNTPQPSLdLP----GLEAKLELRTVG 376
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 1690 meeQTNYD--FNLTVIPGDE----MNISFEYNANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19538   377 ---SAKFDltFELREQYNDGtpngIEGFIEYRTDLFDHETIEALAQRYLLLLESAVEN 431
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
3916-4298 1.86e-31

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 130.50  E-value: 1.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3916 TVEGKLDRDKLQQAFRTLILRHESLRTGF-KMADGEPVQYVLDHAAFEaeWyqGEEDDADLYIRQFI-RPFHLDEPpLLR 3993
Cdd:cd19545    29 ELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPIS--W--TESTSLDEYLEEDRaAPMGLGGP-LVR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3994 VGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEGETLPPlRIQYKDYAvwqtgeARLQQIQKQEA--YWLELYS 4071
Cdd:cd19545   104 LALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPFSRFV------KYLRQLDDEAAaeFWRSYLA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4072 GDVPVLH--LPADYIRPSARDFAGATMHftldkqksdgLKQLASQ--TESTlymVLLASYTLLLSKYSGQEDIIVGSPIA 4147
Cdd:cd19545   177 GLDPAVFppLPSSRYQPRPDATLEHSIS----------LPSSASSgvTLAT---VLRAAWALVLSRYTGSDDVVFGVTLS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4148 GR--PHADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQdypfevlidQL---NIAR---DLSRNPLFD 4219
Cdd:cd19545   244 GRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFE---------HTglqNIRRlgpDARAACNFQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4220 TMFVLQnTEQEQLEINDVTFKPYPNGHTMAKFD---LTLTAVEEGAGIQFTLEYLTALFKPETIERMMGHFEQLVDSIIK 4296
Cdd:cd19545   315 TLLVVQ-PALPSSTSESLELGIEEESEDLEDFSsygLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLAS 393

                  ..
gi 166797876 4297 QP 4298
Cdd:cd19545   394 AP 395
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
263-749 1.89e-31

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 132.96  E-value: 1.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQP-DTLVAILADRsLEMIVSIIAVWKAGG--- 338
Cdd:COG1021    25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVVVQLPNV-AEFVIVFFALFRAGAipv 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  339 ---------------------AYVPLDpeypkerlQYLL--HDADADVLLVQH-HLKNSLAFD--GPVIDLndEASYHAD 392
Cdd:COG1021   104 falpahrraeishfaeqseavAYIIPD--------RHRGfdYRALARELQAEVpSLRHVLVVGdaGEFTSL--DALLAAP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  393 CSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFdafilNF-------FGP 465
Cdd:COG1021   174 ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAH-----NFplsspgvLGV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  466 LISGATLHLLPNEENKETFAIqnaIKQERITHFSTSPRLLKTMIEQMNRE--DFIHVQHVVVGGEQLETDTVEklhslqp 543
Cdd:COG1021   249 LYAGGTVVLAPDPSPDTAFPL---IERERVTVTALVPPLALLWLDAAERSryDLSSLRVLQVGGAKLSPELAR------- 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  544 riRINNEYGPT--------ENSVVSTfhPVQSADEQI--TIGSPVANH-QAYILGAHHQIQPIGIPGELYVGGAGVARGY 612
Cdd:COG1021   319 --RVRPALGCTlqqvfgmaEGLVNYT--RLDDPEEVIltTQGRPISPDdEVRIVDEDGNPVPPGEVGELLTRGPYTIRGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  613 LNRPELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYLGRIDHQVkIR-GYRIEIGEVEAAMFNLENVREAAVVARED 691
Cdd:COG1021   395 YRAPEHNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPD 467
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876  692 AdgakqlyayYVGE----------PSLTAAQFREEL-SRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:COG1021   468 E---------YLGErscafvvprgEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1754-2267 1.93e-31

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 133.18  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1754 EGERRTLLQTLNDTAAPFPQTPVHQLfeeQSQRTPDQaavidkdrqLTYGELNKRANRLARTLRAKGVQT-DQPVAIITR 1832
Cdd:cd05906     6 EGAPRTLLELLLRAAERGPTKGITYI---DADGSEEF---------QSYQDLLEDARRLAAGLRQLGLRPgDSVILQFDD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1833 NSiESVVGILAVLKSGG--AYVPIDPEYPQDR--------IRYMLDDsqaGIVL----MQRDVRKQLA---YEGVTVLLD 1895
Cdd:cd05906    74 NE-DFIPAFWACVLAGFvpAPLTVPPTYDEPNarlrklrhIWQLLGS---PVVLtdaeLVAEFAGLETlsgLPGIRVLSI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1896 DESSYHqDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIwwakevyvKGEKANFPLyssisFDLTVTSIFT 1975
Cdd:cd05906   150 EELLDT-AADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARS--------AGKIQHNGL-----TPQDVFLNWV 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1976 PL--VTGNAII----VYDGEDKT-ALLESIVRDP----------RVDIiKLTP----AHL-QVLKEmnIADQT----AVR 2029
Cdd:cd05906   216 PLdhVGGLVELhlraVYLGCQQVhVPTEEILADPlrwldlidryRVTI-TWAPnfafALLnDLLEE--IEDGTwdlsSLR 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2030 RMIVGGENLSTRLAR---SIHEQFEGRIE-ICNEYGPTETVVGCMIYRYDAAKDRRES---VPIGTAAANTSIYVLDENM 2102
Cdd:cd05906   293 YLVNAGEAVVAKTIRrllRLLEPYGLPPDaIRPAFGMTETCSGVIYSRSFPTYDHSQAlefVSLGRPIPGVSMRIVDDEG 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2103 KPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAkWLADGNIEYAGRIDEQVKIRGYRIELGE 2182
Cdd:cd05906   373 QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHE 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2183 IEAALLQEEVIKE---AVVTAREDVHGFKQLCAYYV------SGGQTTAARLRKQLSQTLAsyMVPAYFIEL--DEMPLT 2251
Cdd:cd05906   446 IEAAVEEVPGVEPsftAAFAVRDPGAETEELAIFFVpeydlqDALSETLRAIRSVVSREVG--VSPAYLIPLpkEEIPKT 523
                         570
                  ....*....|....*.
gi 166797876 2252 SNGKINKKGLPApDFE 2267
Cdd:cd05906   524 SLGKIQRSKLKA-AFE 538
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1785-2265 1.97e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 133.51  E-value: 1.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGgayvpidpeypqdrir 1864
Cdd:PRK07788   60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG---------------- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1865 ymlddsqAGIVLMQRDVRK-QLA----YEGVTVLL-DDE----------------------SSYHQDGSDLAPISDV--- 1913
Cdd:PRK07788  124 -------ARIILLNTGFSGpQLAevaaREGVKALVyDDEftdllsalppdlgrlrawggnpDDDEPSGSTDETLDDLiag 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1914 ----------SHLAYVIYTSGSTGRPKGVLIEH-------GGLTNYI-WWAKEVYVkgekanfpLYSSI--SFDLTVTSI 1973
Cdd:PRK07788  197 sstaplpkppKPGGIVILTSGTTGTPKGAPRPEpsplaplAGLLSRVpFRAGETTL--------LPAPMfhATGWAHLTL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1974 FTPLvtGNAIIVYDGEDKTALLESIVRDpRVDIIKLTPAHLQ----VLKEMNIA-DQTAVRRMIVGGENLSTRLARSIHE 2048
Cdd:PRK07788  269 AMAL--GSTVVLRRRFDPEATLEDIAKH-KATALVVVPVMLSrildLGPEVLAKyDTSSLKIIFVSGSALSPELATRALE 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2049 QFeGRIeICNEYGPTETVVGCMIYRYDAAKDrresvP--IGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLN 2126
Cdd:PRK07788  346 AF-GPV-LYNLYGSTEVAFATIATPEDLAEA-----PgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2127 RPEltaEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHG 2206
Cdd:PRK07788  419 GRD---KQIIDG-------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 2207 FKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPD 2265
Cdd:PRK07788  489 GQRLRAFVVkaPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1921-2258 2.29e-31

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 128.93  E-value: 2.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1921 YTSGSTGRPKGVLIEHGGLTNyiwwakEVYVKGEKANF----------PLYSSisFDLtVTSIFTPLVTGNAII-VYDGE 1989
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVN------NGYFIGERLGLteqdrlcipvPLFHC--FGS-VLGVLACLTHGATMVfPSPSF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1990 DKTALLESIVRDpRVDIIKLTP----AHLQvLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGR-IEICneYGPTE 2064
Cdd:cd05917    80 DPLAVLEAIEKE-KCTALHGVPtmfiAELE-HPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIA--YGMTE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2065 TVVGCMIYRYDAAKDRR-ESVpiGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFep 2142
Cdd:cd05917   156 TSPVSTQTRTDDSIEKRvNTV--GRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGW-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2143 gakmYKTGDLAKWLADGNIEYAGRIDEQVkIRG-YRIELGEIEAALLQEEVIKEA-VVTAREDVHGfKQLCAYYV--SGG 2218
Cdd:cd05917   232 ----LHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVqVVGVPDERYG-EEVCAWIRlkEGA 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 166797876 2219 QTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:cd05917   306 ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
263-744 2.73e-31

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 132.87  E-value: 2.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKFKND------HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKA 336
Cdd:PRK13295   24 RTINDDLDACVASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  337 GGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNslaFDGP-----------------VIDLNDEASY---------- 389
Cdd:PRK13295  104 GAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRG---FDHAamarrlrpelpalrhvvVVGGDGADSFeallitpawe 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  390 ---HADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVF-DAFILNFFGP 465
Cdd:PRK13295  181 qepDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHqTGFMYGLMMP 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  466 LISGATLHLLPNEENKETFAIqnaIKQERITHFSTSPRLLKTMIE--QMNREDFIHVQHVVVGGEQLETDTVEklhslQP 543
Cdd:PRK13295  261 VMLGATAVLQDIWDPARAAEL---IRTEGVTFTMASTPFLTDLTRavKESGRPVSSLRTFLCAGAPIPGALVE-----RA 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  544 RIR----INNEYGPTENSVVSTFHPvQSADEQI--TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPE 617
Cdd:PRK13295  333 RAAlgakIVSAWGMTENGAVTLTKL-DDPDERAstTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQ 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  618 LTEEKFvehlhvpgQKMYKTGDLARWLPDGRIEYLGRiDHQVKIRG-YRIEIGEVEAAMFNLENVREAAVVAREDADGAK 696
Cdd:PRK13295  412 LNGTDA--------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERLGE 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876  697 QLYAYYVGEP--SLTAAQFREEL-SRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK13295  483 RACAFVVPRPgqSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKI 533
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
405-749 3.26e-31

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 127.83  E-value: 3.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  405 LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYP--YVFDAFILnfFGPLISGATLHLLPNEenke 482
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPlyHVGGLAIL--VRSLLAGAELVLLERN---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  483 tFAIQNAIKQERITHFSTSPRLLKTMIEQ-MNREDFIHVQHVVVGGEQLETDTVEKLhsLQPRIRINNEYGPTENSvvst 561
Cdd:cd17630    76 -QALAEDLAPPGVTHVSLVPTQLQRLLDSgQGPAALKSLRAVLLGGAPIPPELLERA--ADRGIPLYTTYGMTETA---- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  562 fhpvqsadEQITIGSPVANHQAY---ILGaHHQIQpIGIPGELYVGGAGVARGYLNRPELTEekfvehlhVPGQKMYKTG 638
Cdd:cd17630   149 --------SQVATKRPDGFGRGGvgvLLP-GRELR-IVEDGEIWVGGASLAMGYLRGQLVPE--------FNEDGWFTTK 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  639 DLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELS 718
Cdd:cd17630   211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRAWLK 290
                         330       340       350
                  ....*....|....*....|....*....|.
gi 166797876  719 RELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd17630   291 DKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1916-2259 3.79e-31

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 127.45  E-value: 3.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1916 LAYVIYTSGSTGRPKGVLIEHGGLTnyiwwakeVYVKGEKANFPLYSSISFDLTVtsiftPL--VTGNAIIV-------- 1985
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLL--------ASAAGLHSRLGFGGGDSWLLSL-----PLyhVGGLAILVrsllagae 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1986 -YDGEDKTALLESIVRDPrVDIIKLTPAHLQVLKE--MNIADQTAVRRMIVGGENLSTRLARSIHEQfegRIEICNEYGP 2062
Cdd:cd17630    69 lVLLERNQALAEDLAPPG-VTHVSLVPTQLQRLLDsgQGPAALKSLRAVLLGGAPIPPELLERAADR---GIPLYTTYGM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2063 TETVVGCMIYRYDAAKDRRESVPIGTAAantsiyvLDenmkpapIGVPGEIYISGAGVARGYLNRPEltaekfVDDPFEP 2142
Cdd:cd17630   145 TETASQVATKRPDGFGRGGVGVLLPGRE-------LR-------IVEDGEIWVGGASLAMGYLRGQL------VPEFNED 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2143 GakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTA 2222
Cdd:cd17630   205 G--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP 282
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 166797876 2223 ARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKK 2259
Cdd:cd17630   283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1796-2256 6.13e-31

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 130.25  E-value: 6.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1796 KDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIV 1875
Cdd:cd05914     4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1876 LmqrdvrkqlayegvtvllddessyhqdgsdlapISDVSHLAYVIYTSGSTGRPKGVLIEHggltNYIWW------AKEV 1949
Cdd:cd05914    84 F---------------------------------VSDEDDVALINYTSGTTGNSKGVMLTY----RNIVSnvdgvkEVVL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1950 YVKGEK--ANFPLYSsiSFDLTVTSIfTPLVTGnAIIVYDGEDKTALLESIVRDpRVDIIKLTPAHLQVLK--EMNIADQ 2025
Cdd:cd05914   127 LGKGDKilSILPLHH--IYPLTFTLL-LPLLNG-AHVVFLDKIPSAKIIALAFA-QVTPTLGVPVPLVIEKifKMDIIPK 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2026 TAVRRMI------VGGENLSTRLARSIHEQFEGRIE-----------------------ICNEYGPTETvvGCMIYRYDA 2076
Cdd:cd05914   202 LTLKKFKfklakkINNRKIRKLAFKKVHEAFGGNIKefviggakinpdveeflrtigfpYTIGYGMTET--APIISYSPP 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2077 AKDRRESVPIGTAAANTSIYvldenmKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWL 2156
Cdd:cd05914   280 NRIRLGSAGKVIDGVEVRID------SPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKID 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2157 ADGNIEYAGRIDEQ-VKIRGYRIELGEIEAALLQ--EEVIKEAVVT------------AREDVHGFKQLCAYyvsggQTT 2221
Cdd:cd05914   348 AEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNmpFVLESLVVVQekklvalayidpDFLDVKALKQRNII-----DAI 422
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 166797876 2222 AARLRKQLSQTLASYMVPAYFIEL-DEMPLTSNGKI 2256
Cdd:cd05914   423 KWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKI 458
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1757-2256 6.94e-31

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 132.32  E-value: 6.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1757 RRTLLQTLNDTAAPFPQTPV---HQLFEEQSQRTPDQAAVI------DKDRQLTYGELNKRANRLARTLRAKGVQTDQPV 1827
Cdd:cd17634    33 KNTSFAPGAPSIKWFEDATLnlaANALDRHLRENGDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1828 AIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVL-------------MQRDVRKQLAYEGVTV-- 1892
Cdd:cd17634   113 AIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrsvpLKKNVDDALNPNVTSVeh 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1893 --LLDDESS-----------YHQDGSDLAPISDVSHLA-----YVIYTSGSTGRPKGVLIEHGGLTNYIWWA-KEVYVKG 1953
Cdd:cd17634   193 viVLKRTGSdidwqegrdlwWRDLIAKASPEHQPEAMNaedplFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYG 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1954 EKANFPLYSSISFdLTVTS--IFTPLVTGNAIIVYDGE---DKTALLESIVRDPRVDIIKLTPAHLQVL-----KEMNIA 2023
Cdd:cd17634   273 PGDIYWCTADVGW-VTGHSylLYGPLACGATTLLYEGVpnwPTPARMWQVVDKHGVNILYTAPTAIRALmaagdDAIEGT 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2024 DQTAVRRMIVGGENLSTRLARSIHEQF-EGRIEICNEYGPTETVVGCMIYRYDAAKDRRES--VPI-GTAAAntsiyVLD 2099
Cdd:cd17634   352 DRSSLRILGSVGEPINPEAYEWYWKKIgKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSatRPVfGVQPA-----VVD 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2100 ENMKPAPIGVPGEIYISGA--GVARGYLNRPeltaEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYR 2177
Cdd:cd17634   427 NEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHR 502
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2178 IELGEIEAALLQEEVIKE-AVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYM----VPAYFIELDEMPLTS 2252
Cdd:cd17634   503 LGTAEIESVLVAHPKVAEaAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTR 582

                  ....
gi 166797876 2253 NGKI 2256
Cdd:cd17634   583 SGKI 586
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
3277-3788 7.07e-31

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 131.79  E-value: 7.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3277 MHYPREKTIHELFEEQAHRTPDNTAVVFE-GKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLK 3355
Cdd:PRK06087   17 QGYWGDASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3356 AGGAYLPIDPDSPSERIRYILNDSSiSVLLYCGKLQDDIGFSGTCIDLMEE--HFYH--------EKDSSLALSY----- 3420
Cdd:PRK06087   97 VGAVSVPLLPSWREAELVWVLNKCQ-AKMFFAPTLFKQTRPVDLILPLQNQlpQLQQivgvdklaPATSSLSLSQiiady 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3421 ---------QSSQLAYAIYTSGTTGKPKGTLIEHRQVIhliegLSRQvysAYDAELNIA------MLAPY-----YFDAS 3480
Cdd:PRK06087  176 eplttaittHGDELAAVLFTSGTEGLPKGVMLTHNNIL-----ASER---AYCARLNLTwqdvfmMPAPLghatgFLHGV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3481 VQQMyasLLSGHTlfiVPKEIVSDGAALCRYYRQHSIDITDGTPAHLKLL--IAAGDLQGVTLQHLLIGGEALSKttvnK 3558
Cdd:PRK06087  248 TAPF---LIGARS---VLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLnlLEKQPADLSALRFFLCGGTTIPK----K 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3559 LKQLFGEHGAApgITNVYGPTETCVDAslfniecssdawarsqnYVPIGKPLGRN-----------RMYILDSKKRLQPK 3627
Cdd:PRK06087  318 VARECQQRGIK--LLSVYGSTESSPHA-----------------VVNLDDPLSRFmhtdgyaaagvEIKVVDEARKTLPP 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3628 GVQGELYIAGDGVGRGYLNLPELTDEkfVADpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVM 3707
Cdd:PRK06087  379 GCEGEEASRGPNVFMGYLDEPELTAR--ALD----EEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDIL 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3708 LNVPDIQEAAAAALKDADDEYYLCGYF---AADKTIQISELRKRMAR-HLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPA 3783
Cdd:PRK06087  453 LQHPKIHDACVVAMPDERLGERSCAYVvlkAPHHSLTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532

                  ....*
gi 166797876 3784 PVKKR 3788
Cdd:PRK06087  533 DIMRR 537
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1780-2258 8.72e-31

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 131.33  E-value: 8.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1780 FEEQSQRTPDQAAVID------KDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVP 1853
Cdd:PRK13295   30 LDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1854 IDPEYPQDRIRYMLDDSQAGIVL------------MQRDVRKQL-AYEGVTVL-LDDESSYH--------QDGSDLAPIS 1911
Cdd:PRK13295  110 LMPIFRERELSFMLKHAESKVLVvpktfrgfdhaaMARRLRPELpALRHVVVVgGDGADSFEallitpawEQEPDAPAIL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1912 --------DVSHLayvIYTSGSTGRPKGVLIEHGGL-TNYIWWAKEVYVKGEKANF---PLYSSISFdltVTSIFTPLVT 1979
Cdd:PRK13295  190 arlrpgpdDVTQL---IYTSGTTGEPKGVMHTANTLmANIVPYAERLGLGADDVILmasPMAHQTGF---MYGLMMPVML 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1980 GNAIIVYDGEDKTALLEsIVRDPRVDIIKLTPAHLQVLKEMNIADQTAV---RRMIVGGENLSTRLARSIHEQFEGRIei 2056
Cdd:PRK13295  264 GATAVLQDIWDPARAAE-LIRTEGVTFTMASTPFLTDLTRAVKESGRPVsslRTFLCAGAPIPGALVERARAALGAKI-- 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2057 CNEYGPTETVVGCMIYRYDAakDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAekfv 2136
Cdd:PRK13295  341 VSAWGMTENGAVTLTKLDDP--DERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG---- 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2137 DDpfepGAKMYKTGDLAKWLADGNIEYAGRiDEQVKIRG-YRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV 2215
Cdd:PRK13295  415 TD----ADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVV 489
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876 2216 ---SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:PRK13295  490 prpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQK 535
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1770-2256 1.12e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 131.28  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1770 PFPQTPVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGG 1849
Cdd:PRK05605   28 DYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1850 AYVPIDPEYPQDRIRYMLDDSQAGIVL-------MQRDVRKQLAYEG-VTVLLDDESSYHQ------------------- 1902
Cdd:PRK05605  108 VVVEHNPLYTAHELEHPFEDHGARVAIvwdkvapTVERLRRTTPLETiVSVNMIAAMPLLQrlalrlpipalrkaraalt 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1903 -------------DGSDLAPISDVSH-------LAYVIYTSGSTGRPKGVLIEHGGL-TNYIW---WAKEVYVKGEK--A 1956
Cdd:PRK05605  188 gpapgtvpwetlvDAAIGGDGSDVSHprptpddVALILYTSGTTGKPKGAQLTHRNLfANAAQgkaWVPGLGDGPERvlA 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1957 NFPLYSSisFDLTVTSIFTPLVTGnaiivydgedKTALLESivrdPRVDII-----KLTPAHL-----------QVLKEM 2020
Cdd:PRK05605  268 ALPMFHA--YGLTLCLTLAVSIGG----------ELVLLPA----PDIDLIldamkKHPPTWLpgvpplyekiaEAAEER 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2021 NIaDQTAVRRMIVGGENLSTRLARSIHEQFEGRIeiCNEYGPTET---VVGCMIyrydaAKDRRESVpIGTAAANTSIYV 2097
Cdd:PRK05605  332 GV-DLSGVRNAFSGAMALPVSTVELWEKLTGGLL--VEGYGLTETspiIVGNPM-----SDDRRPGY-VGVPFPDTEVRI 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2098 -----LDENMkpaPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVK 2172
Cdd:PRK05605  403 vdpedPDETM---PDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELII 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2173 IRGYRIELGEIEAALLQEEVIKEAVVT--AREDvhGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEM 2248
Cdd:PRK05605  473 TGGFNVYPAEVEEVLREHPGVEDAAVVglPRED--GSEEVVAAVVlePGAALDPEGLRAYCREHLTRYKVPRRFYHVDEL 550

                  ....*...
gi 166797876 2249 PLTSNGKI 2256
Cdd:PRK05605  551 PRDQLGKV 558
PRK08316 PRK08316
acyl-CoA synthetase; Validated
4333-4818 1.19e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 130.44  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPI 4412
Cdd:PRK08316   12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4413 DPELPEKRRAFMLKDSGADVLLT---CAGHAIPPLFEGEVLLLDDPLLYQGR------TDNLNLSCSE-----------N 4472
Cdd:PRK08316   92 NFMLTGEELAYILDHSGARAFLVdpaLAPTAEAALALLPVDTLILSLVLGGReapggwLDFADWAEAGsvaepdveladD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 DLMYVIYTSGTTGQPKGVQLEHKTmtnLLA----------YEQDhtqlrfDRVLqfAAMSFDVCYQE---MFSALSSGGI 4539
Cdd:PRK08316  172 DLAQILYTSGTESLPKGAMLTHRA---LIAeyvscivagdMSAD------DIPL--HALPLYHCAQLdvfLGPYLYVGAT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4540 LFIIgneAKRDIRQLNDFVRTHGIQTAFL-PTAFLKLLAS-----------EKHYFepfaecvdhiiaaGEQLIATRMLR 4607
Cdd:PRK08316  241 NVIL---DAPDPELILRTIEAERITSFFApPTVWISLLRHpdfdtrdlsslRKGYY-------------GASIMPVEVLK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4608 DMLARH-QVTLHNHYGPSEthVVTMYTV-DPDtDQELQP--IGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGY 4683
Cdd:PRK08316  305 ELRERLpGLRFYNCYGQTE--IAPLATVlGPE-EHLRRPgsAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGY 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4684 HNRESLTLETFVPHPYDSnqrmyktGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQE--------- 4752
Cdd:PRK08316  382 WDDPEKTAEAFRGGWFHS-------GDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHpaVAEvaviglpdp 454
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 4753 -------AVVLAKENTDgqsdlyayfTAEQSLsISQLKEKLAgqipGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK08316  455 kwieavtAVVVPKAGAT---------VTEDEL-IAHCRARLA----GFKVPKRVIFVDELPRNPSGKILKREL 513
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1779-2281 1.27e-30

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 130.65  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1779 LFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY 1858
Cdd:PRK06155   26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 PQDRIRYMLDDSQAGIVLMQRDVRKQL--AYEGVTVL-----LDDESSYHQD----------GSDLAPISDVS--HLAYV 1919
Cdd:PRK06155  106 RGPQLEHILRNSGARLLVVEAALLAALeaADPGDLPLpavwlLDAPASVSVPagwstaplppLDAPAPAAAVQpgDTAAI 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1920 IYTSGSTGRPKGVLIEHGgltNYIWW-----------AKEVYVkgekANFPLyssisFDLTVTSIFTP-LVTGNAIIVYD 1987
Cdd:PRK06155  186 LYTSGTTGPSKGVCCPHA---QFYWWgrnsaedleigADDVLY----TTLPL-----FHTNALNAFFQaLLAGATYVLEP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1988 GEDKTALLESIVRDpRVDIIKLTPAHLQVL--KEMNIADQT-AVRRMIVGGenlstrLARSIHEQFEGR--IEICNEYGP 2062
Cdd:PRK06155  254 RFSASGFWPAVRRH-GATVTYLLGAMVSILlsQPARESDRAhRVRVALGPG------VPAALHAAFRERfgVDLLDGYGS 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2063 TETVVGCmiyrYDAAKDRRESVpIGTAAANTSIYVLDENMKPAPIGVPGEIYISGA---GVARGYLNRPELTAEKFVDDP 2139
Cdd:PRK06155  327 TETNFVI----AVTHGSQRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLW 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2140 FEpgakmykTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SG 2217
Cdd:PRK06155  402 FH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVlrDG 474
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 2218 GQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAPDFELQ--DR--AEYKAPRTKA 2281
Cdd:PRK06155  475 TALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADtwDReaAGVQLPRSGT 542
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
4339-4818 1.55e-30

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 129.59  E-value: 1.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4339 EQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDK-GACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELP 4417
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4418 EKRRAFMLKDSGADVLLTCAGHAIPPLFEGEVLLLDDPLLYQGRTDNLNLSC------SENDLMYVIYTSGTTGQPKGVQ 4491
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIdnfvekNESASFIICYTSGTTGKPKGAV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4492 LEHKTM-----TNLLAYEqdhtqLRFDRVLQFAAMSFDVCYQEMFS--ALSSGGILFIIGneaKRDIRQLNDFVRTHGIQ 4564
Cdd:PRK06839  169 LTQENMfwnalNNTFAID-----LTMHDRSIVLLPLFHIGGIGLFAfpTLFAGGVIIVPR---KFEPTKALSMIEKHKVT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4565 TAF-LPTAFLKLLASEKhYFEPFAECVDHIIAAG----EQLIATRMLRDMLarhqvtLHNHYGPSETHVVTMYTVDPDTD 4639
Cdd:PRK06839  241 VVMgVPTIHQALINCSK-FETTNLQSVRWFYNGGapcpEELMREFIDRGFL------FGQGFGMTETSPTVFMLSEEDAR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4640 QELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpydSNQRMYkTGDLARYLPEGN 4719
Cdd:PRK06839  314 RKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI------QDGWLC-TGDLARVDEDGF 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4720 IEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQ--LKEKLAGQIPGYMI 4795
Cdd:PRK06839  387 VYIVGRKKEMIISGGENIYPLEVEQVINKLsdVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkdVIEHCRLFLAKYKI 466
                         490       500
                  ....*....|....*....|...
gi 166797876 4796 PSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK06839  467 PKEIVFLKELPKNATGKIQKAQL 489
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
561-842 2.17e-30

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 124.48  E-value: 2.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  561 TFHPVQSADEQITIGSPVANHQAYILgAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVP----GQKMYK 636
Cdd:COG3433     5 TPPPAPPTPDEPPPVIPPAIVQARAL-LLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPypaqPGRQAD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  637 TGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREE 716
Cdd:COG3433    84 DLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  717 LSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAAdENTRAENEYIAPRNT-----IEELLASIWQEVLG--AERIGIL 789
Cdd:COG3433   164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPAL-AAAEALLAAASPAPAletalTEEELRADVAELLGvdPEEIDPD 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876  790 DNFFDFGGDSIKSIQVSSRLYQAGYKVDMKHLFKHPSIAELSQFVAPVSRVAD 842
Cdd:COG3433   243 DNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
3309-3781 2.77e-30

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 127.45  E-value: 2.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3309 FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYcg 3388
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3389 klqddigfsgtcidlmeehfyhekdsslalsyQSSQLAYAIYTSGTTGKPKGTLIEHRQVI-HLIEGLSRQVYSAYDAEL 3467
Cdd:cd05972    79 --------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLgHIPTAAYWLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3468 NIAmlAPYYFDASVQQMYASLLSGHTLFI------VPKeivsdgaalcRYYR---QHSIDITDGTPAHLKLLIAAGDLQG 3538
Cdd:cd05972   127 NIA--DPGWAKGAWSSFFGPWLLGATVFVyegprfDAE----------RILElleRYGVTSFCGPPTAYRMLIKQDLSSY 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3539 V--TLQHLLIGGEALSKTTVNklkqLFGEHGAAPgITNVYGPTETCVDASLFniecssdawaRSQNYVP--IGKPLGRNR 3614
Cdd:cd05972   195 KfsHLRLVVSAGEPLNPEVIE----WWRAATGLP-IRDGYGQTETGLTVGNF----------PDMPVKPgsMGRPTPGYD 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3615 MYILDSKKRLQPKGVQGELYIAGDGVG--RGYLNLPELTDEKFVADpfvpedrMYRTGDLARLLPDGNIEYIGRIDHQVK 3692
Cdd:cd05972   260 VAIIDDDGRELPPGEEGDIAIKLPPPGlfLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIK 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3693 IQGFRIELGEIESVMLN-----------VPDIQEAAAAALKDADDEyylcGYFAADKTIQisELRKRMARHLPGYMIP-- 3759
Cdd:cd05972   333 SSGYRIGPFEVESALLEhpavaeaavvgSPDPVRGEVVKAFVVLTS----GYEPSEELAE--ELQGHVKKVLAPYKYPre 406
                         490       500
                  ....*....|....*....|..
gi 166797876 3760 AHFVqlDKMPLTPNGKLNRQLL 3781
Cdd:cd05972   407 IEFV--EELPKTISGKIRRVEL 426
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1785-2256 2.97e-30

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 129.67  E-value: 2.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVI------DKDRQLTYGELNKRANRLARTLRAKGVQTDqPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY 1858
Cdd:cd05931     4 AARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 P---QDRIRYMLDDSQAGIVL--------MQRDVRKQLAYEGVTVLLDDesSYHQDGSDLAPISDVSH--LAYVIYTSGS 1925
Cdd:cd05931    83 PgrhAERLAAILADAGPRVVLttaaalaaVRAFAASRPAAGTPRLLVVD--LLPDTSAADWPPPSPDPddIAYLQYTSGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1926 TGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANF----PLYSsisfDL-TVTSIFTPLVTGNaiivydgedkTALL---ES 1997
Cdd:cd05931   161 TGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVvswlPLYH----DMgLIGGLLTPLYSGG----------PSVLmspAA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1998 IVRDPR------------------------VDiiKLTPAHLQVLkemniaDQTAVRRMIVGGENLSTRLARSIHEQFEG- 2052
Cdd:cd05931   227 FLRRPLrwlrlisryratisaapnfaydlcVR--RVRDEDLEGL------DLSSWRVALNGAEPVRPATLRRFAEAFAPf 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2053 --RIE-ICNEYG-----------PTETVVGCMIYRYDAAKDRRESVPI-----------GTAAANTSIYVLDEN-MKPAP 2106
Cdd:cd05931   299 gfRPEaFRPSYGlaeatlfvsggPPGTGPVVLRVDRDALAGRAVAVAAddpaarelvscGRPLPDQEVRIVDPEtGRELP 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2107 IGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAkWLADGNIEYAGRIDEQVKIRGYRIELGEIEAA 2186
Cdd:cd05931   379 DGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEAT 457
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 2187 LLQE-EVIKE----AVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASY--MVPA--YFIELDEMPLTSNGKI 2256
Cdd:cd05931   458 AEEAhPALRPgcvaAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPAdvVLVRPGSIPRTSSGKI 536
PRK06145 PRK06145
acyl-CoA synthetase; Validated
4342-4818 3.20e-30

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 128.85  E-value: 3.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRR 4421
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4422 AFMLKDSGADVLLTCAGHAIPPLFEGEVLLLDDPLlyQGRTDNL---NLSCSE------NDLMYVIYTSGTTGQPKGVQL 4492
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAA--QADSRRLaqgGLEIPPqaavapTDLVRLMYTSGTTDRPKGVMH 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4493 EHKtmtNLLAYEQDHTQL----RFDRVLQFAAM----SFDVcyqEMFSALSSGGILFIIGN-EAKRDIRQLNDFVRTHGI 4563
Cdd:PRK06145  170 SYG---NLHWKSIDHVIAlgltASERLLVVGPLyhvgAFDL---PGIAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAW 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4564 QTAFLPTAFLKLLASEKHYFEPFAECvdhiIAAGEQLIATRmLRDML-----ARHQvtlhNHYGPSEthvvtmyTVDPDT 4638
Cdd:PRK06145  244 MAPVMLSRVLTVPDRDRFDLDSLAWC----IGGGEKTPESR-IRDFTrvftrARYI----DAYGLTE-------TCSGDT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4639 ----DQELQPI---GKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDL 4711
Cdd:PRK06145  308 lmeaGREIEKIgstGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-------GDWFRSGDV 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4712 ARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAAL--LKHVQEAVVLAKENTDGQSDLYA--YFTAEQSLSISQLKEKLA 4787
Cdd:PRK06145  381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIyeLPEVAEAAVIGVHDDRWGERITAvvVLNPGATLTLEALDRHCR 460
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876 4788 GQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK06145  461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
404-745 3.28e-30

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 124.83  E-value: 3.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 HLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKET 483
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  484 FAIqnaIKQERITHFSTSPrllkTMIEQMNREDFIH--VQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVsT 561
Cdd:cd17633    81 IRK---INQYNATVIYLVP----TMLQALARTLEPEskIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI-T 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  562 FHPVQSADEQITIGSPVANHQAYILGAHHqiqpiGIPGELYVGGAGVARGYLNRPELTEEKFvehlhvpgqkmYKTGDLA 641
Cdd:cd17633   153 YNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  642 RWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEpSLTAAQFREELSREL 721
Cdd:cd17633   217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKRFLKQKL 295
                         330       340
                  ....*....|....*....|....
gi 166797876  722 PNYMIPSRFIPLERIPLTSNGKID 745
Cdd:cd17633   296 SRYEIPKKIIFVDSLPYTSSGKIA 319
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
288-749 3.88e-30

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 128.90  E-value: 3.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  288 HLTYRELNEKASRLARTLRNCGVQPDTLVAILA---DRSLEMIvsiIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVL 364
Cdd:cd12119    25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELY---YAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  365 L------------------VQHHLKNSLAFDGPVIDLNDEASYHAdcsLLSPVAGHSHL-------AYVI-YTSGTTGKP 418
Cdd:cd12119   102 FvdrdflplleaiaprlptVEHVVVMTDDAAMPEPAGVGVLAYEE---LLAAESPEYDWpdfdentAAAIcYTSGTTGNP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  419 KGVMVEHGGIV-NSLQWKKA-FFKHSPADRVLVLYP--YV------FDAFI----LNFFGPLISGATLHLLpneenketf 484
Cdd:cd12119   179 KGVVYSHRSLVlHAMAALLTdGLGLSESDVVLPVVPmfHVnawglpYAAAMvgakLVLPGPYLDPASLAEL--------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  485 aiqnaIKQERITHFSTSPRLLKTMIEQM--NREDFIHVQHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTENSVVSTF 562
Cdd:cd12119   250 -----IEREGVTFAAGVPTVWQGLLDHLeaNGRDLSSLRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGMTETSPLGTV 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  563 ------HPVQSADEQITI----GSPVANHQAYILGAHHQIQPI--GIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvp 630
Cdd:cd12119   323 arppseHSNLSEDEQLALrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTED----- 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  631 GqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRGyriE-IGEVEaamfnLEN-------VREAAVVARED----------- 691
Cdd:cd12119   398 G--WLRTGDVATIDEDGYLTITDRSKDVIKSGG---EwISSVE-----LENaimahpaVAEAAVIGVPHpkwgerplavv 467
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  692 --ADGAKqlyayyvgepsLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd12119   468 vlKEGAT-----------VTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1347-1742 4.93e-30

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 126.99  E-value: 4.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1347 FDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGwKDQPLQIIFKTKKIGFQFNDLREmkESQKEAMIQKYAREDKMRGFD 1426
Cdd:cd20483    30 CHIKGKPDVNLLQKALSELVRRHEVLRTAYFEG-DDFGEQQVLDDPSFHLIVIDLSE--AADPEAALDQLVRNLRRQELD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1427 LEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQkQPEQSSITPYSQYIE-------WLGRQ 1499
Cdd:cd20483   107 IEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAG-RDLATVPPPPVQYIDftlwhnaLLQSP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1500 DAKEAAAYWDQYLEGYEEQTGL----------PKDHHAAedgryvpeKVTCDISSDLTSKMKRTAGKHHVTLNTLLQTAW 1569
Cdd:cd20483   186 LVQPLLDFWKEKLEGIPDASKLlpfakaerppVKDYERS--------TVEATLDKELLARMKRICAQHAVTPFMFLLAAF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1570 AVLLQKYNRSRDVVFGSVVSGRPAgiPNVETMIGLFINTIPVRFRCEAGTTFAELMKEAQERAVASQKFETHPL-YDIQA 1648
Cdd:cd20483   258 RAFLYRYTEDEDLTIGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPFdYIVDA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1649 ----RTTqkqdliTHLMIFE---NYpvdQYMESIGRQNGTSITISNVQMEE-QTNYDFNLTVI--PGDEMNISFEYNANV 1718
Cdd:cd20483   336 ldvpRST------SHFPIGQiavNY---QVHGKFPEYDTGDFKFTDYDHYDiPTACDIALEAEedPDGGLDLRLEFSTTL 406
                         410       420
                  ....*....|....*....|....
gi 166797876 1719 YERASIERVREHFMQILHQVVTDA 1742
Cdd:cd20483   407 YDSADMERFLDNFVTFLTSVIRDH 430
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1788-2261 5.02e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 129.13  E-value: 5.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:PRK07786   31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQ----------RDVRKQLAyegvTVLL------DDESSYH----QDGSDLAPIsDVSH--LAYVIYTSGS 1925
Cdd:PRK07786  111 SDCGAHVVVTEaalapvatavRDIVPLLS----TVVVaggssdDSVLGYEdllaEAGPAHAPV-DIPNdsPALIMYTSGT 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1926 TGRPKGVLIEHGGLTN------YIWWAKevyvKGEKANF---PLYSSISfdltVTSIFTPLVTGNAIIVY--DGEDKTAL 1994
Cdd:PRK07786  186 TGRPKGAVLTHANLTGqamtclRTNGAD----INSDVGFvgvPLFHIAG----IGSMLPGLLLGAPTVIYplGAFDPGQL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1995 LESIVRDpRVDIIKLTPAHLQVLkemnIADQTA------VRRMIVGGENLSTRLARSIHEQFEGrIEICNEYGPTE-TVV 2067
Cdd:PRK07786  258 LDVLEAE-KVTGIFLVPAQWQAV----CAEQQArprdlaLRVLSWGAAPASDTLLRQMAATFPE-AQILAAFGQTEmSPV 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2068 GCMIYRYDAAKdRRESV--PIGTAAANtsiyVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEpgak 2145
Cdd:PRK07786  332 TCMLLGEDAIR-KLGSVgkVIPTVAAR----VVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH---- 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2146 mykTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV---SGGQTTA 2222
Cdd:PRK07786  403 ---SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnDDAALTL 479
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876 2223 ARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK07786  480 EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1767-2259 5.04e-30

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 128.85  E-value: 5.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1767 TAAPFPQTPVHQLF---EEQSQRTPDQAA-VIDKDR-QLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGI 1841
Cdd:PRK05852    6 GAAPMASDFGPRIAdlvEVAATRLPEAPAlVVTADRiAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1842 LAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAYE-------GVTVLLDDESSY-----HQDGSdLAP 1909
Cdd:PRK05852   86 LAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPttrwwplTVNVGGDSGPSGgtlsvHLDAA-TEP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1910 ISDVS-------HLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEK----ANFPLYSSISFdltVTSIFTPLV 1978
Cdd:PRK05852  165 TPATStpeglrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRdatvAVMPLYHGHGL---IAALLATLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 TGNAIIV-YDGEDKTALLESIVRDPRVDIIKLTPAHLQVL----KEMNIADQTAVRRMIVG-GENLSTRLARSIHEQFEG 2052
Cdd:PRK05852  242 SGGAVLLpARGRFSAHTFWDDIKAVGATWYTAVPTIHQILleraATEPSGRKPAALRFIRScSAPLTAETAQALQTEFAA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2053 RIeICnEYGPTET---VVGCMIYRYDAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPE 2129
Cdd:PRK05852  322 PV-VC-AFGMTEAthqVTTTQIEGIGQTENPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2130 LTAEKFVDDPFepgakmyKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQ 2209
Cdd:PRK05852  400 ITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166797876 2210 LCAYYVSGG--QTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKK 2259
Cdd:PRK05852  473 VAAVIVPREsaPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
410-744 5.40e-30

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 124.70  E-value: 5.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  410 YTSGTTGKPKGVMVEHGGIVNSlqwkkAFF-----KHSPADRVLVLYPyVFDAF--ILNFFGPLISGATLhLLPneenKE 482
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNN-----GYFigerlGLTEQDRLCIPVP-LFHCFgsVLGVLACLTHGATM-VFP----SP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  483 TF---AIQNAIKQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENS 557
Cdd:cd05917    78 SFdplAVLEAIEKEKCTALHGVPTMFIAELEHpdFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  558 VVSTFH-PVQSADEQI-TIGSPVANHQAYILGAHHQIQP-IGIPGELYVGGAGVARGYLNRPELTEEKfvehlhVPGQKM 634
Cdd:cd05917   158 PVSTQTrTDDSIEKRVnTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGW 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  635 YKTGDLARWLPDGRIEYLGRIDHQVkIRG-YRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAA 711
Cdd:cd05917   232 LHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEgaELTEE 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 166797876  712 QFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05917   311 DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
4358-4818 7.59e-30

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 127.43  E-value: 7.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4358 LTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCA 4437
Cdd:cd05926    15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4438 GHAIPPL-----------------------FEGEVLLLDDPLLYQGRTDNLNLscsENDLMYVIYTSGTTGQPKGVQLEH 4494
Cdd:cd05926    95 GELGPASraasklglailelaldvgvliraPSAESLSNLLADKKNAKSEGVPL---PDDLALILHTSGTTGRPKGVPLTH 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4495 K----TMTNLLA-YEQDhtqlRFDRVLqfaamsfdvCYQEMF----------SALSSGG-ILFIIGNEAKR---DIRQLN 4555
Cdd:cd05926   172 RnlaaSATNITNtYKLT----PDDRTL---------VVMPLFhvhglvasllSTLAAGGsVVLPPRFSASTfwpDVRDYN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4556 dfvrthgiQTAF--LPTAFLKLLASEkhyfEPFAECVDH----IIAAGEQLIATrMLRDMLARHQVTLHNHYGPSET-HV 4628
Cdd:cd05926   239 --------ATWYtaVPTIHQILLNRP----EPNPESPPPklrfIRSCSASLPPA-VLEALEATFGAPVLEAYGMTEAaHQ 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4629 VTMYTVDPDTdQELQPIGKPiSNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKT 4708
Cdd:cd05926   306 MTSNPLPPGP-RKPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRT 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4709 GDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLA-KENTDGQsDLYAYFTAE--QSLSISQLK 4783
Cdd:cd05926   378 GDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHpaVLEAVAFGvPDEKYGE-EVAAAVVLRegASVTEEELR 456
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 166797876 4784 EKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05926   457 AFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
4357-4813 1.00e-29

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 125.96  E-value: 1.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4357 TLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLtc 4436
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4437 aghaIPPLFegevlllddpllyqGRTDNLNLScseNDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF-DRV 4515
Cdd:cd05903    79 ----VPERF--------------RQFDPAAMP---DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPgDVF 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4516 LQFAAMSFDVCYQEMFSA---LSSGGILFIIGNEAKrdIRQLndfVRTHGIQTAFLPTAFLKLLasekhyfepfaecVDH 4592
Cdd:cd05903   138 LVASPMAHQTGFVYGFTLpllLGAPVVLQDIWDPDK--ALAL---MREHGVTFMMGATPFLTDL-------------LNA 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4593 IIAAGEQLiatRMLRDM----------LARHQVTLHNH-----YGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFIL 4657
Cdd:cd05903   200 VEEAGEPL---SRLRTFvcggatvprsLARRAAELLGAkvcsaYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4658 NEAGTLQPVGIVGELCISGVSLARGYHNRESLTLEtfvphpyDSNQRMYKTGDLARYLPEGNIEYAGR-RDhqVKIR-GY 4735
Cdd:cd05903   277 DDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRsKD--IIIRgGE 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RVELGEVEAALLKH--VQEAVVLA--KENTDGQSDLYAYFTAEQSLSISQLKEKLAGQ-IPGYMIPSYFIQLEKLPLTGN 4810
Cdd:cd05903   348 NIPVLEVEDLLLGHpgVIEAAVVAlpDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPS 427

                  ...
gi 166797876 4811 GKV 4813
Cdd:cd05903   428 GKV 430
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
4358-4818 1.01e-29

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 126.08  E-value: 1.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4358 LTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTca 4437
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4438 ghaIPPLFEgevlllddpllyqgRTDnlnlscsENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQ 4517
Cdd:cd05969    79 ---TEELYE--------------RTD-------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4518 FAA-------MSFDvcyqeMFSALSSGGILFIigNEAKRDIRQLNDFVRTHGIQ---TAflPTAFLKLLASEKHYFEPF- 4586
Cdd:cd05969   135 CTAdpgwvtgTVYG-----IWAPWLNGVTNVV--YEGRFDAESWYGIIERVKVTvwyTA--PTAIRMLMKEGDELARKYd 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4587 AECVDHIIAAGEQLiATRMLRDMLARHQVTLHNHYGPSET--HVVTMYtvdPDTDQELQPIGKPISNTEIFILNEAGTLQ 4664
Cdd:cd05969   206 LSSLRFIHSVGEPL-NPEAIRWGMEVFGVPIHDTWWQTETgsIMIANY---PCMPIKPGSMGKPLPGVKAAVVDENGNEL 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4665 PVGIVGELCISG--VSLARGYHNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEV 4742
Cdd:cd05969   282 PPGTKGILALKPgwPSMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEV 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4743 EAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSIS-QLKEKLAG----QIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd05969   355 ESALMEHpaVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSdELKEEIINfvrqKLGAHVAPREIEFVDNLPKTRSGKIMR 434

                  ...
gi 166797876 4816 RAL 4818
Cdd:cd05969   435 RVL 437
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1788-2258 1.59e-29

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 126.64  E-value: 1.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLmqrdVRKQLAYEGVTVLLDDESSYHQDGSDLAPISdvshlayVIYTSGSTGRPKGVLIEHGG-----LTNY 1942
Cdd:cd12118    98 RHSEAKVLF----VDREFEYEDLLAEGDPDFEWIPPADEWDPIA-------LNYTSGTTGRPKGVVYHHRGaylnaLANI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1943 IWWAKE---VYVkgekANFPLY--SSISFDLTVTSIftplvtGNAIIVYDGEDKTALLESIvRDPRVDIIKLTPAHLQVL 2017
Cdd:cd12118   167 LEWEMKqhpVYL----WTLPMFhcNGWCFPWTVAAV------GGTNVCLRKVDAKAIYDLI-EKHKVTHFCGAPTVLNML 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2018 KEMNIADQ---TAVRRMIVGGenlSTRLARSIHEQFEGRIEICNEYGPTET---VVGCmIYRYD---------AAKDRRE 2082
Cdd:cd12118   236 ANAPPSDArplPHRVHVMTAG---APPPAAVLAKMEELGFDVTHVYGLTETygpATVC-AWKPEwdelpteerARLKARQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2083 SVPIGTAaanTSIYVLD-ENMKPapigVP------GEIYISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKW 2155
Cdd:cd12118   312 GVRYVGL---EEVDVLDpETMKP----VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAFRGG-------WFHSGDLAVI 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2156 LADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTL 2233
Cdd:cd12118   378 HPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVElkEGAKVTEEEIIAFCREHL 457
                         490       500
                  ....*....|....*....|....*
gi 166797876 2234 ASYMVPAYfIELDEMPLTSNGKINK 2258
Cdd:cd12118   458 AGFMVPKT-VVFGELPKTSTGKIQK 481
PRK07787 PRK07787
acyl-CoA synthetase; Validated
281-751 2.14e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 125.87  E-value: 2.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  281 AVKFKNDHLTYRELNEKASRLARTLRncGVQPdtlVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDAD 360
Cdd:PRK07787   18 AVRIGGRVLSRSDLAGAATAVAERVA--GARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  361 ADVLLVQhhlkNSLAFDG-PVIDLndeaSYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSL------- 432
Cdd:PRK07787   93 AQAWLGP----APDDPAGlPHVPV----RLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLdalaeaw 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  433 QWKkaffkhspADRVLV--LYPYVFDAFILNFFGPLISGATLHLL--PNEEnketfAIQNAIKQ------------ERIT 496
Cdd:PRK07787  165 QWT--------ADDVLVhgLPLFHVHGLVLGVLGPLRIGNRFVHTgrPTPE-----AYAQALSEggtlyfgvptvwSRIA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  497 HFSTSPRLLKTmieqmnredfihVQHVVVGGEQLETDTVEKLHSLQPRiRINNEYGPTENSV-VSTFhpvqsADEQI--- 572
Cdd:PRK07787  232 ADPEAARALRG------------ARLLVSGSAALPVPVFDRLAALTGH-RPVERYGMTETLItLSTR-----ADGERrpg 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  573 TIGSPVANHQAYILGAH-----HQIQPIGipgELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGDLARWLPDG 647
Cdd:PRK07787  294 WVGLPLAGVETRLVDEDggpvpHDGETVG---ELQVRGPTLFDGYLNRPDATAAAFTA------DGWFRTGDVAVVDPDG 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  648 RIEYLGR--IDhQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQFREELSRELPNYM 725
Cdd:PRK07787  365 MHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHK 443
                         490       500
                  ....*....|....*....|....*.
gi 166797876  726 IPSRFIPLERIPLTSNGKIDLKALPA 751
Cdd:PRK07787  444 RPREVRFVDALPRNAMGKVLKKQLLS 469
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
259-749 2.21e-29

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 126.92  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  259 FSGSRtVYQLFEEQAERTPENAAVKFKNDH--LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKA 336
Cdd:PRK05852   13 DFGPR-IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  337 GGAYVPLDPEYPKERLQYLLHDADADVLLV------QHHL-------------KNSLAFDG-PVIDLNDEASYHADCSll 396
Cdd:PRK05852   92 DLVVVPLDPALPIAEQRVRSQAAGARVVLIdadgphDRAEpttrwwpltvnvgGDSGPSGGtLSVHLDAATEPTPATS-- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  397 SPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYP-YVFDAFILNFFGPLISGATLhLL 475
Cdd:PRK05852  170 TPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPlYHGHGLIAALLATLASGGAV-LL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  476 PNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQH----VVVGGEQLETDTVEKLHS--LQPRIrinN 549
Cdd:PRK05852  249 PARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAalrfIRSCSAPLTAETAQALQTefAAPVV---C 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  550 EYGPTE--NSVVST--FHPVQSADEQITIGsPVANH---QAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEK 622
Cdd:PRK05852  326 AFGMTEatHQVTTTqiEGIGQTENPVVSTG-LVGRStgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAAN 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  623 FVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYY 702
Cdd:PRK05852  405 FTD-------GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVI 477
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876  703 VgePSLTAAQFREELS---RE-LPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK05852  478 V--PRESAPPTAEELVqfcRErLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2829-3143 2.39e-29

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 124.49  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLF-HSLLDEaSSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWND-TPLQIVYKTQTPQ-- 2904
Cdd:cd19532     3 PMSFGQSRFWFlQQYLED-PTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDgEPMQGVLASSPLRle 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2905 -IHFADLRDIEEHLreDAIAAYQredkakgFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSA 2983
Cdd:cd19532    82 hVQISDEAEVEEEF--ERLKNHV-------YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2984 lqegrepEPLSAVPYSdYIEWLDRQDQGAAKRYWSGYLEGYKGE-TTL--------LHKIAQ-HEQKEYAYANLICRFDH 3053
Cdd:cd19532   153 -------QPLLPPPLQ-YLDFAARQRQDYESGALDEDLAYWKSEfSTLpeplpllpFAKVKSrPPLTRYDTHTAERRLDA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3054 EQTKQLQQIANQHQVT-----LNTLiqtlwGVLLQKYSGSADVVFGSVVSGRPAEipDVEQMIGLFINTIPVRIRCDEDS 3128
Cdd:cd19532   225 ALAARIKEASRKLRVTpfhfyLAAL-----QVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQ 297
                         330
                  ....*....|....*
gi 166797876 3129 TFADTMQMVQQNALA 3143
Cdd:cd19532   298 TFADVLKETRDKAYA 312
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1775-2261 4.98e-29

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 128.89  E-value: 4.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1775 PVHQLFEEQSQRTPDQAAVIDK-DRQLTYGELNKRANRLARTLRaKGVQTDQPVAIITRNSIESVVGILAVLKSGgaYVP 1853
Cdd:PRK08633  616 PLAEAWIDTAKRNWSRLAVADStGGELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAG--KVP 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1854 IDPEYP--QDRIRYMLDdsQAGI--VLMQRDVRKQLAYEG--VTVLLDDESSYHQD------GSD---------LAPIS- 1911
Cdd:PRK08633  693 VNLNYTasEAALKSAIE--QAQIktVITSRKFLEKLKNKGfdLELPENVKVIYLEDlkakisKVDkltallaarLLPARl 770
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1912 ---------DVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEK----ANFPLYSSisFDLTVTsIFTPLV 1978
Cdd:PRK08633  771 lkrlygptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDdvilSSLPFFHS--FGLTVT-LWLPLL 847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 TG-NAIIVYDGEDKTALLESIVRDpRVDIIKLTPAHLQV---LKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEgrI 2054
Cdd:PRK08633  848 EGiKVVYHPDPTDALGIAKLVAKH-RATILLGTPTFLRLylrNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFG--I 924
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2055 EICNEYGPTET--VVGCMIYRYDAAKDRRE------SVpiGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYL 2125
Cdd:PRK08633  925 RILEGYGATETspVASVNLPDVLAADFKRQtgskegSV--GMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYL 1002
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2126 NRPELTAEKFVDdpfEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQeeVIKEA----VVTAR 2201
Cdd:PRK08633 1003 GDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK--ALGGEevvfAVTAV 1077
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2202 EDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK08633 1078 PDEKKGEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK07529 PRK07529
AMP-binding domain protein; Validated
263-758 5.66e-29

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 126.61  E-value: 5.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKF--------KNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEmivSIIAVW 334
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPE---THFALW 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  335 --KAGGAYVPLDPEYPKERLQYLLHDADADVLL-------------VQ------HHLKNSLAFDGP-------------- 379
Cdd:PRK07529  102 ggEAAGIANPINPLLEPEQIAELLRAAGAKVLVtlgpfpgtdiwqkVAevlaalPELRTVVEVDLArylpgpkrlavpli 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  380 -------VIDLNDE-ASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLY 451
Cdd:PRK07529  182 rrkaharILDFDAElARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  452 P--YVFdAFILNFFGPLISGATLHLLPNEENKETFAIQN---AIKQERITHFSTSPRLLKTMIEQ-MNREDFIHVQHVVV 525
Cdd:PRK07529  262 PlfHVN-ALLVTGLAPLARGAHVVLATPQGYRGPGVIANfwkIVERYRINFLSGVPTVYAALLQVpVDGHDISSLRYALC 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  526 GGEQLetdTVEKLHSLQPR--IRINNEYGPTENSVVSTFHPVqsaDEQITIGS---PVANHQAYIL-----GAHHQIQPI 595
Cdd:PRK07529  341 GAAPL---PVEVFRRFEAAtgVRIVEGYGLTEATCVSSVNPP---DGERRIGSvglRLPYQRVRVVilddaGRYLRDCAV 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  596 GIPGELYVGGAGVARGYLNrpeltEEKfvEHLHVPGQKMYKTGDLARWLPDGRIEYLGRidhqVK---IR-GYRIEIGEV 671
Cdd:PRK07529  415 DEVGVLCIAGPNVFSGYLE-----AAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGR----AKdliIRgGHNIDPAAI 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  672 EAAMFNLENVREAAVVAREDADgAKQLYAYYV---GEPSLTAAQFREELSRELPN-YMIPSRFIPLERIPLTSNGKI--- 744
Cdd:PRK07529  484 EEALLRHPAVALAAAVGRPDAH-AGELPVAYVqlkPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIfkp 562
                         570
                  ....*....|....
gi 166797876  745 DLKALPAADENTRA 758
Cdd:PRK07529  563 ALRRDAIRRVLRAA 576
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
270-755 7.55e-29

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 125.47  E-value: 7.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  270 EEQAERTPENAAVKFKN--------DHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYV 341
Cdd:cd05906    13 LELLLRAAERGPTKGITyidadgseEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  342 PLDP----EYPKERLQYLLH-----------------DADADVLLVQHHLKNSLAFdgpVIDLND-EASYHAdcsllsPV 399
Cdd:cd05906    93 PLTVpptyDEPNARLRKLRHiwqllgspvvltdaelvAEFAGLETLSGLPGIRVLS---IEELLDtAADHDL------PQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  400 AGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyvFD-AFILNFFG--PLISG------A 470
Cdd:cd05906   164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP--LDhVGGLVELHlrAVYLGcqqvhvP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  471 TLHLLPNEENketfaIQNAIKQERITHfSTSPRLLKTMIEQMNRE------DFIHVQHVVVGGEQLETDTVEKL------ 538
Cdd:cd05906   242 TEEILADPLR-----WLDLIDRYRVTI-TWAPNFAFALLNDLLEEiedgtwDLSSLRYLVNAGEAVVAKTIRRLlrllep 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  539 HSLQPRIrINNEYGPTENSVVSTF------HPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGY 612
Cdd:cd05906   316 YGLPPDA-IRPAFGMTETCSGVIYsrsfptYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  613 LNRPELTEEKFVEhlhvpgQKMYKTGDLArWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVRE---AAVVAR 689
Cdd:cd05906   395 YNNPEANAEAFTE------DGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVR 467
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  690 EDADGAKQLYAYYV------GEPSLTAAQFREELSREL---PNYMIPsrfIPLERIPLTSNGKIDLKALPAADEN 755
Cdd:cd05906   468 DPGAETEELAIFFVpeydlqDALSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKLKAAFEA 539
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
3292-3781 8.53e-29

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 124.30  E-value: 8.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3292 QAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSER 3371
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3372 IRYILNDSSISVLLYCGKLQDD--IGFSGTCIDLMEEhfyHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLiehrqvi 3449
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKliPGISVKFAELMNG---PKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3450 hlieglsrQVY-----SAYDAELNIAM------LA--PYYFDASVQQMYASLLSGHTLFIVPKeivSDGAALCRYYRQHS 3516
Cdd:PRK03640  161 --------QTYgnhwwSAVGSALNLGLteddcwLAavPIFHISGLSILMRSVIYGMRVVLVEK---FDAEKINKLLQTGG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3517 IDITDGTPAHLKLLIAagDLQGV----TLQHLLIGGEALSKTTVNKLKqlfgEHGaAPGITNvYGPTETCVDASLFNIEC 3592
Cdd:PRK03640  230 VTIISVVSTMLQRLLE--RLGEGtypsSFRCMLLGGGPAPKPLLEQCK----EKG-IPVYQS-YGMTETASQIVTLSPED 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3593 SSDAWARSqnyvpiGKPLGRNRMYILDSKKRLQPKgVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDL 3672
Cdd:PRK03640  302 ALTKLGSA------GKPLFPCELKIEKDGVVVPPF-EEGEIVVKGPNVTKGYLNREDATRETF-------QDGWFKTGDI 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3673 ARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARH 3752
Cdd:PRK03640  368 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEK 447
                         490       500
                  ....*....|....*....|....*....
gi 166797876 3753 LPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK03640  448 LAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
265-761 1.48e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 124.76  E-value: 1.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  265 VYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLD 344
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  345 PEYPKERLQYLLHDADADVLL-----------------VQH----HLKNSLAF---------------------DGPVID 382
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILcldlvfprvtnvqsatkIEHvivtRIADFLPFpknllypfvqkkqsnlvvkvsESETIH 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  383 LNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQWKKAFFKHSPADRVLVLYPYVFDAF--- 458
Cdd:PRK06710  186 LWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVVLGVLPFFHVYgmt 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  459 -ILNFfgPLISGATLHLLPNEENKETFaiqNAIKQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTV 535
Cdd:PRK06710  266 aVMNL--SIMQGYKMVLIPKFDMKMVF---EAIKKHKVTLFPGAPTIYIALLNSplLKEYDISSIRACISGSAPLPVEVQ 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  536 EKLHSLQPRiRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHH-QIQPIGIPGELYVGGAGVARGYLN 614
Cdd:PRK06710  341 EKFETVTGG-KLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIMKGYWN 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  615 RPELTEEKFVEH-LHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDAD 693
Cdd:PRK06710  420 KPEETAAVLQDGwLH--------TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPY 491
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876  694 GAKQLYAYYVGEPSLTAAQfrEELSR----ELPNYMIPSRFIPLERIPLTSNGKIDLKALpAADENTRAENE 761
Cdd:PRK06710  492 RGETVKAFVVLKEGTECSE--EELNQfarkYLAAYKVPKVYEFRDELPKTTVGKILRRVL-IEEEKRKNEDE 560
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
2829-3250 1.62e-28

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 122.37  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwNDTPLQIVYKTQTPQIHFA 2908
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEE-DGVPYQLILEEDEATPKLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2909 DLRDIEEHLrEDAIAAYQREDkakgFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSALQEGR 2988
Cdd:cd19538    82 IKEVDEEEL-ESEINEAVRYP----FDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2989 EPEpLSAVP--YSDYI----EWL--DRQDQGAAKR---YWSGYLEGYKGETTLLHKIAQHEQKEYAYANLICRFDHEQTK 3057
Cdd:cd19538   157 APE-LAPLPvqYADYAlwqqELLgdESDPDSLIARqlaYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3058 QLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEipDVEQMIGLFINTIPVRIRCDEDSTFADTMQMV 3137
Cdd:cd19538   236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDTSGNPSFRELLERV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3138 QQNALASQSYDTYPLYEIQAQTEQKQNLIDH----IM-IFENYP---IGQQAEETghhGTELNITN-------FHMQEHS 3202
Cdd:cd19538   314 KETNLEAYEHQDIPFERLVEALNPTRSRSRHplfqIMlALQNTPqpsLDLPGLEA---KLELRTVGsakfdltFELREQY 390
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 166797876 3203 HydlnvvviPGKQLAVH--FGFNENEYEKSEVERLRGHFEKLMQQVLRQP 3250
Cdd:cd19538   391 N--------DGTPNGIEgfIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
3310-3781 2.01e-28

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 121.68  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3310 TYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISvllycgk 3389
Cdd:cd05912     3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3390 lQDDIgfsgtcidlmeehfyhekdsslalsyqssqlAYAIYTSGTTGKPKGTLIEHRQviHLieglsrqvYSAYDAELNI 3469
Cdd:cd05912    76 -LDDI-------------------------------ATIMYTSGTTGKPKGVQQTFGN--HW--------WSAIGSALNL 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3470 AM------LA--PYYFDASVQQMYASLLSGHTLFIVPKeivSDGAALCRYYRQHSIDITDGTPAHLKLLIAA-GDLQGVT 3540
Cdd:cd05912   114 GLteddnwLCalPLFHISGLSILMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLEIlGEGYPNN 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3541 LQHLLIGGEALSKTTVNKLKQLfgehgAAPgITNVYGPTETCVDASLFNIEcssDAWARSQNyvpIGKPLGRNRMYIlds 3620
Cdd:cd05912   191 LRCILLGGGPAPKPLLEQCKEK-----GIP-VYQSYGMTETCSQIVTLSPE---DALNKIGS---AGKPLFPVELKI--- 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3621 KKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIEL 3700
Cdd:cd05912   256 EDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYP 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3701 GEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQL 3780
Cdd:cd05912   329 AEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408

                  .
gi 166797876 3781 L 3781
Cdd:cd05912   409 L 409
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1800-2258 2.25e-28

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 122.24  E-value: 2.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQR 1879
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1880 DVRKQLAyEGVTVLLddessyhqdgsdlapisdvshlayviYTSGSTGRPKGVLIEHGGLTNYIWWAKE-VYVKGEKA-- 1956
Cdd:cd05973    81 ANRHKLD-SDPFVMM--------------------------FTSGTTGLPKGVPVPLRALAAFGAYLRDaVDLRPEDSfw 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1957 -------NFPLYSSISfdltvtsifTPLVTGNAIIVYDGEDKTALLESIVRDPRVDIIKLTPAHLQVLKEMNIADQTAV- 2028
Cdd:cd05973   134 naadpgwAYGLYYAIT---------GPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPk 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2029 ---RRMIVGGENLS--------TRLARSIHEQFeGRIE----ICNEYGPTETV-VGCMiyrydaakdrresvpiGTAAAN 2092
Cdd:cd05973   205 grlRRVSSAGEPLTpevirwfdAALGVPIHDHY-GQTElgmvLANHHALEHPVhAGSA----------------GRAMPG 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2093 TSIYVLDENMKPAPIGVPGEIYISGAGVA----RGYLNRPELTaekfvddpfePGAKMYKTGDLAKWLADGNIEYAGRID 2168
Cdd:cd05973   268 WRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRAD 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2169 EQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED------VHGFKQLCAYYvSGGQTTAARLRKQLSQTLASYMVPAYF 2242
Cdd:cd05973   338 DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDpertevVKAFVVLRGGH-EGTPALADELQLHVKKRLSAHAYPRTI 416
                         490
                  ....*....|....*.
gi 166797876 2243 IELDEMPLTSNGKINK 2258
Cdd:cd05973   417 HFVDELPKTPSGKIQR 432
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1785-2261 2.56e-28

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 123.56  E-value: 2.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGgaYVPIDPEYPQDRI- 1863
Cdd:PRK10946   34 HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSe 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1864 ----------RYMLDDSQAGIVL---MQRDVRKQLAYEGVTVLLDDESS-------YHQDGSDLAPISDVSHLAYVIYTS 1923
Cdd:PRK10946  112 lnayasqiepALLIADRQHALFSdddFLNTLVAEHSSLRVVLLLNDDGEhslddaiNHPAEDFTATPSPADEVAFFQLSG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1924 GSTGRPKgvLI---------------EHGGLTnyiwwAKEVYVKGEKA--NFPLYSSISFdltvtSIFtpLVTGNAIIVY 1986
Cdd:PRK10946  192 GSTGTPK--LIprthndyyysvrrsvEICGFT-----PQTRYLCALPAahNYPMSSPGAL-----GVF--LAGGTVVLAP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1987 DGEDKTALleSIVRDPRVDIIKLTPAH----LQVLKEMNIADQTA-VRRMIVGGENLSTRLARSIHEQFEGRIEicNEYG 2061
Cdd:PRK10946  258 DPSATLCF--PLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQLAsLKLLQVGGARLSETLARRIPAELGCQLQ--QVFG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2062 PTETVVGcmiyrYDAAKDRRESV------PIgtaAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKF 2135
Cdd:PRK10946  334 MAEGLVN-----YTRLDDSDERIfttqgrPM---SPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2136 VDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQ-EEVIKEAVVTAREDVHGFKQlCAYY 2214
Cdd:PRK10946  406 DANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRhPAVIHAALVSMEDELMGEKS-CAFL 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 2215 VSGGQTTAARLRKQL-SQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK10946  479 VVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
268-927 3.28e-28

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 125.14  E-value: 3.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  268 LFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEY 347
Cdd:PRK06060   10 LAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  348 PKERLQYLLHDADADVLLVQHHLKNSLAFDGPV--IDLNDEASyHADCSLLSPVAGHSHlAYVIYTSGTTGKPKGVMVEH 425
Cdd:PRK06060   90 HRDDHALAARNTEPALVVTSDALRDRFQPSRVAeaAELMSEAA-RVAPGGYEPMGGDAL-AYATYTSGTTGPPKAAIHRH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  426 GGIVNSLQ--WKKAFfKHSPADRVLVLYPYVFDAFILN-FFGPLISGATLHLLPNEENKETFAIQNAIKQERITHfsTSP 502
Cdd:PRK06060  168 ADPLTFVDamCRKAL-RLTPEDTGLCSARMYFAYGLGNsVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLY--GVP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  503 RLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTEnsVVSTFHPvQSADEQI--TIGSPVAN 580
Cdd:PRK06060  245 NFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTE--VGQTFVS-NRVDEWRlgTLGRVLPP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  581 HQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPE--LTEEKFVEhlhvpgqkmykTGDLARWLPDGRIEYLGRIDHQ 658
Cdd:PRK06060  322 YEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDRVCIDSDGWVTYRCRADDT 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  659 VKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVgePSLTAA-------QFREELSRELPNYMIPSRFI 731
Cdd:PRK06060  391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATidgsvmrDLHRGLLNRLSAFKVPHRFA 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  732 PLERIPLTSNGKIDLKALPAAD------ENTRAENEYIAPRN-------------------TIEELLASIWQE------- 779
Cdd:PRK06060  469 VVDRLPRTPNGKLVRGALRKQSptkpiwELSLTEPGSGVRAQrddlsasnmtiaggndggaTLRERLVALRQErqrlvvd 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  780 --------VLGAERIGILDN---FFDFGGDSIKSIQVSSRLYQA-GYKVDMKHLFKHPSIAELSQFV-APVS----RVAD 842
Cdd:PRK06060  549 avcaeaakMLGEPDPWSVDQdlaFSELGFDSQMTVTLCKRLAAVtGLRLPETVGWDYGSISGLAQYLeAELAgghgRLKS 628
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  843 QGEVNGGTK-LTPIQhwffeqkmphaHHYNQAVMLYSAEGFKEGPlrrtmeRIASHHDALRMIFEKTPDGYAPRI-TGTD 920
Cdd:PRK06060  629 AGPVNSGATgLWAIE-----------EQLNKVEELVAVIADGEKQ------RVADRLRALLGTIAGSEAGLGKLIqAAST 691

                  ....*..
gi 166797876  921 ESELFHL 927
Cdd:PRK06060  692 PDEIFQL 698
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
3910-4298 3.64e-28

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 121.26  E-value: 3.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3910 NMLGLMtveGKLDRDKLQQAFRTLILRHESLRTGFKMAD-GEPVQYVLDHAAfeAEW----YQGEEDD--ADLYIRQFIR 3982
Cdd:cd19547    28 NVLELV---GGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLA--PPWalldWSGEDPDrrAELLERLLAD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3983 P----FHLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYEG------ETLPPLRiQYKDYAVWQtg 4052
Cdd:cd19547   103 DraagLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEElahgrePQLSPCR-PYRDYVRWI-- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4053 EARLQQIQKQEAYWLELYSGDVPVLHLPAdyirPSARDFAGATMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLS 4132
Cdd:cd19547   180 RARTAQSEESERFWREYLRDLTPSPFSTA----PADREGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4133 KYSGQEDIIVGSPIAGRPH--ADLEPIIGMFVNTLAMRNYPEKGKTFSQYLSEVKENALKAYEHQDYPFEVLIDQLNIAR 4210
Cdd:cd19547   256 LQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQIKSWASGER 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4211 dLSRNPLFDTMFVLQNTEQEQLEINDVTFK----------PYPNGhtmakfdLTLTAVEEgagIQFTLEYLTALFKPETI 4280
Cdd:cd19547   336 -LSGGRVFDNLVAFENYPEDNLPGDDLSIQiidlhaqektEYPIG-------LIVLPLQK---LAFHFNYDTTHFTRAQV 404
                         410
                  ....*....|....*...
gi 166797876 4281 ERMMGHFEQLVDSIIKQP 4298
Cdd:cd19547   405 DRFIEVFRLLTEQLCRRP 422
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
288-744 4.95e-28

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 121.70  E-value: 4.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  288 HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ 367
Cdd:cd17640     5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  368 HHLKNslafdgpvidlndeasyhadcsllspvaghshLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRV 447
Cdd:cd17640    85 NDSDD--------------------------------LATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRF 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  448 LVLYP--YVFD-AFILNFFGPLISGA--TLHLLPNEenketfaiqnaIKQERITHFSTSPRLLKTM----IEQMNREDFI 518
Cdd:cd17640   133 LSILPiwHSYErSAEYFIFACGCSQAytSIRTLKDD-----------LKRVKPHYIVSVPRLWESLysgiQKQVSKSSPI 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  519 H------------VQHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTENSVVSTfhpVQSADEQI--TIGSPVANHQAY 584
Cdd:cd17640   202 KqflflfflsggiFKFGISGGGALPPHVDTFFEAIG--IEVLNGYGLTETSPVVS---ARRLKCNVrgSVGRPLPGTEIK 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  585 ILGAH-HQIQPIGIPGELYVGGAGVARGYLNRPELTEEkfvehlhVPGQK-MYKTGDLARWLPDGRIEYLGRI-DHQVKI 661
Cdd:cd17640   277 IVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK-------VLDSDgWFNTGDLGWLTCGGELVLTGRAkDTIVLS 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVVAREDadgaKQLYAYYVGepsltaaqFREELSRELPNYMIpsrFIPLERIPLTSN 741
Cdd:cd17640   350 NGENVEPQPIEEALMRSPFIEQIMVVGQDQ----KRLGALIVP--------NFEELEKWAKESGV---KLANDRSQLLAS 414

                  ...
gi 166797876  742 GKI 744
Cdd:cd17640   415 KKV 417
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
3297-3781 5.37e-28

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 122.09  E-value: 5.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYCGKLQDDIGFSGTCID-------------------LMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGK 3437
Cdd:cd05959    98 EDSRARVVVVSGELAPVLAAALTKSEhtlvvlivsggagpeagalLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3438 PKGTLIEHRQVIHLIEGLSRQVysAYDAELNIAMLAPYYFDAS--VQQMYASLLSGHTLFIVPKEIVSDgaALCRYYRQH 3515
Cdd:cd05959   178 PKGVVHLHADIYWTAELYARNV--LGIREDDVCFSAAKLFFAYglGNSLTFPLSVGATTVLMPERPTPA--AVFKRIRRY 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3516 SIDITDGTPAHLKLLIAAGDLQ---GVTLQHLLIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTEtcvdasLFNIEC 3592
Cdd:cd05959   254 RPTVFFGVPTLYAAMLAAPNLPsrdLSSLRLCVSAGEALPAEVGERWKARFGLD-----ILDGIGSTE------MLHIFL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3593 SSdaWARSQNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADpfvpedrMYRTGDL 3672
Cdd:cd05959   323 SN--RPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-------WTRTGDK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3673 ARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYF-----AADKTIQISELRK 3747
Cdd:cd05959   394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrpgYEDSEALEEELKE 473
                         490       500       510
                  ....*....|....*....|....*....|....
gi 166797876 3748 RMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05959   474 FVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
2829-3143 6.90e-28

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 120.61  E-value: 6.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRF-YSGwnDTPLQivyktqtpQIHF 2907
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFpEDD--GGPYQ--------VVLP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2908 ADLRDIE---EHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSAL 2984
Cdd:cd19540    73 AAEARPDltvVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAAR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2985 QEGREP--EPLsAVPYSDYI----EWLDRQDQG---AAK--RYWSGYLEG------------------YKGETTLLhkia 3035
Cdd:cd19540   153 RAGRAPdwAPL-PVQYADYAlwqrELLGDEDDPdslAARqlAYWRETLAGlpeelelptdrprpavasYRGGTVEF---- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3036 qheqkeyayanlicRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEipDVEQMIGLFI 3115
Cdd:cd19540   228 --------------TIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFV 291
                         330       340
                  ....*....|....*....|....*...
gi 166797876 3116 NTIPVRIRCDEDSTFADTMQMVQQNALA 3143
Cdd:cd19540   292 NTLVLRTDVSGDPTFAELLARVRETDLA 319
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1799-2235 7.69e-28

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 120.93  E-value: 7.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1799 QLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSqagivlmq 1878
Cdd:cd17640     5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHS-------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1879 rdvrkqlayEGVTVLLDDessyhqDGSDLAPIsdvshlayvIYTSGSTGRPKGVLIEHGGLTNYIWWAKEvYVKGEKAN- 1957
Cdd:cd17640    77 ---------ESVALVVEN------DSDDLATI---------IYTSGTTGNPKGVMLTHANLLHQIRSLSD-IVPPQPGDr 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1958 ----FPLYSS-------ISFDLTVTSIFTplvtgnAIIVYDGEDKTALLESIVRDPRVDIIKLTPAHLQVlkemniADQT 2026
Cdd:cd17640   132 flsiLPIWHSyersaeyFIFACGCSQAYT------SIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQV------SKSS 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2027 AVRRMIVGGENLSTR----------LARSIHEQFEG-RIEICNEYGPTET--VVGCmiyrydaakdRRESVPI-GTAAA- 2091
Cdd:cd17640   200 PIKQFLFLFFLSGGIfkfgisgggaLPPHVDTFFEAiGIEVLNGYGLTETspVVSA----------RRLKCNVrGSVGRp 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2092 --NTSIYVLDENMK-PAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRI- 2167
Cdd:cd17640   270 lpGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAk 343
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 2168 DEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED-------VHGFKQLCAYYVSGGQttaaRLRKQLSQTLAS 2235
Cdd:cd17640   344 DTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQkrlgaliVPNFEELEKWAKESGV----KLANDRSQLLAS 414
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1776-2263 9.04e-28

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 122.98  E-value: 9.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVI-----DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGA 1850
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRwegedGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1851 YVPIDPEYPQDRIRYMLDDSQAG-------------IVLMQRDVRKQLAY----EGVTVL----------LDDESSYHQD 1903
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKalitadgftrrgrEVNLKEEADKACAQcptvEKVVVVrhlgndftpaKGRDLSYDEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1904 ---GSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTnyiwwakevyvkgEKANFPLYssISFDL----TVT----- 1971
Cdd:cd05968   223 ketAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFP-------------LKAAQDMY--FQFDLkpgdLLTwftdl 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1972 -------SIFTPLVTGNAIIVYDG---EDKTALLESIVRDPRVDIIKLTPAHLQVLK-----EMNIADQTAVRRMIVGGE 2036
Cdd:cd05968   288 gwmmgpwLIFGGLILGATMVLYDGapdHPKADRLWRMVEDHEITHLGLSPTLIRALKprgdaPVNAHDLSSLRVLGSTGE 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2037 NLSTRLARSIHEQ-FEGRIEICNEYGPTET---VVGCMIYRYDAAKDRRESVPiGTAAAntsiyVLDENMKPAPIGVpGE 2112
Cdd:cd05968   368 PWNPEPWNWLFETvGKGRNPIINYSGGTEIsggILGNVLIKPIKPSSFNGPVP-GMKAD-----VLDESGKPARPEV-GE 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2113 IYISGA--GVARGYLNRPEltaeKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALL-Q 2189
Cdd:cd05968   441 LVLLAPwpGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNaH 516
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 2190 EEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYM----VPAYFIELDEMPLTSNGKINKKGLPA 2263
Cdd:cd05968   517 PAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRA 594
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
290-749 9.08e-28

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 120.28  E-value: 9.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  290 TYRELNEKASRLARTLRNCGV-QPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:cd05958    12 TYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALCAH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNSlafdgpvidlndeasyhADCSLLSpvaghshlayviYTSGTTGKPKGVMVEHGGIVNSLQ-WKKAFFKHSPADRV 447
Cdd:cd05958    92 ALTAS-----------------DDICILA------------FTSGTTGAPKATMHFHRDPLASADrYAVNVLRLREDDRF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  448 LVLYPYVFD-AFILNFFGPLISGATLHLLPNEENKETFaiqNAIKQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVV 524
Cdd:cd05958   143 VGSPPLAFTfGLGGVLLFPFGVGASGVLLEEATPDLLL---SAIARYKPTVLFTAPTAYRAMLAHpdAAGPDLSSLRKCV 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  525 VGGEQLETDTVEKLHSLQPrIRINNEYGPTENsvvstFHPVQSADEQI----TIGSPVANHQAYILGAHHQIQPIGIPGE 600
Cdd:cd05958   220 SAGEALPAALHRAWKEATG-IPIIDGIGSTEM-----FHIFISARPGDarpgATGKPVPGYEAKVVDDEGNPVPDGTIGR 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  601 LYVGGAGVARGylnrpeLTEEKfvEHLHVPGQKMYkTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLEN 680
Cdd:cd05958   294 LAVRGPTGCRY------LADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPA 364
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876  681 VREAAVVAREDADGAKQLYAYYVGEPSLT-----AAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05958   365 VAECAVVGHPDESRGVVVKAFVVLRPGVIpgpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
3309-3783 9.34e-28

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 120.30  E-value: 9.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3309 FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYCG 3388
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3389 KLQDDIgfsgtcidlmeehfyHEKDSSLALsyqssqlayaiYTSGTTGKPKGTLIEHRQVI-HLIEGlsRQVYSAYDAEL 3467
Cdd:cd05969    81 ELYERT---------------DPEDPTLLH-----------YTSGTTGTPKGVLHVHDAMIfYYFTG--KYVLDLHPDDI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3468 NIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDgaalcRYY---RQHSIDITDGTPAHLKLLIAAG-------DLQ 3537
Cdd:cd05969   133 YWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAE-----SWYgiiERVKVTVWYTAPTAIRMLMKEGdelarkyDLS 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3538 gvTLQHLLIGGEALSKTTVNKLKQLFGehgaAPgITNVYGPTETCVDAsLFNIECSsDAWARSqnyvpIGKPLGRNRMYI 3617
Cdd:cd05969   208 --SLRFIHSVGEPLNPEAIRWGMEVFG----VP-IHDTWWQTETGSIM-IANYPCM-PIKPGS-----MGKPLPGVKAAV 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3618 LDSKKRLQPKGVQGELYIAGD--GVGRGYLNLPELTDEKFVadpfvpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQG 3695
Cdd:cd05969   274 VDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSG 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3696 FRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS-----ELRKRMARHLPGYMIP--AHFVqlDKM 3768
Cdd:cd05969   347 HRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSdelkeEIINFVRQKLGAHVAPreIEFV--DNL 424
                         490
                  ....*....|....*
gi 166797876 3769 PLTPNGKLNRQLLPA 3783
Cdd:cd05969   425 PKTRSGKIMRRVLKA 439
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
3293-3687 1.21e-27

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 121.58  E-value: 1.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVF------EGKQFTYEELNRRANQLARTLQAKGVQADqLVGIMTERSLEMVVGILGVLKAGGAYLPIDPD 3366
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3367 SPS---ERIRYILNDSSISVLLYCGKLQDDI-----------GFSGTCIDLMEEHfyhEKDSSLALSYQSSQLAYAIYTS 3432
Cdd:cd05931    82 TPGrhaERLAAILADAGPRVVLTTAAALAAVrafaasrpaagTPRLLVVDLLPDT---SAADWPPPSPDPDDIAYLQYTS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3433 GTTGKPKGTLIEHRQVIHLIEGLSRqvysAYDAELNIAMLA--PYYFDasvqqM------YASLLSGHTL-FIVPKEIVS 3503
Cdd:cd05931   159 GSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSwlPLYHD-----MgligglLTPLYSGGPSvLMSPAAFLR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3504 DGA----ALCRYYRQHS--------IDITDGTPAHLklliAAGDLQgvTLQHLLIGGEALSKTTVNKLKQLFGEHGAAPG 3571
Cdd:cd05931   230 RPLrwlrLISRYRATISaapnfaydLCVRRVRDEDL----EGLDLS--SWRVALNGAEPVRPATLRRFAEAFAPFGFRPE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3572 -ITNVYG----------------PTETCVDASLFNIECSSDAwARSQNYVPI---GKPLGRNRMYILD--SKKRLQPKGV 3629
Cdd:cd05931   304 aFRPSYGlaeatlfvsggppgtgPVVLRVDRDALAGRAVAVA-ADDPAARELvscGRPLPDQEVRIVDpeTGRELPDGEV 382
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 3630 qGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLpDGNIeYI-GRI 3687
Cdd:cd05931   383 -GEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGFLH-DGEL-YItGRL 438
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
4923-5335 1.42e-27

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 118.94  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4923 VYPVSSVQK-MVYLTTQIIGgelPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRT-VVEMVREEAVQVIKSQVEFSM 5000
Cdd:cd19545     1 IYPCTPLQEgLMALTARQPG---AYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTrIVQSDSGGLLQVVVKESPISW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5001 ErYEATADEVEECFRAfvRPFDLSQaPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGKELAPlRIQY 5080
Cdd:cd19545    78 T-ESTSLDEYLEEDRA--APMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5081 KDFTewKHQKEQreRIKSQEEYW---L-GVFHEELPSFELPKDFARPPVRSfdgkRHNFTLDKTVTQGIkqleelTGSTa 5156
Cdd:cd19545   153 SRFV--KYLRQL--DDEAAAEFWrsyLaGLDPAVFPPLPSSRYQPRPDATL----EHSISLPSSASSGV------TLAT- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5157 ymILFSAYSILLAKYSGQDDIVVGTPIAGR--PHADLEPIIGMFVNTLAIRTAPMAEKT---FLDYITETKETMLKaFEH 5231
Cdd:cd19545   218 --VLRAAWALVLSRYTGSDDVVFGVTLSGRnaPVPGIEQIVGPTIATVPLRVRIDPEQSvedFLQTVQKDLLDMIP-FEH 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5232 qeypfeelvekLGVKR------DLSRNPLFDTMFVLQ-NTEQTDieVDSLAVRPYEQTETAAKFD---LQLNFLIDQD-- 5299
Cdd:cd19545   295 -----------TGLQNirrlgpDARAACNFQTLLVVQpALPSST--SESLELGIEEESEDLEDFSsygLTLECQLSGSgl 361
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 166797876 5300 EIQGSFDycTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19545   362 RVRARYD--SSVISEEQVERLLDQFEHVLQQLASAP 395
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1785-2280 1.66e-27

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 120.92  E-value: 1.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIR 1864
Cdd:PRK07470   18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1865 YMLDDSQAGIVLMQRD--------------VRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSH--LAYVIYTSGSTGR 1928
Cdd:PRK07470   98 YLAEASGARAMICHADfpehaaavraaspdLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHddPCWFFFTSGTTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1929 PKGVLIEHGGL----TNYIwwakevyvkgekAN-FPLYSSISFDLTVTsiftPLVTGNAI----IVYDGEdKTALLES-- 1997
Cdd:PRK07470  178 PKAAVLTHGQMafviTNHL------------ADlMPGTTEQDASLVVA----PLSHGAGIhqlcQVARGA-ATVLLPSer 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1998 --------IVRDPRVDIIKLTPAHLQVLKE---MNIADQTAVRRMIVGGENLsTRLARSIHEQFEGRIeICNEYGPTEtV 2066
Cdd:PRK07470  241 fdpaevwaLVERHRVTNLFTVPTILKMLVEhpaVDRYDHSSLRYVIYAGAPM-YRADQKRALAKLGKV-LVQYFGLGE-V 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2067 VGCMIYRYDAAKDRrESVP---IGTAA-ANTSIYV--LDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPF 2140
Cdd:PRK07470  318 TGNITVLPPALHDA-EDGPdarIGTCGfERTGMEVqiQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2141 epgakmyKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKE----------------AVVTAREdv 2204
Cdd:PRK07470  397 -------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEvavlgvpdpvwgevgvAVCVARD-- 467
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 2205 hgfkqlcayyvsGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPApdfELQDRAEYKAPRTK 2280
Cdd:PRK07470  468 ------------GAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE---ELEERGLLDLERAP 528
PRK07788 PRK07788
acyl-CoA synthetase; Validated
255-753 1.81e-27

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 121.19  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  255 TVRDFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVW 334
Cdd:PRK07788   41 LAADIRRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  335 KAGGAYVPLDPEYPK---------ERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHS-- 403
Cdd:PRK07788  121 KVGARIILLNTGFSGpqlaevaarEGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSta 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 -------HLAYVIYTSGTTGKPKGVMVEHggiVNSLQWKKAFFKHSP--ADRVLVLYPYVFDA-----FILNFFgpliSG 469
Cdd:PRK07788  201 plpkppkPGGIVILTSGTTGTPKGAPRPE---PSPLAPLAGLLSRVPfrAGETTLLPAPMFHAtgwahLTLAMA----LG 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  470 ATLHLLPNEENKETFAiqnAIKQERITHFSTSPRLLKTMI----EQMNREDFIHVQHVVVGGEQLETDTVEKLH-SLQPr 544
Cdd:PRK07788  274 STVVLRRRFDPEATLE---DIAKHKATALVVVPVMLSRILdlgpEVLAKYDTSSLKIIFVSGSALSPELATRALeAFGP- 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  545 iRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNrpelteekfv 624
Cdd:PRK07788  350 -VLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD---------- 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  625 ehlhvPGQK-----MYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLY 699
Cdd:PRK07788  419 -----GRDKqiidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLR 493
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  700 AYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAAD 753
Cdd:PRK07788  494 AFVVKAPgaALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
4333-4818 2.09e-27

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 120.31  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMF--GNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFL 4410
Cdd:cd05923     2 TVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4411 PIDPEL-PEKRRAFMLKDSGADVLLTCAGHAIPPLFEGEVlllddPLLYQGRTDNLNLSCSENDLM-----------YVI 4478
Cdd:cd05923    82 LINPRLkAAELAELIERGEMTAAVIAVDAQVMDAIFQSGV-----RVLALSDLVGLGEPESAGPLIedpprepeqpaFVF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4479 YTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF---DRVLQFAAMSFDVCYQEMF-SALSSGGILFIIGNEAKRDIRQL 4554
Cdd:cd05923   157 YTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHgrhNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEEFDPADALKL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4555 ndfVRTHGIQTAFL-PTAFLKLLASEKhyFEPF-AECVDHIIAAGEQLiaTRMLRDMLARH-QVTLHNHYGPSETHvvtM 4631
Cdd:cd05923   237 ---IEQERVTSLFAtPTHLDALAAAAE--FAGLkLSSLRHVTFAGATM--PDAVLERVNQHlPGEKVNIYGTTEAM---N 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4632 YTVDPDTDQElqPIGKPISNTEIFILNEAGTLQ---PVGIVGELCISGVSLA--RGYHNRESLTLETFVphpydsnQRMY 4706
Cdd:cd05923   307 SLYMRDARTG--TEMRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DGWY 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4707 KTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTD-GQSDLYAYFTAEQSLSISQLK 4783
Cdd:cd05923   378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHpgVTEVVVIGVADERwGQSVTACVVPREGTLSADELD 457
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 166797876 4784 EK-LAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05923   458 QFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK09088 PRK09088
acyl-CoA synthetase; Validated
272-753 2.19e-27

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 119.91  E-value: 2.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  272 QAERTPEN-AAVKFKND-HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPK 349
Cdd:PRK09088    4 HARLQPQRlAAVDLALGrRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  350 ERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHAdcSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHG--- 426
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALE--PADTPSIPPERVSLILFTSGTSGQPKGVMLSERnlq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  427 ------GIVNSLQWKKAFFKHSPADRVLVLypyvfdafILNFFGPLISGATLHLLPNEENKETFAiQNAIKQERITHFST 500
Cdd:PRK09088  162 qtahnfGVLGRVDAHSSFLCDAPMFHIIGL--------ITSVRPVLAVGGSILVSNGFEPKRTLG-RLGDPALGITHYFC 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  501 SPRLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTVekLHSLQPRIRINNEYGPTENSVVSTFhPVQSADEQITIGS-- 576
Cdd:PRK09088  233 VPQMAQAFRAQpgFDAAALRHLTALFTGGAPHAAEDI--LGWLDDGIPMVDGFGMSEAGTVFGM-SVDCDVIRAKAGAag 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  577 -PVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVehlhvpGQKMYKTGDLARWLPDGRIEYLGRI 655
Cdd:PRK09088  310 iPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGDIARRDADGFFWVVDRK 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  656 DHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPL 733
Cdd:PRK09088  384 KDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADgaPLDLERIRSHLSTRLAKYKVPKHLRLV 463
                         490       500
                  ....*....|....*....|...
gi 166797876  734 ERIPLTSNGKI---DLKALPAAD 753
Cdd:PRK09088  464 DALPRTASGKLqkaRLRDALAAG 486
PRK06164 PRK06164
acyl-CoA synthetase; Validated
260-759 4.94e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 119.85  E-value: 4.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  260 SGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGA 339
Cdd:PRK06164    7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  340 YVPLDPEYPKERLQYLLHDADADVLLVQHHLKnSLAFDG-----------------PVIDLNDEASYHADCSLLSPVAGH 402
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGFK-GIDFAAilaavppdalpplraiaVVDDAADATPAPAPGARVQLFALP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  403 ---------------SHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyVFDAFILN-FFGPL 466
Cdd:PRK06164  166 dpappaaageraadpDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALP-FCGVFGFStLLGAL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  467 ISGATLHLLPNEENKETFAiqnAIKQERITHFSTSPRLLKTMIEQM-NREDFIHVQHVVVGgeqletDTVEKLHSLQPRI 545
Cdd:PRK06164  245 AGGAPLVCEPVFDAARTAR---ALRRHRVTHTFGNDEMLRRILDTAgERADFPSARLFGFA------SFAPALGELAALA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  546 R-----INNEYGPTENSVVSTFHPVqSADEQITI--GSPVANHQAYILGAHHQ---IQPIGIPGELYVGGAGVARGYLNR 615
Cdd:PRK06164  316 RargvpLTGLYGSSEVQALVALQPA-TDPVSVRIegGGRPASPEARVRARDPQdgaLLPDGESGEIEIRAPSLMRGYLDN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  616 PELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREdADGA 695
Cdd:PRK06164  395 PDATARALTD------DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-RDGK 467
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  696 KQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLT--SNG-KIDLKALPA-ADENTRAE 759
Cdd:PRK06164  468 TVPVAFVIPTDgaSPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLREmAQARLAAE 537
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
3310-3781 4.97e-27

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 117.97  E-value: 4.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3310 TYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYCGK 3389
Cdd:cd05935     3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3390 LQDdigfsgtcidlmeehfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQVIhlIEGLSRQVYSAYDAELNI 3469
Cdd:cd05935    83 LDD--------------------------------LALIPYTSGTTGLPKGCMHTHFSAA--ANALQSAVWTGLTPSDVI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3470 AMLAPYYFDAS-VQQMYASLLSGHTLFIVPKeivSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLI-- 3546
Cdd:cd05935   129 LACLPLFHVTGfVGSLNTAVYVGGTYVLMAR---WDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVlt 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3547 -GGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETCVDASLfniecSSDAWARSQNyvpIGKPLGRNRMYILD-SKKRL 3624
Cdd:cd05935   206 gGGAPMPPAVAEKLLKLTGLR-----FVEGYGLTETMSQTHT-----NPPLRPKLQC---LGIP*FGVDARVIDiETGRE 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3625 QPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIE 3704
Cdd:cd05935   273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK---GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3705 SVM-----------LNVPDIQEAAAAALKDADDEYYLcGYFAADKTIQISelRKRMArhlpGYMIPAHFVQLDKMPLTPN 3773
Cdd:cd05935   350 AKLykhpai*evcvISVPDERVGEEVKAFIVLRPEYR-GKVTEEDIIEWA--REQMA----AYKYPREVEFVDELPRSAS 422

                  ....*...
gi 166797876 3774 GKLNRQLL 3781
Cdd:cd05935   423 GKILWRLL 430
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1800-2261 5.31e-27

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 118.97  E-value: 5.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRaKGVQTDQPVAIITRNSIESVVGILAVLKSGgaYVPIDPEYPQ--DRIRYMLD--------- 1868
Cdd:cd05909     8 LTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKlagiktvlt 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1869 ----------------DSQAGIVLMQrDVRKQLAY-EGVTVLLD----DESSYHQDGSDLAPISDVshlAYVIYTSGSTG 1927
Cdd:cd05909    85 skqfieklklhhlfdvEYDARIVYLE-DLRAKISKaDKCKAFLAgkfpPKWLLRIFGVAPVQPDDP---AVILFTSGSEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1928 RPKGVLIEHGGLTNYIWWAKEVYVKGEKANF----PLYSSisFDLTVTsIFTPLVTGNAIIVYDGEDKTALLESIVRDPR 2003
Cdd:cd05909   161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVfgalPFFHS--FGLTGC-LWLPLLSGIKVVFHPNPLDYKKIPELIYDKK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2004 VDIIKLTPAHL-QVLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIeicNE-YGPTET--VVGCMIYRYDAakd 2079
Cdd:cd05909   238 ATILLGTPTFLrGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRI---LEgYGTTECspVISVNTPQSPN--- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2080 RRESVpiGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDdpfepgaKMYKTGDLAKWLAD 2158
Cdd:cd05909   312 KEGTV--GRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD-------GWYDTGDIGKIDGE 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2159 GNIEYAGRIDEQVKIRGYRIELGEIEAALL-----QEEVIKEAVVTARedvHGFK-QLCayyVSGGQTTAARLRKQLSQT 2232
Cdd:cd05909   383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSeilpeDNEVAVVSVPDGR---KGEKiVLL---TTTTDTDPSSLNDILKNA 456
                         490       500       510
                  ....*....|....*....|....*....|
gi 166797876 2233 -LASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05909   457 gISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
3279-3781 5.39e-27

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 118.58  E-value: 5.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3279 YPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGG 3358
Cdd:cd05920    11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3359 ayLPIDPdSPSER---IRYILNDSSISVLLYCGKLQDDiGFSGTCIDLMEEHfyhekdsslalsyqsSQLAYAIYTSGTT 3435
Cdd:cd05920    91 --VPVLA-LPSHRrseLSAFCAHAEAVAYIVPDRHAGF-DHRALARELAESI---------------PEVALFLLSGGTT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3436 GKPKgtLI--EHRQVIHLIE------GLSRQ-VYSAydaelniAMLAPYYFDASVQQMYASLLSGHTLFIVPKeiVSDGA 3506
Cdd:cd05920   152 GTPK--LIprTHNDYAYNVRasaevcGLDQDtVYLA-------VLPAAHNFPLACPGVLGTLLAGGRVVLAPD--PSPDA 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3507 ALcRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLL---IGGEALSKTTVNKLKQLFGehgaaPGITNVYGPTETCV 3583
Cdd:cd05920   221 AF-PLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRllqVGGARLSPALARRVPPVLG-----CTLQQVFGMAEGLL 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3584 daSLFNIECSSDAWARSQnyvpiGKPLGR-NRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvp 3662
Cdd:cd05920   295 --NYTRLDDPDEVIIHTQ-----GRPMSPdDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-- 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3663 edrmYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYF-AADKTIQ 3741
Cdd:cd05920   366 ----YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVvLRDPPPS 441
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 166797876 3742 ISELRKRM-ARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05920   442 AAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4358-4818 7.40e-27

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 117.62  E-value: 7.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4358 LTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLtca 4437
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4438 ghaipplfegevlllddpllyqgrTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQ 4517
Cdd:cd05973    78 ------------------------TDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFW 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4518 FAA---MSFDVcYQEMFSALSSG--GILfiigNEAKRDIRQLNDFVRTHGIqTAFL--PTAFLKLLASEKHYFEPFAECV 4590
Cdd:cd05973   134 NAAdpgWAYGL-YYAITGPLALGhpTIL----LEGGFSVESTWRVIERLGV-TNLAgsPTAYRLLMAAGAEVPARPKGRL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4591 DHIIAAGEQLiATRMLRDMLARHQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVG 4670
Cdd:cd05973   208 RRVSSAGEPL-TPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4671 ELCI----SGVSLARGYHNRESLTLETfvphpydsnqRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAAL 4746
Cdd:cd05973   287 RLAIdianSPLMWFRGYQLPDTPAIDG----------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESAL 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4747 LKH--VQEAVVLAK----------------ENTDGQSDLyayfTAEQSLSIsqlKEKLAGQipGYMIPSYFIqlEKLPLT 4808
Cdd:cd05973   357 IEHpaVAEAAVIGVpdpertevvkafvvlrGGHEGTPAL----ADELQLHV---KKRLSAH--AYPRTIHFV--DELPKT 425
                         490
                  ....*....|
gi 166797876 4809 GNGKVNRRAL 4818
Cdd:cd05973   426 PSGKIQRFLL 435
PRK08315 PRK08315
AMP-binding domain protein; Validated
1766-2273 8.79e-27

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 119.15  E-value: 8.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1766 DTAAPFPQTPVHQLFEEQSQRTPDQAAVIDKDRQL--TYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILA 1843
Cdd:PRK08315    8 PTDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1844 VLKSGGAYVPIDPEYPQDRIRYMLddSQAGI--------------VLMQRDVRKQLA--------------YEGVTVLLD 1895
Cdd:PRK08315   88 TAKIGAILVTINPAYRLSELEYAL--NQSGCkaliaadgfkdsdyVAMLYELAPELAtcepgqlqsarlpeLRRVIFLGD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1896 DESSYHQDGSDL-APISDVSHLAY-----------VI---YTSGSTGRPKGVLIEHGGLTN---YIwwakevyvkGEKAN 1957
Cdd:PRK08315  166 EKHPGMLNFDELlALGRAVDDAELaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNngyFI---------GEAMK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1958 F----------PLYSSISFDLTVTSIftplVTGNAIIVYDGE--DKTALLESiVRDPRVDIIKLTPAhlqvlkeMNIA-- 2023
Cdd:PRK08315  237 LteedrlcipvPLYHCFGMVLGNLAC----VTHGATMVYPGEgfDPLATLAA-VEEERCTALYGVPT-------MFIAel 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2024 --------DQTAVRRMIVGGENLSTRLARSIHEQFEGR-IEICneYGPTETVVGCMIYRYDAAKDRR-ESVpiGTAAANT 2093
Cdd:PRK08315  305 dhpdfarfDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSeVTIA--YGMTETSPVSTQTRTDDPLEKRvTTV--GRALPHL 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2094 SIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakMYkTGDLAKWLADGNIEYAGRIDEQVk 2172
Cdd:PRK08315  381 EVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-----MH-TGDLAVMDEEGYVNIVGRIKDMI- 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2173 IRG----Y-RielgEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIEL 2245
Cdd:PRK08315  454 IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlrPGATLTEEDVRDFCRGKIAHYKIPRYIRFV 529
                         570       580
                  ....*....|....*....|....*...
gi 166797876 2246 DEMPLTSNGKINKkglpapdFELQDRAE 2273
Cdd:PRK08315  530 DEFPMTVTGKIQK-------FKMREMMI 550
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
265-744 9.01e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 119.10  E-value: 9.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  265 VYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPL 343
Cdd:PRK05677   26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  344 DPEYPKERLQYLLHDADADVLL-----------------VQH-----------------------HLKNSL-AFDGP-VI 381
Cdd:PRK05677  106 NPLYTAREMEHQFNDSGAKALVclanmahlaekvlpktgVKHvivtevadmlpplkrllinavvkHVKKMVpAYHLPqAV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  382 DLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQWKKAFFKHSPADRVLVLYP---YVFDA 457
Cdd:PRK05677  186 KFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVaNMLQCRALMGSNLNEGCEILIAPlplYHIYA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  458 FILNFFGPLISGATLHLLPNEENKETFaiqnaIKQERITHFSTSPRLLKTMIEQMNRE-----DFIHVQHVVVGGEQLET 532
Cdd:PRK05677  266 FTFHCMAMMLIGNHNILISNPRDLPAM-----VKELGKWKFSGFVGLNTLFVALCNNEafrklDFSALKLTLSGGMALQL 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  533 DTVEKLHSLQPrIRINNEYGPTENSVVSTFHPVQSAdeQI-TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARG 611
Cdd:PRK05677  341 ATAERWKEVTG-CAICEGYGMTETSPVVSVNPSQAI--QVgTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  612 YLNRPELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVARED 691
Cdd:PRK05677  418 YWQRPEATDEILDS------DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPD 491
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  692 ADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK05677  492 EKSGEAIKVFVVVKPgeTLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKI 546
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
4330-4818 9.30e-27

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 118.20  E-value: 9.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4330 IPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKG-ACTDQVVAVLTDRSAHMIIgILAILKAGAa 4408
Cdd:cd05920    13 QDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGiRPGDRVVVQLPNVAEFVVL-FFALLRLGA- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4409 fLPIDPeLPEKRRAfmlkdsgaDVLLTCAgHAIPPLfegevLLLDDPllyQGRTDNLNLS----CSENDLMYVIYTSGTT 4484
Cdd:cd05920    91 -VPVLA-LPSHRRS--------ELSAFCA-HAEAVA-----YIVPDR---HAGFDHRALArelaESIPEVALFLLSGGTT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4485 GQPKGVQLEH-------KTMTNLLAYEQDHTQLRfdrVLQfAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLndf 4557
Cdd:cd05920   152 GTPKLIPRTHndyaynvRASAEVCGLDQDTVYLA---VLP-AAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPL--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4558 VRTHGIQ-TAFLPTAFLKLLasekhyfepfaecvDHIIAAGEQLIATRMLR-------DMLARhQV------TLHNHYGP 4623
Cdd:cd05920   225 IEREGVTvTALVPALVSLWL--------------DAAASRRADLSSLRLLQvggarlsPALAR-RVppvlgcTLQQVFGM 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4624 SETHVVtmYTV--DPDtDQELQPIGKPIS-NTEIFILNEAGTLQPVGIVGELCISGVSLARGY-----HNRESLTLETFv 4695
Cdd:cd05920   290 AEGLLN--YTRldDPD-EVIIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYyrapeHNARAFTPDGF- 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4696 phpydsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA 4773
Cdd:cd05920   366 ----------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHpaVHDAAVVAMPDELLGERSCAFVVL 435
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 4774 -EQSLSISQLKEKLAGQ-IPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05920   436 rDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
4333-4815 1.41e-26

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 118.34  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTL--TYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFL 4410
Cdd:PRK12583   19 TIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4411 PIDPELPEKRRAFMLKDSG------ADVLLTCAGHAI-----PPLFEGE--------------VLLLD----------DP 4455
Cdd:PRK12583   99 NINPAYRASELEYALGQSGvrwvicADAFKTSDYHAMlqellPGLAEGQpgalacerlpelrgVVSLApapppgflawHE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4456 LLYQGRT------DNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQL-RFDRVLqfAAMSFDVCYQ 4528
Cdd:PRK12583  179 LQARGETvsrealAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLtEHDRLC--VPVPLYHCFG 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4529 EMFSALS--SGGILFIIGNEAkrdirqlndfvrthgiqtaFLPTAFLKLLASEKH---YFEP--FAECVDHI-------- 4593
Cdd:PRK12583  257 MVLANLGcmTVGACLVYPNEA-------------------FDPLATLQAVEEERCtalYGVPtmFIAELDHPqrgnfdls 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4594 -----IAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTMYT-VDPDTDQELQPIGKPISNTEIFILNEAGTLQPVG 4667
Cdd:PRK12583  318 slrtgIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTtAADDLERRVETVGRTQPHLEVKVVDPDGATVPRG 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4668 IVGELCISGVSLARGYHNRESLTLETFvphpyDSNQRMYkTGDLARYLPEGNIEYAGRRDHQVkIR-GYRVELGEVEAAL 4746
Cdd:PRK12583  398 EIGELCTRGYSVMKGYWNNPEATAESI-----DEDGWMH-TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEEFL 470
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 4747 LKH--VQEAVVLAKENTDGQSDLYAYFTAE--QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:PRK12583  471 FTHpaVADVQVFGVPDEKYGEEIVAWVRLHpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1775-2261 1.59e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 118.60  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1775 PVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI 1854
Cdd:PRK06710   25 PLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPEYPQDRIRYMLDDSQAGIVL-----------MQRDVR----------------KQLAY---------------EGVTV 1892
Cdd:PRK06710  105 NPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKiehvivtriadflpfpKNLLYpfvqkkqsnlvvkvsESETI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1893 LLDDESSYHQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGL-TNYIWWAKEVY--VKGEKANFPLYSSISFDLT 1969
Cdd:PRK06710  185 HLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYncKEGEEVVLGVLPFFHVYGM 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1970 VTSIFTPLVTGNAIIVYDGEDKTALLESIVRD-----PRVDIIKLTPAHLQVLKEMNIadqTAVRRMIVGgenlSTRLAR 2044
Cdd:PRK06710  265 TAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHkvtlfPGAPTIYIALLNSPLLKEYDI---SSIRACISG----SAPLPV 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2045 SIHEQFEgRI---EICNEYGPTETvvgCMIYRYDAAKDRRESVPIGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGV 2120
Cdd:PRK06710  338 EVQEKFE-TVtggKLVEGYGLTES---SPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQI 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2121 ARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTA 2200
Cdd:PRK06710  414 MKGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 2201 REDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK06710  487 VPDPYRGETVKAFVVlkEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
4332-4824 1.84e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 118.14  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4332 TTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQD-----KGactDQVvAVLTDRSAHMIIGILAILKAG 4406
Cdd:PRK08314   10 TSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQecgvrKG---DRV-LLYMQNSPQFVIAYYAILRAN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4407 AAFLPIDPELPEKRRAFMLKDSGADVLLTCA---------------GHAI--------------------------PPLF 4445
Cdd:PRK08314   86 AVVVPVNPMNREEELAHYVTDSGARVAIVGSelapkvapavgnlrlRHVIvaqysdylpaepeiavpawlraepplQALA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4446 EGEVLLLDDpLLYQGRTDnLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKT-MTNLLAyEQDHTQLRFDRV-LQFAAMsF 4523
Cdd:PRK08314  166 PGGVVAWKE-ALAAGLAP-PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTvMANAVG-SVLWSNSTPESVvLAVLPL-F 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4524 DVCYQE--MFSALSSGGILFIIgneAKRDIRQLNDFVRTHGIQ--TAfLPTAFLKLLASEKhyFEPF----AECVDHIIA 4595
Cdd:PRK08314  242 HVTGMVhsMNAPIYAGATVVLM---PRWDREAAARLIERYRVThwTN-IPTMVVDFLASPG--LAERdlssLRYIGGGGA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4596 AGEQLIATRMLRdmlaRHQVTLHNHYGPSETHVVTMytVDPDTDQELQPIGKPISNTEIFILNEAgTLQ--PVGIVGELC 4673
Cdd:PRK08314  316 AMPEAVAERLKE----LTGLDYVEGYGLTETMAQTH--SNPPDRPKLQCLGIPTFGVDARVIDPE-TLEelPPGEVGEIV 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4674 ISGVSLARGYHNRESLTLETFVPHpydSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQ 4751
Cdd:PRK08314  389 VHGPQVFKGYWNRPEATAEAFIEI---DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHpaIQ 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4752 EA-VVLAKENTDGQS--------DLYAYFTAEQSLsISQLKEKLAGqipgYMIPSYFIQLEKLPLTGNGKVNRRALPMPE 4822
Cdd:PRK08314  466 EAcVIATPDPRRGETvkavvvlrPEARGKTTEEEI-IAWAREHMAA----YKYPRIVEFVDSLPKSGSGKILWRQLQEQE 540

                  ..
gi 166797876 4823 AG 4824
Cdd:PRK08314  541 KA 542
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2084-2354 2.28e-26

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 112.92  E-value: 2.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2084 VPIGTAAANTSIYVLDENMKPAPIGVPGEIYIsgAGVARGYLNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEY 2163
Cdd:COG3433    18 PVIPPAIVQARALLLIVDLQGYFGGFGGEGGL--LGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2164 AGRIDEQVKIRGYRIELGEIEAALLQE----EVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVP 2239
Cdd:COG3433    96 GGGLERLVQQVVIRAERGEEEELLLVLraaaVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2240 AYFIELDEMPLTSNGKINKKGLPAPDFELQDRAEYKAPRTKA---EEILVSAWESVLG--AENVSILDNFFDLGGDSIKS 2314
Cdd:COG3433   176 SAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETaltEEELRADVAELLGvdPEEIDPDDNLFDLGLDSIRL 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 166797876 2315 IQVSSRLNQQGYKMEIKDLFQYATIAELSPHIKQNLRIAD 2354
Cdd:COG3433   256 MQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1785-2261 2.39e-26

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 117.10  E-value: 2.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVI--DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDR 1862
Cdd:PRK13391    8 QTTPDKPAVImaSTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 IRYMLDDSQAGIVLM---QRDVRKQLAYE--GVT----VLLDDESSYHQDGSDL------APISDVSHLAYVIYTSGSTG 1927
Cdd:PRK13391   88 AAYIVDDSGARALITsaaKLDVARALLKQcpGVRhrlvLDGDGELEGFVGYAEAvaglpaTPIADESLGTDMLYSSGTTG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1928 RPKGVLIE--HGGL---TNYIWWAKEVYVKGEKANF----PLYSS--ISFDLTVTSIftplvtGNAIIVYDGEDKTALLE 1996
Cdd:PRK13391  168 RPKGIKRPlpEQPPdtpLPLTAFLQRLWGFRSDMVYlspaPLYHSapQRAVMLVIRL------GGTVIVMEHFDAEQYLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1997 SIVRdprvdiIKLTpaHLQVLKEMNIadqtavrRMIVGGE------NLSTrLARSIH-------EQFEGRIE----ICNE 2059
Cdd:PRK13391  242 LIEE------YGVT--HTQLVPTMFS-------RMLKLPEevrdkyDLSS-LEVAIHaaapcppQVKEQMIDwwgpIIHE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2060 -YGPTETVVGCMIyRYDAAKDRRESVpiGTAAANTsIYVLDENMKPAPIGVPGEIYISGaGVARGYLNRPELTAEKFVDD 2138
Cdd:PRK13391  306 yYAATEGLGFTAC-DSEEWLAHPGTV--GRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPD 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2139 PfepgaKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALL-QEEVIKEAVVTAR-----EDVHGFKQLca 2212
Cdd:PRK13391  381 G-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLItHPKVADAAVFGVPnedlgEEVKAVVQP-- 453
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166797876 2213 yyVSGGQTT---AARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK13391  454 --VDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
3278-3715 2.56e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 117.75  E-value: 2.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3278 HYPrEKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAK-GVQADQLVGIMTERSLEMVVGILGVLKA 3356
Cdd:PRK08314    6 TLP-ETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3357 GGAYLPIDPDSPSERIRYILNDSSISVLLyCG--------KLQDDIG--------FSGTCID---------LMEEHFYHE 3411
Cdd:PRK08314   85 NAVVVPVNPMNREEELAHYVTDSGARVAI-VGselapkvaPAVGNLRlrhvivaqYSDYLPAepeiavpawLRAEPPLQA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3412 KDSSLALSYQSS---------------QLAYAIYTSGTTGKPKGTLIEHRQVIHLIegLSRQVYSAYDAELNIAMLAPYY 3476
Cdd:PRK08314  164 LAPGGVVAWKEAlaaglappphtagpdDLAVLPYTSGTTGVPKGCMHTHRTVMANA--VGSVLWSNSTPESVVLAVLPLF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3477 FDASVQQ-MYASLLSGHTLFIVPKeivSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLI---GGEALS 3552
Cdd:PRK08314  242 HVTGMVHsMNAPIYAGATVVLMPR---WDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYiggGGAAMP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3553 KTTVNKLKQLFGehgaapgITNV--YGPTETcVDASLFNiecssdawarsqnyvpigkPLGRNRMYIL------------ 3618
Cdd:PRK08314  319 EAVAERLKELTG-------LDYVegYGLTET-MAQTHSN-------------------PPDRPKLQCLgiptfgvdarvi 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3619 --DSKKRLqPKGVQGELYIAGDGVGRGYLNLPELTDEKFVAdpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGF 3696
Cdd:PRK08314  372 dpETLEEL-PPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGF 447
                         490
                  ....*....|....*....
gi 166797876 3697 RIELGEIESVMLNVPDIQE 3715
Cdd:PRK08314  448 KVWPAEVENLLYKHPAIQE 466
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
289-744 2.86e-26

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 115.69  E-value: 2.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNSLAfDGPVIDLndeasyhadcsllspvaghshlayviYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd05973    81 ANRHKLD-SDPFVMM--------------------------FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFW 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VL----YPYVFDAFILnffGPLISGatlhlLPNEENKETFAIQNA---IKQERITHFSTSP---RLLKTMIEQMNREDFI 518
Cdd:cd05973   134 NAadpgWAYGLYYAIT---GPLALG-----HPTILLEGGFSVESTwrvIERLGVTNLAGSPtayRLLMAAGAEVPARPKG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  519 HVQHVVVGGEQLeTDTVEKLHSLQPRIRINNEYGPTE-NSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGI 597
Cdd:cd05973   206 RLRRVSSAGEPL-TPEVIRWFDAALGVPIHDHYGQTElGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGE 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  598 PGELYVGGAGVA----RGYLNRPELTeekfvehlhvPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEA 673
Cdd:cd05973   285 PGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES 354
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  674 AMFNLENVREAAVVAREDADGAKQLYAYYV------GEPSLtAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05973   355 ALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrggheGTPAL-ADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
4340-4734 2.96e-26

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 117.34  E-value: 2.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4340 QQAERNPDHEAVMF------GNQTLTYRQLNERSNQLARVLQDKGACTDqVVAVLTDRSAHMIIGILAILKAGAAFLPI- 4412
Cdd:cd05931     1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4413 DPELPE--KRRAFMLKDSGADVLLTCAGH--------AIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSG 4482
Cdd:cd05931    80 PPTPGRhaERLAAILADAGPRVVLTTAAAlaavrafaASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4483 TTGQPKGVQLEHKtmtNLLAyeqDHTQLRfdrvLQFAAMSFDVC------YQEMfsalssGGILFIIgneakrdirqLND 4556
Cdd:cd05931   160 STGTPKGVVVTHR---NLLA---NVRQIR----RAYGLDPGDVVvswlplYHDM------GLIGGLL----------TPL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4557 FVRTHGIQTAflPTAF-------LKLLASEK--HYFEP---FAECVD----------------HIIAAGEQL-IATrmLR 4607
Cdd:cd05931   214 YSGGPSVLMS--PAAFlrrplrwLRLISRYRatISAAPnfaYDLCVRrvrdedlegldlsswrVALNGAEPVrPAT--LR 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4608 DMLAR------HQVTLHNHYGPSETHV-VTM------YTVDPDTDQELQPI-----------------GKPISNTEIFIL 4657
Cdd:cd05931   290 RFAEAfapfgfRPEAFRPSYGLAEATLfVSGgppgtgPVVLRVDRDALAGRavavaaddpaarelvscGRPLPDQEVRIV 369
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4658 NEAG-TLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLArYLPEGNIEYAGRRDHQVKIRG 4734
Cdd:cd05931   370 DPETgRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRG 446
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1788-2276 3.32e-26

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 116.51  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKD-RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYM 1866
Cdd:PRK07514   16 RDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1867 LDDSQAGIVL----MQRDVRKQLAYEGVTVL--LDDESSyhqdGS--DLAPISDVSH---------LAYVIYTSGSTGRP 1929
Cdd:PRK07514   96 IGDAEPALVVcdpaNFAWLSKIAAAAGAPHVetLDADGT----GSllEAAAAAPDDFetvprgaddLAAILYTSGTTGRS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1930 KGVLIEHGGL-TNYI-------WWAKEVYVKGekanFPLYSsisfdltVTSIFtplVTGNaiivydgedkTALLE--SIV 1999
Cdd:PRK07514  172 KGAMLSHGNLlSNALtlvdywrFTPDDVLIHA----LPIFH-------THGLF---VATN----------VALLAgaSMI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2000 RDPRVD---IIKLTPA----------HLQVLKEMNIaDQTAVRRM--IVGGenlSTRLARSIHEQFEGRI--EICNEYGP 2062
Cdd:PRK07514  228 FLPKFDpdaVLALMPRatvmmgvptfYTRLLQEPRL-TREAAAHMrlFISG---SAPLLAETHREFQERTghAILERYGM 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2063 TETvvgCMIYR--YDAakDRRESVpIGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDP 2139
Cdd:PRK07514  304 TET---NMNTSnpYDG--ERRAGT-VGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2140 FepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKE----------------AVVTARed 2203
Cdd:PRK07514  378 F------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVEsavigvphpdfgegvtAVVVPK-- 449
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 2204 vhgfkqlcayyvSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLpapdfelqdRAEYKA 2276
Cdd:PRK07514  450 ------------PGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL---------REQYAD 501
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
4333-4818 4.21e-26

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 117.08  E-value: 4.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGN------QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAG 4406
Cdd:PRK13295   25 TINDDLDACVASCPDKTAVTAVRlgtgapRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4407 AAFLPIDPELPEKRRAFMLKDSGADVLltcaghAIPPLFEG------------------EVL------------LLDDPL 4456
Cdd:PRK13295  105 AVLNPLMPIFRERELSFMLKHAESKVL------VVPKTFRGfdhaamarrlrpelpalrHVVvvggdgadsfeaLLITPA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4457 LYQGRTDNLNLSCSE---NDLMYVIYTSGTTGQPKGVQLEHKT-MTNLLAYEQdhtQLRF---DRVLQFAAMSFDVCYQ- 4528
Cdd:PRK13295  179 WEQEPDAPAILARLRpgpDDVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAE---RLGLgadDVILMASPMAHQTGFMy 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4529 --EMFSALSSGGILFIIGNEAkrdirQLNDFVRTHGIQTAFLPTAFL-KLLASEKHYFEPFAEcVDHIIAAGEQlIATRM 4605
Cdd:PRK13295  256 glMMPVMLGATAVLQDIWDPA-----RAAELIRTEGVTFTMASTPFLtDLTRAVKESGRPVSS-LRTFLCAGAP-IPGAL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4606 LRDMLARHQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHN 4685
Cdd:PRK13295  329 VERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLK 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4686 RESLTLetfvphpyDSNQRMYKTGDLARYLPEGNIEYAGR-RDhqVKIRG-YRVELGEVEAALLKH--VQEAVVLAKENT 4761
Cdd:PRK13295  409 RPQLNG--------TDADGWFDTGDLARIDADGYIRISGRsKD--VIIRGgENIPVVEIEALLYRHpaIAQVAIVAYPDE 478
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 4762 DGQSDLYAYFT--AEQSLSISQLKE-----KLAGQipgyMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK13295  479 RLGERACAFVVprPGQSLDFEEMVEflkaqKVAKQ----YIPERLVVRDALPRTPSGKIQKFRL 538
PRK06188 PRK06188
acyl-CoA synthetase; Validated
4321-4818 4.37e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 116.62  E-value: 4.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4321 NDTAVAEKRIPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGIL 4400
Cdd:PRK06188    1 QATMADLLHSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4401 AILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTcagHAIPPLFEGEVLLLDDPLLYQ--------GRTDNLNLSCSEN 4472
Cdd:PRK06188   81 AAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIV---DPAPFVERALALLARVPSLKHvltlgpvpDGVDLLAAAAKFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 -----------DLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFD-RVLqfaamsfdvcyqeMFSALSSGGIL 4540
Cdd:PRK06188  158 paplvaaalppDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADpRFL-------------MCTPLSHAGGA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4541 FII-----GNE----AKRDIRQLNDFVRTHGIQTAFL-PTAFLKLLasekhyfepfaecvDH------------IIAAGE 4598
Cdd:PRK06188  225 FFLptllrGGTvivlAKFDPAEVLRAIEEQRITATFLvPTMIYALL--------------DHpdlrtrdlssleTVYYGA 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4599 QLIATRMLRDMLARHQVTLHNHYGPSETH--VVTMYTVDPDTDQE--LQPIGKPISNTEIFILNEAGTLQPVGIVGELCI 4674
Cdd:PRK06188  291 SPMSPVRLAEAIERFGPIFAQYYGQTEAPmvITYLRKRDHDPDDPkrLTSCGRPTPGLRVALLDEDGREVAQGEVGEICV 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4675 SGVSLARGYHNRESLTLETFvphpydSNQRMYkTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH----- 4749
Cdd:PRK06188  371 RGPLVMDGYWNRPEETAEAF------RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHpavaq 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4750 --------------VQEAVVLakeNTDGQSDlyayfTAEQslsISQLKE-KLAGQIPGYMIpsyFIqlEKLPLTGNGKVN 4814
Cdd:PRK06188  444 vavigvpdekwgeaVTAVVVL---RPGAAVD-----AAEL---QAHVKErKGSVHAPKQVD---FV--DSLPLTALGKPD 507

                  ....
gi 166797876 4815 RRAL 4818
Cdd:PRK06188  508 KKAL 511
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
4330-4818 4.52e-26

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 116.61  E-value: 4.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4330 IPTTIHQLFEQQAERNPDHEAVMFGN----QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKA 4405
Cdd:cd05906     8 APRTLLELLLRAAERGPTKGITYIDAdgseEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4406 G--AAFLPIDPELPEKRRA-------FMLKDSGAdVLLTCAGHA-IPPLFEGEVLLLDDPLLYQGRTDNLNLS----CSE 4471
Cdd:cd05906    88 GfvPAPLTVPPTYDEPNARlrklrhiWQLLGSPV-VLTDAELVAeFAGLETLSGLPGIRVLSIEELLDTAADHdlpqSRP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4472 NDLMYVIYTSGTTGQPKGVQLEHKTMTN-LLAYEQDHTQLRFDRVLQFAAMS----------FDVCYQ-EMFSALSSGgI 4539
Cdd:cd05906   167 DDLALLMLTSGSTGFPKAVPLTHRNILArSAGKIQHNGLTPQDVFLNWVPLDhvgglvelhlRAVYLGcQQVHVPTEE-I 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4540 LfiigneakRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEKHYFEPFA---ECVDHIIAAGEQLIA--TRMLRDMLARHQ 4614
Cdd:cd05906   246 L--------ADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTwdlSSLRYLVNAGEAVVAktIRRLLRLLEPYG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4615 V---TLHNHYGPSETHVVTMYTVD---PDTDQELQ--PIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNR 4686
Cdd:cd05906   318 LppdAIRPAFGMTETCSGVIYSRSfptYDHSQALEfvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNN 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4687 ESLTLETFVPHPYdsnqrmYKTGDLArYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAAllkhVQEAVVLAKENT----- 4761
Cdd:cd05906   398 PEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAA----VEEVPGVEPSFTaafav 466
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4762 ---DGQSDLYAYF----------TAEQSLSISQLKEKLAGQIPGYMIPsyfIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05906   467 rdpGAETEELAIFfvpeydlqdaLSETLRAIRSVVSREVGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
3307-3715 4.61e-26

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 115.53  E-value: 4.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3307 KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLy 3386
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3387 cgkLQDDigfsgtcidlmeehfyhekdsslalsyqSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSrQVYSAYDAE 3466
Cdd:cd17640    83 ---VEND----------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLS-DIVPPQPGD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3467 LNIAMLAPYY----------FDASVQQMYASL---------LSGHTLFIVPK--EIVSDGaalcrYYRQhsidITDGTPA 3525
Cdd:cd17640   131 RFLSILPIWHsyersaeyfiFACGCSQAYTSIrtlkddlkrVKPHYIVSVPRlwESLYSG-----IQKQ----VSKSSPI 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3526 HLKLLIAAgdLQGVTLQHLLIGGEALSKtTVNKLKQLFGEHgaapgITNVYGPTETCVDASLFNIECssdawarsqNYV- 3604
Cdd:cd17640   202 KQFLFLFF--LSGGIFKFGISGGGALPP-HVDTFFEAIGIE-----VLNGYGLTETSPVVSARRLKC---------NVRg 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 PIGKPLGRNRMYILDSK-KRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEY 3683
Cdd:cd17640   265 SVGRPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVL 338
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 3684 IGRI-DHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd17640   339 TGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQ 371
PRK07514 PRK07514
malonyl-CoA synthase; Validated
289-744 7.48e-26

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 115.74  E-value: 7.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH 368
Cdd:PRK07514   29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNSL---AFD---GPVIDLNDEASyhadCSLLSPVAGHSH-----------LAYVIYTSGTTGKPKGVMVEHGGIVNS 431
Cdd:PRK07514  109 ANFAWLskiAAAagaPHVETLDADGT----GSLLEAAAAAPDdfetvprgaddLAAILYTSGTTGRSKGAMLSHGNLLSN 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  432 LQWKKAFFKHSPADRVLVLYPyVFDA---FI-LNffGPLISGATLHLLPNEENKETFAiqnaiKQERITHFSTSP----R 503
Cdd:PRK07514  185 ALTLVDYWRFTPDDVLIHALP-IFHThglFVaTN--VALLAGASMIFLPKFDPDAVLA-----LMPRATVMMGVPtfytR 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  504 LLKTmiEQMNREDFIHVQHVVVGGEQLETDTveklH-SLQPRI--RINNEYGPTEnSVVSTFHPVQSADEQITIGSPVAN 580
Cdd:PRK07514  257 LLQE--PRLTREAAAHMRLFISGSAPLLAET----HrEFQERTghAILERYGMTE-TNMNTSNPYDGERRAGTVGFPLPG 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  581 HQAYILG-AHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYLGRIDHQV 659
Cdd:PRK07514  330 VSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRA------DGFFITGDLGKIDERGYVHIVGRGKDLI 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  660 KIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIP 737
Cdd:PRK07514  404 ISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPgaALDEAAILAALKGRLARFKQPKRVFFVDELP 483

                  ....*..
gi 166797876  738 LTSNGKI 744
Cdd:PRK07514  484 RNTMGKV 490
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1779-2272 1.27e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 115.64  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1779 LFEEQSQRTPDQAAVI--DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDP 1856
Cdd:PRK12583   23 AFDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1857 EYPQDRIRYMLDDSQA-GIVLMQR-----------DVRKQLAYEGVT-------------VLLDDE-----SSYHQ---- 1902
Cdd:PRK12583  103 AYRASELEYALGQSGVrWVICADAfktsdyhamlqELLPGLAEGQPGalacerlpelrgvVSLAPApppgfLAWHElqar 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1903 ----DGSDLAPISDVSHLAYVI---YTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEK----ANFPLYSSISFDLTVT 1971
Cdd:PRK12583  183 getvSREALAERQASLDRDDPIniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHdrlcVPVPLYHCFGMVLANL 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1972 SIftplVTGNAIIVYDGE--DKTALLESIVRDprvdiiKLTPahLQVLKEMNIA----------DQTAVRRMIVGGENLS 2039
Cdd:PRK12583  263 GC----MTVGACLVYPNEafDPLATLQAVEEE------RCTA--LYGVPTMFIAeldhpqrgnfDLSSLRTGIMAGAPCP 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2040 TRLARSIHEQFEgRIEICNEYGPTETV-VGCMIYRYDAAKDRRESVpiGTAAANTSIYVLDENMKPAPIGVPGEIYISGA 2118
Cdd:PRK12583  331 IEVMRRVMDEMH-MAEVQIAYGMTETSpVSLQTTAADDLERRVETV--GRTQPHLEVKVVDPDGATVPRGEIGELCTRGY 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2119 GVARGYLNRPELTAEKFVDDPFepgakMYkTGDLAKWLADGNIEYAGRIDEQVkIRG-YRIELGEIEAALLQEEVIKEAV 2197
Cdd:PRK12583  408 SVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRGgENIYPREIEEFLFTHPAVADVQ 480
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 2198 VTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKkglpapdFELQDRA 2272
Cdd:PRK12583  481 VFGVPDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK-------FRMREIS 550
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
288-744 1.40e-25

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 114.80  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  288 HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ 367
Cdd:PRK12406   11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  368 HHLKNSLAFDGP------VIDLNDE--ASYHADCSLLSPVAGHSHL------------------AYVIYTSGTTGKPKGV 421
Cdd:PRK12406   91 ADLLHGLASALPagvtvlSVPTPPEiaAAYRISPALLTPPAGAIDWegwlaqqepydgppvpqpQSMIYTSGTTGHPKGV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  422 -----MVEHGgiVNSLQWKKAFFKHSPADRVLV---LY---PYVFDAFILNFfgplisGATLHLLPNEENKETFAIqnaI 490
Cdd:PRK12406  171 rraapTPEQA--AAAEQMRALIYGLKPGIRALLtgpLYhsaPNAYGLRAGRL------GGVLVLQPRFDPEELLQL---I 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  491 KQERITHFSTSP----RLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLhslqprIR-----INNEYGPTENSVVST 561
Cdd:PRK12406  240 ERHRITHMHMVPtmfiRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAM------IEwwgpvIYEYYGSTESGAVTF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  562 FHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVAR-GYLNRPE----LTEEKFVehlhvpgqkmyK 636
Cdd:PRK12406  314 ATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEkraeIDRGGFI-----------T 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  637 TGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFR 714
Cdd:PRK12406  383 SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPgaTLDEADIR 462
                         490       500       510
                  ....*....|....*....|....*....|
gi 166797876  715 EELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK12406  463 AQLKARLAGYKVPKHIEIMAELPREDSGKI 492
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1792-2261 1.62e-25

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 113.34  E-value: 1.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1792 AVIDKDRQLTYGELNKRANRLARTLRAKGV-QTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPeypqdrirymldds 1870
Cdd:cd05958     3 CLRSPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP-------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1871 qagiVLMQRDVRKQLAYEGVTVLLDDESSYHQDgsdlapisDVSHLAYviyTSGSTGRPKGVLIEHGG-LTNYIWWAKEV 1949
Cdd:cd05958    69 ----LLRPKELAYILDKARITVALCAHALTASD--------DICILAF---TSGTTGAPKATMHFHRDpLASADRYAVNV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1950 YVKGEKANF----PLYSSISFDLTvtsIFTPLVTGNAIIVYDGEDKTALLESIVRDpRVDIIKLTP---AHLQVLKEMNI 2022
Cdd:cd05958   134 LRLREDDRFvgspPLAFTFGLGGV---LLFPFGVGASGVLLEEATPDLLLSAIARY-KPTVLFTAPtayRAMLAHPDAAG 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2023 ADQTAVRRMIVGGENLSTRLARSIHEQFEgrIEICNEYGPTETVVGCMIYRYDAAKDRRESVPI-GTAAAntsiyVLDEN 2101
Cdd:cd05958   210 PDLSSLRKCVSAGEALPAALHRAWKEATG--IPIIDGIGSTEMFHIFISARPGDARPGATGKPVpGYEAK-----VVDDE 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2102 MKPAPIGVPGEIYISGAgvaRGYLNRPELTAEKFVDDPFEpgakmyKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELG 2181
Cdd:cd05958   283 GNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWN------ITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPP 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2182 EIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV-----SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKI 2256
Cdd:cd05958   354 EVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKL 433

                  ....*
gi 166797876 2257 NKKGL 2261
Cdd:cd05958   434 QRFAL 438
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
405-749 1.79e-25

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 117.33  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  405 LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyVFDAFIL--NFFGPLISGATLHLLPNEenKE 482
Cdd:PRK08633  784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLP-FFHSFGLtvTLWLPLLEGIKVVYHPDP--TD 860
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  483 TFAIQNAIKQERIT-HFSTSPRL-LKTMIEQMNREDFIHVQHVVVGGEQLETDT----VEKLHslqprIRINNEYGPTEN 556
Cdd:PRK08633  861 ALGIAKLVAKHRATiLLGTPTFLrLYLRNKKLHPLMFASLRLVVAGAEKLKPEVadafEEKFG-----IRILEGYGATET 935
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  557 S-VVSTFHP--------VQSADEQITIGSPVANHQAYILGAHH-QIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEh 626
Cdd:PRK08633  936 SpVASVNLPdvlaadfkRQTGSKEGSVGMPLPGVAVRIVDPETfEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD- 1014
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  627 lhVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVE---AAMFNLENVrEAAVVAREDADGAKQLYAYYV 703
Cdd:PRK08633 1015 --IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelAKALGGEEV-VFAVTAVPDEKKGEKLVVLHT 1091
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876  704 gEPSLTAAQFREELSR-ELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK08633 1092 -CGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
261-744 1.89e-25

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 114.86  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  261 GSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAY 340
Cdd:PRK06155   19 SERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  341 VPLDPEYPKERLQYLLHDADADVLLVQHHLKNSL-AFDGPVIDLND--------EASYHADCSLLSPVAGHSHL------ 405
Cdd:PRK06155   99 VPINTALRGPQLEHILRNSGARLLVVEAALLAALeAADPGDLPLPAvwlldapaSVSVPAGWSTAPLPPLDAPApaaavq 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  406 ----AYVIYTSGTTGKPKGVMVEHGgivnSLQW---KKAFFKHSPADRVLVLYPYVFDAFILN-FFGPLISGATLHLLPN 477
Cdd:PRK06155  179 pgdtAAILYTSGTTGPSKGVCCPHA----QFYWwgrNSAEDLEIGADDVLYTTLPLFHTNALNaFFQALLAGATYVLEPR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  478 EENKETFAiqnaikqERITHFSTSPRLLKTMIEQM-----NREDFIHVQHVVVGG---EQLETDTVEKLHslqprIRINN 549
Cdd:PRK06155  255 FSASGFWP-------AVRRHGATVTYLLGAMVSILlsqpaRESDRAHRVRVALGPgvpAALHAAFRERFG-----VDLLD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  550 EYGPTE-NSVVSTFHPVQSADeqiTIGSPVANHQAYILGAHHQIQPIGIPGELYVGGA---GVARGYLNRPELTEEKFvE 625
Cdd:PRK06155  323 GYGSTEtNFVIAVTHGSQRPG---SMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW-R 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  626 HLhvpgqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGE 705
Cdd:PRK06155  399 NL------WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLR 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 166797876  706 PSlTAAQFrEELSR----ELPNYMIPsRFIP-LERIPLTSNGKI 744
Cdd:PRK06155  473 DG-TALEP-VALVRhcepRLAYFAVP-RYVEfVAALPKTENGKV 513
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
4356-4757 2.28e-25

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 113.46  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 caghaipplfegevlllDDPllyqgrtdnlnlscseNDLMYVIYTSGTTGQPKGVQLEHKTMT-NLLAYEQDHTQLRFDR 4514
Cdd:cd05907    84 -----------------EDP----------------DDLATIIYTSGTTGRPKGVMLSHRNILsNALALAERLPATEGDR 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4515 VLQFAAMS--FDVCYQEMFSALSSGGILFIigneakRDIRQLNDFVRThgiqtaFLPTAFLKLLAS-EKHYfepfaecvd 4591
Cdd:cd05907   131 HLSFLPLAhvFERRAGLYVPLLAGARIYFA------SSAETLLDDLSE------VRPTVFLAVPRVwEKVY--------- 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4592 hiiAAGEQLIATRMLRDMLARHQ--------------------------VTLHNHYGPSETHVVtmYTVDPDTDQELQPI 4645
Cdd:cd05907   190 ---AAIKVKAVPGLKRKLFDLAVggrlrfaasggaplpaellhffralgIPVYEGYGLTETSAV--VTLNPPGDNRIGTV 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4646 GKPISNTEIFIlneagtlqpvGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPEGNIEYAGR 4725
Cdd:cd05907   265 GKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGR 328
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 166797876 4726 -RDHQVKIRGYRVELGEVEAALLKH--VQEAVVLA 4757
Cdd:cd05907   329 kKDLIITSGGKNISPEPIENALKASplISQAVVIG 363
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1787-2258 3.06e-25

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 114.13  E-value: 3.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1787 TPDQAAVIDKD-----RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI------- 1854
Cdd:cd05970    30 YPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAthqltak 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPEYPQDR--IRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDES-----SYHQDGSDLAPISDVSH---------LAY 1918
Cdd:cd05970   110 DIVYRIESadIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVpegwiDFRKLIKNASPDFERPTansypcgedILL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKgvLIEHGG-------LTNYIW----------------WAKEVYVKgekanfplyssisfdltvtsIFT 1975
Cdd:cd05970   190 VYFSSGTTGMPK--MVEHDFtyplghiVTAKYWqnvregglhltvadtgWGKAVWGK--------------------IYG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1976 PLVTGNAIIVYDGE--DKTALLESIVRDpRVDIIKLTPAHLQVLKEMNIA--DQTAVRRMIVGGENLSTrlarSIHEQFE 2051
Cdd:cd05970   248 QWIAGAAVFVYDYDkfDPKALLEKLSKY-GVTTFCAPPTIYRFLIREDLSryDLSSLRYCTTAGEALNP----EVFNTFK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2052 GR--IEICNEYGPTETVVGCMIYRYDAAKdrresvP--IGTAAANTSIYVLDENMKPAPIGVPGEIYISGA-----GVAR 2122
Cdd:cd05970   323 EKtgIKLMEGFGQTETTLTIATFPWMEPK------PgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2123 GYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARE 2202
Cdd:cd05970   397 GYYKDAEKTAEVWHDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVP 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 2203 D------VHGFKQLCAYYvSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:cd05970   470 DpirgqvVKATIVLAKGY-EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
3279-3781 3.41e-25

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 114.09  E-value: 3.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3279 YPREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGG 3358
Cdd:COG1021    21 YWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3359 ----AYlpidpdsPSER---IRYILNDSSISVLLYCGK------------LQDD---------IGFSGTCIDLmeEHFYH 3410
Cdd:COG1021   101 ipvfAL-------PAHRraeISHFAEQSEAVAYIIPDRhrgfdyralareLQAEvpslrhvlvVGDAGEFTSL--DALLA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3411 EKDSSLALSYQSSQLAYAIYTSGTTGKPKgtLIE--HRQVIHLIE------GLSRQvySAYDAEL----NIAMLAPYYFd 3478
Cdd:COG1021   172 APADLSEPRPDPDDVAFFQLSGGTTGLPK--LIPrtHDDYLYSVRasaeicGLDAD--TVYLAALpaahNFPLSSPGVL- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3479 asvqqmyASLLSGHTLFIVPkeiVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGV---TLQHLLIGGEALSKTT 3555
Cdd:COG1021   247 -------GVLYAGGTVVLAP---DPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYdlsSLRVLQVGGAKLSPEL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3556 VNKLKQLFGehgaaPGITNVYGPTE-----TCVDASLfniecssDAWARSQnyvpiGKPLG-----RnrmyILDSKKRLQ 3625
Cdd:COG1021   317 ARRVRPALG-----CTLQQVFGMAEglvnyTRLDDPE-------EVILTTQ-----GRPISpddevR----IVDEDGNPV 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3626 PKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIES 3705
Cdd:COG1021   376 PPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVEN 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3706 VMLNVPDIQ---------EaaaaalkdaddeyYL----CGYF-AADKTIQISELRKRM-ARHLPGYMIPAHFVQLDKMPL 3770
Cdd:COG1021   450 LLLAHPAVHdaavvampdE-------------YLgersCAFVvPRGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPL 516
                         570
                  ....*....|.
gi 166797876 3771 TPNGKLNRQLL 3781
Cdd:COG1021   517 TAVGKIDKKAL 527
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
262-744 4.29e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 114.10  E-value: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  262 SRTVYQLFEEQAERTPENAAVKFKNDHL--TYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGA 339
Cdd:PRK12583   17 TQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  340 YVPLDPEYPKERLQYLLHDADADVLLVQHHLKNS------------LAFDGPVIDLNDEASYHADCSLLSPVAGHSHLAY 407
Cdd:PRK12583   97 LVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhamlqellpgLAEGQPGALACERLPELRGVVSLAPAPPPGFLAW 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 -----------------------------VIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYvFDAF 458
Cdd:PRK12583  177 helqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL-YHCF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  459 --ILNFFGPLISGATLhLLPNEENKETFAIQnAIKQERITHFSTSPRLLKTMIE--QMNREDFIHVQHVVVGGE----QL 530
Cdd:PRK12583  256 gmVLANLGCMTVGACL-VYPNEAFDPLATLQ-AVEEERCTALYGVPTMFIAELDhpQRGNFDLSSLRTGIMAGApcpiEV 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  531 ETDTVEKLHslQPRIRINneYGPTENSVVSTFHPVQSADEQ--ITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGV 608
Cdd:PRK12583  334 MRRVMDEMH--MAEVQIA--YGMTETSPVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  609 ARGYLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVkIR-GYRIEIGEVEAAMFNLENVREAA 685
Cdd:PRK12583  410 MKGYWNNPEATAESIDEDgwMH--------TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEEFLFTHPAVADVQ 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876  686 VVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK12583  481 VFGVPDEKYGEEIVAWVRLHPghAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
258-749 4.52e-25

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 113.96  E-value: 4.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  258 DFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAG 337
Cdd:PRK07059   18 DASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  338 GAYVPLDPEYPKERLQYLLHD--ADADVLL------VQHHLKNS-------------LAFDGPVIDL------------- 383
Cdd:PRK07059   98 YVVVNVNPLYTPRELEHQLKDsgAEAIVVLenfattVQQVLAKTavkhvvvasmgdlLGFKGHIVNFvvrrvkkmvpaws 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  384 -------NDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQ---WKKAFFKHSPADRVLV--- 449
Cdd:PRK07059  178 lpghvrfNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQmeaWLQPAFEKKPRPDQLNfvc 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  450 ---LYpYVFdAFILNFFGPLISGATLHLLPNEENketfaIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHV--QHVV 524
Cdd:PRK07059  258 alpLY-HIF-ALTVCGLLGMRTGGRNILIPNPRD-----IPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLdfSKLI 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  525 V---GGEQLETDTVEKLHSLQpRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGEL 601
Cdd:PRK07059  331 VangGGMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEI 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  602 YVGGAGVARGYLNRPE-----LTEEKFvehlhvpgqkmYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMF 676
Cdd:PRK07059  410 CIRGPQVMAGYWNRPDetakvMTADGF-----------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  677 NLENVREAAVVAREDADGAKQLYAYYV-GEPSLTAAQFREELSRELPNYMIPsRFIPL-ERIPLTSNGKIDLKAL 749
Cdd:PRK07059  479 SHPGVLEVAAVGVPDEHSGEAVKLFVVkKDPALTEEDVKAFCKERLTNYKRP-KFVEFrTELPKTNVGKILRREL 552
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1791-2281 4.74e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 113.07  E-value: 4.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1791 AAVIDKD-RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDD 1869
Cdd:PRK08276    2 AVIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1870 SQAGIVLMQ---RDVRKQLAYE---GVTVLL------DDESSYHQ--DGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIE 1935
Cdd:PRK08276   82 SGAKVLIVSaalADTAAELAAElpaGVPLLLvvagpvPGFRSYEEalAAQPDTPIADETAGADMLYSSGTTGRPKGIKRP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1936 HGGL--------------TNYIWWAKEVYVKGEkanfPLYSS--ISFDLTVTSIftplvtGNAIIVYDGEDKTALLESIV 1999
Cdd:PRK08276  162 LPGLdpdeapgmmlallgFGMYGGPDSVYLSPA----PLYHTapLRFGMSALAL------GGTVVVMEKFDAEEALALIE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2000 RDpRVDIIKLTPAHLqvlkemniadqtavRRMIVGGENLSTR-----LARSIH-------EQFEGRIE----ICNE-YGP 2062
Cdd:PRK08276  232 RY-RVTHSQLVPTMF--------------VRMLKLPEEVRARydvssLRVAIHaaapcpvEVKRAMIDwwgpIIHEyYAS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2063 TETVVGCMIYRYDAAKdRRESVpiGTAAANTsIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFep 2142
Cdd:PRK08276  297 SEGGGVTVITSEDWLA-HPGSV--GKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW-- 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2143 gakmYKTGDLAkWL-ADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQ------------------EEVIkeAVVTARED 2203
Cdd:PRK08276  371 ----VTVGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVThpkvadvavfgvpdeemgERVK--AVVQPADG 443
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 2204 VHGFKQLcayyvsggqttAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLpapdfelqdRAEYKAPRTKA 2281
Cdd:PRK08276  444 ADAGDAL-----------AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL---------RDRYWEGRQRA 501
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1789-2368 6.36e-25

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 114.36  E-value: 6.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1789 DQAAVIDKDrQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLD 1868
Cdd:PRK06060   21 DRPAFYAAD-VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAAR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1869 DSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDG-SDLAPISDVSHlAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAK 1947
Cdd:PRK06060  100 NTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVApGGYEPMGGDAL-AYATYTSGTTGPPKAAIHRHADPLTFVDAMC 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1948 EVYVKGEKANFPLYSS---ISFDLTvTSIFTPLVTGNAIIVYD---GEDKTALLeSIVRDPRVdiIKLTPAHLQVLKEMN 2021
Cdd:PRK06060  179 RKALRLTPEDTGLCSArmyFAYGLG-NSVWFPLATGGSAVINSapvTPEAAAIL-SARFGPSV--LYGVPNFFARVIDSC 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2022 IADQ-TAVRRMIVGGENLSTRLARSIHEQFEGrIEICNEYGPTEtvVGcMIYRYDAAKDRRESVpIGTAAANTSIYVLDE 2100
Cdd:PRK06060  255 SPDSfRSLRCVVSAGEALELGLAERLMEFFGG-IPILDGIGSTE--VG-QTFVSNRVDEWRLGT-LGRVLPPYEIRVVAP 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2101 NMKPAPIGVPGEIYISGAGVARGYLNRPE--LTAEKFVDdpfepgakmykTGDLAKWLADGNIEYAGRIDEQVKIRGYRI 2178
Cdd:PRK06060  330 DGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDRVCIDSDGWVTYRCRADDTEVIGGVNV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2179 ELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLR---KQLSQTLASYMVPAYFIELDEMPLTSN 2253
Cdd:PRK06060  399 DPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVatSGATIDGSVMRdlhRGLLNRLSAFKVPHRFAVVDRLPRTPN 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2254 GKINKKGL----PA-PDFEL---QDRAEYKA-----PRTKAEEILVSAWESVLG-------------------AENVSIL 2301
Cdd:PRK06060  479 GKLVRGALrkqsPTkPIWELsltEPGSGVRAqrddlSASNMTIAGGNDGGATLRerlvalrqerqrlvvdavcAEAAKML 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2302 DN-----------FFDLGGDSIKSIQVSSRLN-QQGYKMEIKDLFQYATIAELSPHIKQNLRIAD------QGEVKGKVS 2363
Cdd:PRK06060  559 GEpdpwsvdqdlaFSELGFDSQMTVTLCKRLAaVTGLRLPETVGWDYGSISGLAQYLEAELAGGHgrlksaGPVNSGATG 638

                  ....*
gi 166797876 2364 LTPIQ 2368
Cdd:PRK06060  639 LWAIE 643
PLN02246 PLN02246
4-coumarate--CoA ligase
1775-2203 8.55e-25

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 112.77  E-value: 8.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1775 PVHQ-LFEEQSQRtPDQAAVID--KDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAY 1851
Cdd:PLN02246   24 PLHDyCFERLSEF-SDRPCLIDgaTGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1852 VPIDPEYPQDRIRYMLDDSQAGIVLMQR----DVRKQLAYEGVTVLLDD---ESSYH------QDGSDLAPIS----DVS 1914
Cdd:PLN02246  103 TTANPFYTPAEIAKQAKASGAKLIITQScyvdKLKGLAEDDGVTVVTIDdppEGCLHfseltqADENELPEVEispdDVV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1915 HLAyviYTSGSTGRPKGVLIEHGGLTNYIwwAKEvyVKGEKANF------------PLYSSISFDltvtSI-FTPLVTGN 1981
Cdd:PLN02246  183 ALP---YSSGTTGLPKGVMLTHKGLVTSV--AQQ--VDGENPNLyfhsddvilcvlPMFHIYSLN----SVlLCGLRVGA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1982 AIIVYDGEDKTALLESIVRDpRVDIIKLTPA-HLQVLK--EMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIeICN 2058
Cdd:PLN02246  252 AILIMPKFEIGALLELIQRH-KVTIAPFVPPiVLAIAKspVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAV-LGQ 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2059 EYGPTE--TVVG-CMIYrydaAKdrrESVPI-----GTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPE 2129
Cdd:PLN02246  330 GYGMTEagPVLAmCLAF----AK---EPFPVksgscGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPE 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2130 LTAEkfvddpfepgakmykTGDLAKWLADGNIEY---------AGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTA 2200
Cdd:PLN02246  403 ATAN---------------TIDKDGWLHTGDIGYiddddelfiVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVP 467

                  ...
gi 166797876 2201 RED 2203
Cdd:PLN02246  468 MKD 470
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
4947-5331 8.68e-25

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 110.35  E-value: 8.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4947 NMTGILETEGKLPLNRLLTAFQRLMQGHEPLRT--------VVEMVREEAVQViksqvefsmeRYEATADeveecFRAFV 5018
Cdd:cd19537    25 NVSFACRLSGDVDRDRLASAWNTVLARHRILRSryvprdggLRRSYSSSPPRV----------QRVDTLD-----VWKEI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5019 -RPFDLSQAPLLRaglIELEQDlhIFMFDMHHIITDGASMNIFVEKLIQLYDGKELAPLRIQYKDFTEWKHQKEQRERik 5097
Cdd:cd19537    90 nRPFDLEREDPIR---VFISPD--TLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSRPASPEDL-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5098 sqeEYWLgvfhEELPSFELPKDFARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDI 5177
Cdd:cd19537   163 ---DFWS----EYLSGLPLLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5178 VVGTPIAGRPHADLEPIIGMFVNTLAIR--TAPMAEKTFLDYITETKETMLKAFEHQeYPFEELVEKLGVKRDLSRNPLF 5255
Cdd:cd19537   236 VLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLF 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 5256 DTM--FVLQNTEQTDIEVDSLAVRpYEQTEtAAKFDLQLNFL-IDQDEIQGSFDYCTKLFKKKTIAVLAKdyvMILSAI 5331
Cdd:cd19537   315 DVMvtFHDDRGVSLALPIPGVEPL-YTWAE-GAKFPLMFEFTaLSDDSLLLRLEYDTDCFSEEEIDRIES---LILAAL 388
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
4300-4829 1.23e-24

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 112.16  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4300 AELARLNMMTKEEERdiqqlfndTAVAEKRIPTtihqLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGA 4379
Cdd:PRK06155    1 GEPLGAGLAARAVDP--------LPPSERTLPA----MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4380 CTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCAG-----HAIPPLFEG--EVLLL 4452
Cdd:PRK06155   69 KRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAllaalEAADPGDLPlpAVWLL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4453 DDPllyQGRTDNLNLSCSE---------------NDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQ 4517
Cdd:PRK06155  149 DAP---ASVSVPAGWSTAPlppldapapaaavqpGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLY 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4518 FAAMSFDVCYQEMF-SALSSGGILFIignEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEkhyfEPFAECVDHIIAA 4596
Cdd:PRK06155  226 TTLPLFHTNALNAFfQALLAGATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQ----PARESDRAHRVRV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4597 GEQL-IATRMLRDMLARHQVTLHNHYGPSETHVVtMYTVDPdtDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCIS 4675
Cdd:PRK06155  299 ALGPgVPAALHAAFRERFGVDLLDGYGSTETNFV-IAVTHG--SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLR 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4676 G---VSLARGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--V 4750
Cdd:PRK06155  376 AdepFAFATGYFGMPEKTVEAW-------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHpaV 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4751 QEAVVLAKENTDGQSDLYAYFTAE--QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALpmPEAGLQTG 4828
Cdd:PRK06155  449 AAAAVFPVPSELGEDEVMAAVVLRdgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL--REQGVTAD 526

                  .
gi 166797876 4829 T 4829
Cdd:PRK06155  527 T 527
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1791-2264 1.25e-24

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 111.71  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1791 AAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDS 1870
Cdd:PRK12406    3 ATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1871 QAGIVLMQRDVRKQLA---YEGVTVLL-----DDESSYHQDGSDLAPISD------------------VSHLAYVIYTSG 1924
Cdd:PRK12406   83 GARVLIAHADLLHGLAsalPAGVTVLSvptppEIAAAYRISPALLTPPAGaidwegwlaqqepydgppVPQPQSMIYTSG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1925 STGRPKGV-----LIEHggLTNYIWWAKEVYvkGEKANF------PLYSSI--SFDLTVTSIftplvtGNAIIVYDGEDK 1991
Cdd:PRK12406  163 TTGHPKGVrraapTPEQ--AAAAEQMRALIY--GLKPGIralltgPLYHSApnAYGLRAGRL------GGVLVLQPRFDP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1992 TALLESIVRDpRVDIIKLTPAHLQVLkeMNIADqtAVRRmivgGENLSTrLARSIH-------EQFEGRIE-----ICNE 2059
Cdd:PRK12406  233 EELLQLIERH-RITHMHMVPTMFIRL--LKLPE--EVRA----KYDVSS-LRHVIHaaapcpaDVKRAMIEwwgpvIYEY 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2060 YGPTET--VVGCMiyrYDAAKDRRESVpiGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVAR-GYLNRPELTAEKFV 2136
Cdd:PRK12406  303 YGSTESgaVTFAT---SEDALSHPGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDR 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2137 DDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYY-- 2214
Cdd:PRK12406  378 GG-------FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVep 450
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876 2215 VSGGQTTAARLRKQLSQTLASYMVPAyFIEL-DEMPLTSNGKINKKGLPAP 2264
Cdd:PRK12406  451 QPGATLDEADIRAQLKARLAGYKVPK-HIEImAELPREDSGKIFKRRLRDP 500
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
289-687 1.54e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 111.01  E-value: 1.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADvllvqh 368
Cdd:cd05910     3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPD------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 hlknslAFDGpvIDLNDEAsyhadcsllspvaghshlAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVL 448
Cdd:cd05910    77 ------AFIG--IPKADEP------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 VLYPyvfdafILNFFGPLISGATL-----HLLPNEENKEtfAIQNAIKQERITHFSTSPRLLKTMIEQMNRED--FIHVQ 521
Cdd:cd05910   131 ATFP------LFALFGPALGLTSVipdmdPTRPARADPQ--KLVGAIRQYGVSIVFGSPALLERVARYCAQHGitLPSLR 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  522 HVVVGGEQLETDTVEKLHS-LQPRIRINNEYGPTE---------NSVVSTFHPVQSADEQITIGSPVANHQAYIL----G 587
Cdd:cd05910   203 RVLSAGAPVPIALAARLRKmLSDEAEILTPYGATEalpvssigsRELLATTTAATSGGAGTCVGRPIPGVRVRIIeiddE 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  588 AHHQIQ-----PIGIPGELYVGGAGVARGYLNRPELTEekfVEHLHVPGQKM-YKTGDLARWLPDGRIEYLGRIDHQVKI 661
Cdd:cd05910   283 PIAEWDdtlelPRGEIGEITVTGPTVTPTYVNRPVATA---LAKIDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVIT 359
                         410       420
                  ....*....|....*....|....*.
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVV 687
Cdd:cd05910   360 TGGTLYTEPVERVFNTHPGVRRSALV 385
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
856-1334 2.17e-24

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 113.80  E-value: 2.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  856 QHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGTDESELFHLEVMNYKGE 935
Cdd:COG1020    26 RLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  936 TDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQLPQKT 1014
Cdd:COG1020   106 LAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLlLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1015 DSFPFWADQLSKYAAETDMEEEIAYWTE--LSSIKPQPLPKDTISEGSLLRDSEEVTIQWTKEETEQLLKQAnRAYNTDI 1092
Cdd:COG1020   186 IQYADYALWQREWLQGEELARQLAYWRQqlAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALA-RRHGVTL 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1093 NDLLLTSLGLAVHKWTGTEDIVVNLEGHGRepiiPDADISRTIGWFTSQYPVVLRMEAGKNLSQRIKIVKEGLRRI---- 1168
Cdd:COG1020   265 FMVLLAAFALLLARYSGQDDVVVGTPVAGR----PRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAyahq 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1169 ------------PDKGMnysiikyiSGHPEADSLqlkpeisFNYLGQFDQDLKHQALRISPFstglsmnENQERTAVLDL 1236
Cdd:COG1020   341 dlpferlveelqPERDL--------SRNPLFQVM-------FVLQNAPADELELPGLTLEPL-------ELDSGTAKFDL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1237 NGMIAE--GTLSLTLSYSSKQYERSTMAQFArglkESLQEVIAHCVSRQQTSLTPSDILlkdiSIDELEQLLEqtrELGE 1314
Cdd:COG1020   399 TLTVVEtgDGLRLTLEYNTDLFDAATIERMA----GHLVTLLEALAADPDQPLGDLPLL----TAAERQQLLA---EWNA 467
                         490       500
                  ....*....|....*....|
gi 166797876 1315 AENIYPLTPmqkgmLFHSLF 1334
Cdd:COG1020   468 TAAPYPADA-----TLHELF 482
PRK09088 PRK09088
acyl-CoA synthetase; Validated
4341-4818 2.55e-24

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 110.67  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4341 QAERNPDHEAV--MFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPE 4418
Cdd:PRK09088    4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4419 KRRAFMLKDSGADVLLtcaGHAIPPLFEGEVLLLDDpllYQGRTDNLNL----SCSENDLMYVIYTSGTTGQPKGVQLEH 4494
Cdd:PRK09088   84 SELDALLQDAEPRLLL---GDDAVAAGRTDVEDLAA---FIASADALEPadtpSIPPERVSLILFTSGTSGQPKGVMLSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4495 KTmtnllayeQDHTQLRFDRVLQFAAMSFDVCYQEMF----------SALSSGG-ILFIIGNEAKRDIRQLND--FVRTH 4561
Cdd:PRK09088  158 RN--------LQQTAHNFGVLGRVDAHSSFLCDAPMFhiiglitsvrPVLAVGGsILVSNGFEPKRTLGRLGDpaLGITH 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4562 GI-----------QTAFLPTAFLKLLAsekhyfepfaecvdhIIAAGEQLIATRmLRDMLARhQVTLHNHYGPSETHVVT 4630
Cdd:PRK09088  230 YFcvpqmaqafraQPGFDAAALRHLTA---------------LFTGGAPHAAED-ILGWLDD-GIPMVDGFGMSEAGTVF 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4631 MYTVDPDT-DQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpydSNQRMYKTG 4709
Cdd:PRK09088  293 GMSVDCDViRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4710 DLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVLAKENTDGQSDLYAYFTAEQS-LSISQLKEK 4785
Cdd:PRK09088  367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHpgiRECAVVGMADAQWGEVGYLAIVPADGApLDLERIRSH 446
                         490       500       510
                  ....*....|....*....|....*....|...
gi 166797876 4786 LAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK09088  447 LSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK07787 PRK07787
acyl-CoA synthetase; Validated
4349-4822 2.82e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 110.08  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4349 EAVMFGNQTLTYRQLNERSNQLARVLQDKGActdqvVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDS 4428
Cdd:PRK07787   17 DAVRIGGRVLSRSDLAGAATAVAERVAGARR-----VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4429 GADVLLtcaghAIPPlfEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHT 4508
Cdd:PRK07787   92 GAQAWL-----GPAP--DDPAGLPHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4509 QLRFDRVLQFAAMSFDVcyqemfsalsSGGILFIIGNeakrdIRQLNDFVRThgiqTAFLPTAFLKLLASEKH-YFE-Pf 4586
Cdd:PRK07787  165 QWTADDVLVHGLPLFHV----------HGLVLGVLGP-----LRIGNRFVHT----GRPTPEAYAQALSEGGTlYFGvP- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4587 aeCVDHIIA----AGEQLIATRML-----------RDMLAR---HQVTlhNHYGPSEThvvtMYTVDPDTDQELQP--IG 4646
Cdd:PRK07787  225 --TVWSRIAadpeAARALRGARLLvsgsaalpvpvFDRLAAltgHRPV--ERYGMTET----LITLSTRADGERRPgwVG 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4647 KPISNTEIFILNEAGTLQPVG--IVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPEGNIEYAG 4724
Cdd:PRK07787  297 LPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVG 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4725 RRDHQ-VKIRGYRVELGEVEAALLKH--VQEAVVLAKENTD-GQSdLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFI 4800
Cdd:PRK07787  371 RESTDlIKSGGYRIGAGEIETALLGHpgVREAAVVGVPDDDlGQR-IVAYVVGADDVAADELIDFVAQQLSVHKRPREVR 449
                         490       500
                  ....*....|....*....|..
gi 166797876 4801 QLEKLPLTGNGKVNRRALPMPE 4822
Cdd:PRK07787  450 FVDALPRNAMGKVLKKQLLSEG 471
PRK13382 PRK13382
bile acid CoA ligase;
1779-2264 3.42e-24

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 111.00  E-value: 3.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1779 LFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY 1858
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 PQDRIRYMLDDSQAGIVLMQRD----VRKQLA-YEGVTVLLDDESSYHQDGSD--------LAPISDVSHLAYVIYTSGS 1925
Cdd:PRK13382  128 AGPALAEVVTREGVDTVIYDEEfsatVDRALAdCPQATRIVAWTDEDHDLTVEvliaahagQRPEPTGRKGRVILLTSGT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1926 TGRPKGVliEHGGLTNYI----------WWAKEVYVKGEkanfPLYSSISFD--LTVTSIFTPLVTGNAiivYDGEDKTA 1993
Cdd:PRK13382  208 TGTPKGA--RRSGPGGIGtlkaildrtpWRAEEPTVIVA----PMFHAWGFSqlVLAASLACTIVTRRR---FDPEATLD 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1994 LLESivrdPRVDIIKLTPAHLQVLKE-----MNIADQTAVRRMIVGGENLSTRLARSIHEQFeGRIeICNEYGPTEtvVG 2068
Cdd:PRK13382  279 LIDR----HRATGLAVVPVMFDRIMDlpaevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF-GDV-IYNNYNATE--AG 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2069 cMIYRYDAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYlnrpelTAEKfvDDPFEPGakMYK 2148
Cdd:PRK13382  351 -MIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TSGS--TKDFHDG--FMA 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2149 TGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLR 2226
Cdd:PRK13382  420 SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlkPGASATPETLK 499
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 166797876 2227 KQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPAP 2264
Cdd:PRK13382  500 QHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3921-4197 4.30e-24

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 108.73  E-value: 4.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3921 LDRDKLQQAFRTLILRHESLRTGFkMADGEpvQYVLDHAAfeaeWYQ--------GEEDDADLYIRQfIRP------FHL 3986
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRAVF-LDDGT--QQILPEVP----WYGitvhdlrgLSEEEAEAALEE-LRErlshrvLDV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3987 DEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYE--GETLPPLRIQYKDYaVWQTGEARLQQIQKQEA 4064
Cdd:cd19535   109 ERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPLPPLELSFRDY-LLAEQALRETAYERARA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4065 YWLE----LYSGdvPVLHLPADYIRPSARDFAgaTMHFTLDKQKSDGLKQLASQTESTLYMVLLASYTLLLSKYSGQEDI 4140
Cdd:cd19535   188 YWQErlptLPPA--PQLPLAKDPEEIKEPRFT--RREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRF 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 4141 IVGSPIAGRP--HADLEPIIGMFVNT--LAMRnyPEKGKTFSQYLSEVKENALKAYEHQDY 4197
Cdd:cd19535   264 LLNLTLFNRLplHPDVNDVVGDFTSLllLEVD--GSEGQSFLERARRLQQQLWEDLDHSSY 322
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1774-2263 5.56e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 110.09  E-value: 5.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1774 TPVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVP 1853
Cdd:PRK13383   35 TNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1854 IDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHlAYVIYTSGSTGRPKGV- 1932
Cdd:PRK13383  115 ISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGVp 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1933 ----LIEHGGLTNYIWWAKEVYVkGEKANF--PLYSSISFDLTVTSIftplVTGNAIIVYDGEDKTALLESIVRDpRVDI 2006
Cdd:PRK13383  194 rapqLRSAVGVWVTILDRTRLRT-GSRISVamPMFHGLGLGMLMLTI----ALGGTVLTHRHFDAEAALAQASLH-RADA 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2007 IKLTPAHLQVLkeMNIADQTAVRR-------MIVGGENLSTRLARSIHEQFeGRIeICNEYGPTETVVGCMIYRYDaAKD 2079
Cdd:PRK13383  268 FTAVPVVLARI--LELPPRVRARNplpqlrvVMSSGDRLDPTLGQRFMDTY-GDI-LYNGYGSTEVGIGALATPAD-LRD 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2080 RRESVpiGTAAANTSIYVLDENMKPAPIGVPGEIYISGagvargylnrpELTAEKFVDDpfepGAK-----MYKTGDLAK 2154
Cdd:PRK13383  343 APETV--GKPVAGCPVRILDRNNRPVGPRVTGRIFVGG-----------ELAGTRYTDG----GGKavvdgMTSTGDMGY 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2155 WLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVS--GGQTTAARLRKQLSQT 2232
Cdd:PRK13383  406 LDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLhpGSGVDAAQLRDYLKDR 485
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876 2233 LASYMVPAYFIELDEMPLTSNGKINKKGLPA 2263
Cdd:PRK13383  486 VSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
3290-3781 5.95e-24

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 109.56  E-value: 5.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3290 EEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAK-GVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSP 3368
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3369 SERIRYILNDSSISVLLYCGKLQDDI----GFSGTC----IDLMEEHFYHEKDSslaLSYQSSQLAYAI-YTSGTTGKPK 3439
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTFQNMAlsmqKVSYVQrvisITSLKEIEDRKIDN---FVEKNESASFIIcYTSGTTGKPK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3440 GTLIEHRQVI-HLIEGLSRQVYSAYDaeLNIAMLAPYYFDASVQQMYASLLSGHTLfIVPKEIVSDGAAlcRYYRQHSID 3518
Cdd:PRK06839  166 GAVLTQENMFwNALNNTFAIDLTMHD--RSIVLLPLFHIGGIGLFAFPTLFAGGVI-IVPRKFEPTKAL--SMIEKHKVT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3519 ITDGTPAHLKLLIAAGDLQGVTLQHLLI---GGEALSKttvnKLKQLFGEHGAAPGitNVYGPTETCvdASLFNIecSSD 3595
Cdd:PRK06839  241 VVMGVPTIHQALINCSKFETTNLQSVRWfynGGAPCPE----ELMREFIDRGFLFG--QGFGMTETS--PTVFML--SEE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3596 AWARSQNyvPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARL 3675
Cdd:PRK06839  311 DARRKVG--SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-------QDGWLCTGDLARV 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3676 LPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISE--LRKRMARHL 3753
Cdd:PRK06839  382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkdVIEHCRLFL 461
                         490       500
                  ....*....|....*....|....*...
gi 166797876 3754 PGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK06839  462 AKYKIPKEIVFLKELPKNATGKIQKAQL 489
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
407-747 6.45e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 107.08  E-value: 6.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  407 YVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPAD--------------RVLVLYPYVFDAFILNFFGPLISGATL 472
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaagtVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  473 HLLPNEENKEtfAIQNAIKQERITHFS-TSPRLLKTMIEQMNRE---DFIHVQHVVVGGEQLETDTVEKLHSLQPRIRIN 548
Cdd:cd05924    87 VLPDDRFDPE--EVWRTIEKHKVTSMTiVGDAMARPLIDALRDAgpyDLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  549 NEYGPTENSVVSTFHPVQSADEqiTIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAG-VARGYLNRPELTEEKFVEhl 627
Cdd:cd05924   165 DAFGSSETGFTGSGHSAGSGPE--TGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAETFPE-- 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  628 hVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP- 706
Cdd:cd05924   241 -VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREg 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 166797876  707 -SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLK 747
Cdd:cd05924   320 aGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
408-744 7.95e-24

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 106.05  E-value: 7.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 VIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYvFDAF--ILNFFGPLISGATlhLLPnEENKETFA 485
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF-FHTFgyKAGIVACLLTGAT--VVP-VAVFDVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  486 IQNAIKQERITHFSTSPRLLKTMIEQMNREDF--IHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFH 563
Cdd:cd17638    81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFdlSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMCR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  564 PVQSA-DEQITIGSPVANHQAYILGahhqiqpigiPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGDL 640
Cdd:cd17638   161 PGDDAeTVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADgwLH--------TGDV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  641 ARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQfrEEL--- 717
Cdd:cd17638   223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTE--EDViaw 300
                         330       340
                  ....*....|....*....|....*...
gi 166797876  718 SRE-LPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd17638   301 CRErLANYKVPRFVRFLDELPRNASGKV 328
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
3293-3713 9.68e-24

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 109.25  E-value: 9.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVV--FEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSE 3370
Cdd:cd05904    15 ASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3371 RIRYILNDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQS-----------SQLAYAIYTSGTTGKPK 3439
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADeaeppvvvikqDDVAALLYSSGTTGRSK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3440 GTLIEHRQVIHLIEGLSRQVYSAYDAELNIAMLAP----YYFDASvqqMYASLLSGHTLFIVPK-EIVSDGAALCRYyrq 3514
Cdd:cd05904   175 GVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPmfhiYGLSSF---ALGLLRLGATVVVMPRfDLEELLAAIERY--- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3515 hsiDITDGT---PAHLKL----LIAAGDLQgvTLQHLLIGGEALSKTTVNKLKQLFGehgaapgitNV-----YGPTE-T 3581
Cdd:cd05904   249 ---KVTHLPvvpPIVLALvkspIVDKYDLS--SLRQIMSGAAPLGKELIEAFRAKFP---------NVdlgqgYGMTEsT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3582 CVDASLFNIECSSdawarsQNYVPIGKPLGRNRMYILD-SKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpf 3660
Cdd:cd05904   315 GVVAMCFAPEKDR------AKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID---- 384
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876 3661 vpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:cd05904   385 --KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEI 435
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
1775-2342 1.06e-23

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 110.95  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1775 PVHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI 1854
Cdd:COG3319     2 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVT--VLLDDESSYHQDGSDLAPISDVSH---LAYVIYTSGSTGRP 1929
Cdd:COG3319    82 AALALALAAAAAALLLAALALLLALLAALALALLALLlaALLLALAALAAAAAAAALAAAAAAaaaLAAAAGLGGGGGGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1930 KGVLIEHGGLTNYIWWAKEVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDGEDKTALLESIVRDPRVDIIKL 2009
Cdd:COG3319   162 GVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2010 TPAHLQVLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCMIYRYDAAKDRRESVPIGTA 2089
Cdd:COG3319   242 LLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2090 AANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEPGA--KMYKTGDLAKWLADGNIEYAGRI 2167
Cdd:COG3319   322 PGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGArgRLRRGGDRGRRLGGGLLLGLGRL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2168 DEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGfKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDE 2247
Cdd:COG3319   402 RLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAA-AAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2248 MPLTSNGKINKKGLPAPDFELQDRAEYKAPRTKAEEILVSAWESVLGAENVSILDNFFDLGGDSIKSIQVSSRLNQQGYK 2327
Cdd:COG3319   481 LLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLR 560
                         570
                  ....*....|....*
gi 166797876 2328 MEIKDLFQYATIAEL 2342
Cdd:COG3319   561 LLLLLALLLAPTLAA 575
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
4331-4756 1.10e-23

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 109.80  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4331 PTTIHQLFEQQAERNPDHEAVMF----GNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAG 4406
Cdd:COG1022    10 ADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4407 AAFLPIDPELPEKRRAFMLKDSGADVL----------LTCAGHAIPPL-----FEGEVLLLDDPLLY------QGRT--- 4462
Cdd:COG1022    90 AVTVPIYPTSSAEEVAYILNDSGAKVLfvedqeqldkLLEVRDELPSLrhivvLDPRGLRDDPRLLSldellaLGREvad 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4463 ----DNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLA-----------YEQD---------HTqlrFDRVLQF 4518
Cdd:COG1022   170 paelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHR---NLLSnarallerlplGPGDrtlsflplaHV---FERTVSY 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4519 AAMS--FDVCYQE--------------------------MFSALSSGgilfiiGNEAKRDIRQLNDFVRTHGIQTAFL-- 4568
Cdd:COG1022   244 YALAagATVAFAEspdtlaedlrevkptfmlavprvwekVYAGIQAK------AEEAGGLKRKLFRWALAVGRRYARArl 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4569 ----PTAFLKLLAS--EKHYFEPFAE----CVDHIIAAGEQL---IAtRMLRDMlarhQVTLHNHYGPSETHVVTmyTVD 4635
Cdd:COG1022   318 agksPSLLLRLKHAlaDKLVFSKLREalggRLRFAVSGGAALgpeLA-RFFRAL----GIPVLEGYGLTETSPVI--TVN 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4636 PDTDQELQPIGKPISNTEIFILNEagtlqpvgivGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYL 4715
Cdd:COG1022   391 RPGDNRIGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELD 454
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 166797876 4716 PEGNIEYAGRRDHQVKIR-GYRVELGEVEAALLKH--VQEAVVL 4756
Cdd:COG1022   455 EDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASplIEQAVVV 498
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1320-1741 1.31e-23

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 107.51  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNF-YRGwkDQPLQIIFKTKKIGFQF 1398
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFpEDD--GGPYQVVLPAAEARPDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1399 nDLREMKESQKEAMIQKYARedkmRGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQQ 1478
Cdd:cd19540    81 -TVVDVTEDELAARLAEAAR----RGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1479 KQPEQssiTP----YSQYI----EWLGRQDAKEAA-----AYWDQYLEGYEEQTGLPKDHHAAEDGRYVPEKVTCDISSD 1545
Cdd:cd19540   156 RAPDW---APlpvqYADYAlwqrELLGDEDDPDSLaarqlAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1546 LTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSGRpaGIPNVETMIGLFINTIPVRFRCEAGTTFAELM 1625
Cdd:cd19540   233 LHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGR--GDEALDDLVGMFVNTLVLRTDVSGDPTFAELL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1626 KEAQER---AVASQK--FET-------------HPLYdiQArttqkqdlithLMIFENYPVDQymesiGRQNGTSITISN 1687
Cdd:cd19540   311 ARVRETdlaAFAHQDvpFERlvealnpprstarHPLF--QV-----------MLAFQNTAAAT-----LELPGLTVEPVP 372
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 1688 VQMeEQTNYD--FNLTVIPGDE-----MNISFEYNANVYERASIERVREHFMQILHQVVTD 1741
Cdd:cd19540   373 VDT-GVAKFDlsFTLTERRDADgapagLTGELEYATDLFDRSTAERLADRFVRVLEAVVAD 432
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
3309-3713 1.31e-23

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 108.91  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3309 FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDP----DSPSERIRYILN------- 3377
Cdd:cd05906    40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARLRKLRHiwqllgs 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3378 ------DSSISVLLYCGKLQDDIGFSGTCIDLMEEHfyhekdSSLALSYQSS--QLAYAIYTSGTTGKPKGTLIEHRQVI 3449
Cdd:cd05906   120 pvvltdAELVAEFAGLETLSGLPGIRVLSIEELLDT------AADHDLPQSRpdDLALLMLTSGSTGFPKAVPLTHRNIL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3450 HLIEGLSR-QVYSAYDAELN---------IAMLapyyfdaSVQQMYaslLSGHTLFIVPKEIVSDGAALCRYYRQHSIDI 3519
Cdd:cd05906   194 ARSAGKIQhNGLTPQDVFLNwvpldhvggLVEL-------HLRAVY---LGCQQVHVPTEEILADPLRWLDLIDRYRVTI 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3520 TDGTPAHLKLLIAA--------GDLQGvtLQHLLIGGEALSKTTVNKLKQLFGEHGAAP-GITNVYGPTETCvDASLFNI 3590
Cdd:cd05906   264 TWAPNFAFALLNDLleeiedgtWDLSS--LRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdAIRPAFGMTETC-SGVIYSR 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3591 ECSSDAWARSQNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpfvpEDRMYRTG 3670
Cdd:cd05906   341 SFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFT------EDGWFRTG 414
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 166797876 3671 DLArLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:cd05906   415 DLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456
PRK06145 PRK06145
acyl-CoA synthetase; Validated
3293-3781 1.50e-23

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 108.43  E-value: 1.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERI 3372
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3373 RYILNDSSISVLLYCGKLQDDIGFsGTCIDLMEEHfyHEKDSS-LALSYQSSQLAYA---------IYTSGTTGKPKGTL 3442
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVAL-ETPKIVIDAA--AQADSRrLAQGGLEIPPQAAvaptdlvrlMYTSGTTDRPKGVM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3443 IEH-----RQVIHLIE-GLSrqvysaydAELNIAMLAP-YYFDASVQQMYASLLSGHTLFIvpkEIVSDGAALCRYYRQH 3515
Cdd:PRK06145  169 HSYgnlhwKSIDHVIAlGLT--------ASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRI---HREFDPEAVLAAIERH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3516 SIDITDGTPAHLKLLIAAGDLQGVTLQHL---LIGGEalsKTTVNKLKQlFGEHGAAPGITNVYGPTETCVDASLFniec 3592
Cdd:PRK06145  238 RLTCAWMAPVMLSRVLTVPDRDRFDLDSLawcIGGGE---KTPESRIRD-FTRVFTRARYIDAYGLTETCSGDTLM---- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3593 ssDAWARSQNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmyRTGDL 3672
Cdd:PRK06145  310 --EAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDV 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3673 ARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCG--YFAADKTIQISELRKRMA 3750
Cdd:PRK06145  381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAvvVLNPGATLTLEALDRHCR 460
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876 3751 RHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK06145  461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
4333-4818 2.27e-23

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 108.31  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKG-ACTDQVVAVLTDRsAHMIIGILAILKAGAafLP 4411
Cdd:COG1021    26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGlRPGDRVVVQLPNV-AEFVIVFFALFRAGA--IP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4412 IDPeLPEKRRA---FMLKDSGADVLLTCAGHA--------------IPPLfeGEVLLLDDP-------LLYQGRTDNLNL 4467
Cdd:COG1021   103 VFA-LPAHRRAeisHFAEQSEAVAYIIPDRHRgfdyralarelqaeVPSL--RHVLVVGDAgeftsldALLAAPADLSEP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4468 SCSENDLMYVIYTSGTTGQPKGVQLEH-------KTMTNLLAYEQDHTQLrfdrVLQFAAMSFDVCYQEMFSALSSGGIL 4540
Cdd:COG1021   180 RPDPDDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEICGLDADTVYL----AALPAAHNFPLSSPGVLGVLYAGGTV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4541 FIIGNEAKRDIRQLndfVRTHGI-QTAFLPTAFLKLLasekhyfepfaecvDHIIAAGEQLIATRMLR-------DMLAR 4612
Cdd:COG1021   256 VLAPDPSPDTAFPL---IERERVtVTALVPPLALLWL--------------DAAERSRYDLSSLRVLQvggaklsPELAR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4613 hQV------TLHNHYGPSETHVvtMYTvDPDTDQELQ--PIGKPIS-NTEIFILNEAGTLQPVGIVGELCISGVSLARGY 4683
Cdd:COG1021   319 -RVrpalgcTLQQVFGMAEGLV--NYT-RLDDPEEVIltTQGRPISpDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4684 -----HNRESLTLETFvphpydsnqrmYKTGDLARYLPEGNIEYAGRRDHQVkIRGyrvelGE------VEAALLKH--V 4750
Cdd:COG1021   395 yrapeHNARAFTPDGF-----------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHpaV 457
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 4751 QEAVVLAkentdgQSDLY------AYFTA-EQSLSISQLKEKLAGQ-IPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:COG1021   458 HDAAVVA------MPDEYlgerscAFVVPrGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4479-4815 2.92e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 105.05  E-value: 2.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4479 YTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLR-FDRVlqfaamsfdVCYQEMFSALSSggilfIIGNEAkrdirqlndf 4557
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTeQDRL---------CIPVPLFHCFGS-----VLGVLA---------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4558 VRTHG-----IQTAFLPTAFLKLLASEK---HYFEP--FAECVDHI-------------IAAG----EQLIaTRMLRDMl 4610
Cdd:cd05917    65 CLTHGatmvfPSPSFDPLAVLEAIEKEKctaLHGVPtmFIAELEHPdfdkfdlsslrtgIMAGapcpPELM-KRVIEVM- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4611 arHQVTLHNHYGPSETH-VVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQP-VGIVGELCISGVSLARGYHNRES 4688
Cdd:cd05917   143 --NMKDVTIAYGMTETSpVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4689 LTLETFvphpydSNQRMYKTGDLARYLPEGNIEYAGR-RDhqVKIRGyrvelG------EVEAALLKH--VQEA-VVLAK 4758
Cdd:cd05917   221 KTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRiKD--MIIRG-----GeniyprEIEEFLHTHpkVSDVqVVGVP 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 4759 ENTDGQsDLYAY--FTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd05917   288 DERYGE-EVCAWirLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1756-2260 4.10e-23

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 108.21  E-value: 4.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1756 ERR---TLLQTLNDTAAPFPQTPVHQLfEEQSQRTPDQAAVIDKD------RQLTYGELNKRANRLARTLRAKGVQTDQP 1826
Cdd:PRK12582   29 ERRadgSIVIKSRHPLGPYPRSIPHLL-AKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1827 VAIITRNSIESVVGILAVLKSGGAYVPIDPEY---PQD--RIRYMLDDSQAGIVLMQRDV-----RKQLAYEGVTVLL-- 1894
Cdd:PRK12582  108 VMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQSGApfaraLAALDLLDVTVVHvt 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1895 ---DDESSYHQDgsDLA--PISD--------VSH--LAYVIYTSGSTGRPKGVLIEHGGLTNYIwwAKEVYVKGEKANFP 1959
Cdd:PRK12582  188 gpgEGIASIAFA--DLAatPPTAavaaaiaaITPdtVAKYLFTSGSTGMPKAVINTQRMMCANI--AMQEQLRPREPDPP 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1960 LysSISFD-------LTVTSIFTP-LVTGNAIIVYDGEDKTALLESIVRDPRvDIIKLT----PAHLQVLKEMNIADQtA 2027
Cdd:PRK12582  264 P--PVSLDwmpwnhtMGGNANFNGlLWGGGTLYIDDGKPLPGMFEETIRNLR-EISPTVygnvPAGYAMLAEAMEKDD-A 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2028 VRR--------MIVGGENLS----TRL-ARSIHEQFEgRIEICNEYGPTETV-VGCMIYrYDAakdRRESVpIGTAAANT 2093
Cdd:PRK12582  340 LRRsffknlrlMAYGGATLSddlyERMqALAVRTTGH-RIPFYTGYGATETApTTTGTH-WDT---ERVGL-IGLPLPGV 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2094 SiyvldenMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGN----IEYAGRIDE 2169
Cdd:PRK12582  414 E-------LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVDPDDpekgLIFDGRVAE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2170 QVKI-RGYRIELGEIEAALLQ--EEVIKEAVVTARE----------DVHGFKQLCA-YYVSGGQTTA-----ARLRKQLS 2230
Cdd:PRK12582  481 DFKLsTGTWVSVGTLRPDAVAacSPVIHDAVVAGQDrafigllawpNPAACRQLAGdPDAAPEDVVKhpavlAILREGLS 560
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 166797876 2231 QTLASymVP------AYFIELDEMPLTSNGKINKKG 2260
Cdd:PRK12582  561 AHNAE--AGgsssriARALLMTEPPSIDAGEITDKG 594
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1915-2256 4.91e-23

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 103.64  E-value: 4.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1915 HLAYVIYTSGSTGRPKGVL-IEHGGLTNYIWWAKEVYVKGEK---ANFPLyssiSFDLTVTSIFTPLVTGNAIIVYDGED 1990
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYrSERSWIESFVCNEDLFNISGEDailAPGPL----SHSLFLYGAISALYLGGTFIGQRKFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1991 KTALLESIVRDPRVDIIkLTPAHLQVLKEMNIADqTAVRRMIVGGENLSTRLARSIHEQFEgRIEICNEYGPTETvvGCM 2070
Cdd:cd17633    77 PKSWIRKINQYNATVIY-LVPTMLQALARTLEPE-SKIKSIFSSGQKLFESTKKKLKNIFP-KANLIEFYGTSEL--SFI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2071 IYRYDAAKDRRESVpiGTAAANTSIYVLDENMkpapiGVPGEIYISGAGVARGYLNRPELTAEKFvddpfepgakmYKTG 2150
Cdd:cd17633   152 TYNFNQESRPPNSV--GRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2151 DLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDvHGFKQLCAYYVSGGQTTAARLRKQLS 2230
Cdd:cd17633   214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPD-ARFGEIAVALYSGDKLTYKQLKRFLK 292
                         330       340
                  ....*....|....*....|....*.
gi 166797876 2231 QTLASYMVPAYFIELDEMPLTSNGKI 2256
Cdd:cd17633   293 QKLSRYEIPKKIIFVDSLPYTSSGKI 318
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
265-752 5.20e-23

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 107.96  E-value: 5.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  265 VYQLFEEQAERTPENAAVKFKNDH-----LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGA 339
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  340 YVPLDPEYPKERLQYLLHDADADVLLVQhhlkNSLAFDGPVIDLNDEA-SYHADCSLLSPVAGHSHLAY----------- 407
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITA----DGFTRRGREVNLKEEAdKACAQCPTVEKVVVVRHLGNdftpakgrdls 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 ----------------------VIYTSGTTGKPKGVMVEHGGivnsLQWKKAF-----FKHSPADRVL-------VLYPY 453
Cdd:cd05968   219 ydeeketagdgaertesedplmIIYTSGTTGKPKGTVHVHAG----FPLKAAQdmyfqFDLKPGDLLTwftdlgwMMGPW 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  454 VfdafilnFFGPLISGATLHL---LPNEENKETfaIQNAIKQERITHFSTSPRLLKTMI----EQMNREDFIHVQHVVVG 526
Cdd:cd05968   295 L-------IFGGLILGATMVLydgAPDHPKADR--LWRMVEDHEITHLGLSPTLIRALKprgdAPVNAHDLSSLRVLGST 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  527 GEQLETDTVEKL--HSLQPRIRINNEYGPTE-------NSVVSTFHPvqsadeqITIGSPVANHQAYILgaHHQIQPI-G 596
Cdd:cd05968   366 GEPWNPEPWNWLfeTVGKGRNPIINYSGGTEisggilgNVLIKPIKP-------SSFNGPVPGMKADVL--DESGKPArP 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  597 IPGELYVGGA--GVARGYLNrpelTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAA 674
Cdd:cd05968   437 EVGELVLLAPwpGMTRGFWR----DEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESV 512
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  675 MFNLENVREAAVVAREDADGAKQLYAYYVGEPSLT-AAQFREEL----SRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05968   513 LNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTpTEALAEELmervADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592

                  ...
gi 166797876  750 PAA 752
Cdd:cd05968   593 RAA 595
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3280-3771 5.34e-23

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 107.14  E-value: 5.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3280 PREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA 3359
Cdd:PRK06164    7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3360 YLPIDPDSPSERIRYILNDSSISVLLY---------CGKLQD---------------DIGFS-------GTCIDLMEEHF 3408
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGRARWLVVwpgfkgidfAAILAAvppdalpplraiavvDDAADatpapapGARVQLFALPD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3409 YHEKDSSLALSYQSSQLAYAIYTSGTTGKPKgtLIEHRQVIHLIEGlsRQVYSAYDAELNIAMLA--PYYFDASVQQMYA 3486
Cdd:PRK06164  167 PAPPAAAGERAADPDAGALLFTTSGTTSGPK--LVLHRQATLLRHA--RAIARAYGYDPGAVLLAalPFCGVFGFSTLLG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3487 SLLSGHTLFIVPkeiVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGvTLQHLLIGGEALSKTTVNKLKQLFGEH 3566
Cdd:PRK06164  243 ALAGGAPLVCEP---VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLFGFASFAPALGELAALARAR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3567 GAApgITNVYGPTEtcVDAsLFNIECSSDAWarSQNYVPIGKPL-GRNRMYILDSKK-RLQPKGVQGELYIAGDGVGRGY 3644
Cdd:PRK06164  319 GVP--LTGLYGSSE--VQA-LVALQPATDPV--SVRIEGGGRPAsPEARVRARDPQDgALLPDGESGEIEIRAPSLMRGY 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3645 LNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIqeaaaaalkda 3724
Cdd:PRK06164  392 LDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGV----------- 454
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 3725 ddeyYLCGYFAAD---KTIQIS-------------ELRKRMARHLPGYMIPAHFVQLDKMPLT 3771
Cdd:PRK06164  455 ----AAAQVVGATrdgKTVPVAfviptdgaspdeaGLMAACREALAGFKVPARVQVVEAFPVT 513
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
4333-4818 6.12e-23

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 106.69  E-value: 6.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGN-----QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGA 4407
Cdd:PRK08008    8 HLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4408 AFLPIDPELPEKRRAFMLKDSGADVLLTCAghAIPPLFEgEVLLLDDPLLYQ------------GRTDNLNL-------- 4467
Cdd:PRK08008   88 IMVPINARLLREESAWILQNSQASLLVTSA--QFYPMYR-QIQQEDATPLRHicltrvalpaddGVSSFTQLkaqqpatl 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4468 ----SCSENDLMYVIYTSGTTGQPKGVQLEHktmTNLL---AYEQDHTQLRFDRVLQFAAMSFDVCYQ--EMFSALSSGG 4538
Cdd:PRK08008  165 cyapPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRfagYYSAWQCALRDDDVYLTVMPAFHIDCQctAAMAAFSAGA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4539 ILFIIGN-EAKRDIRQLNDF-----------VRTHGIQTAfLPTA----------FLKLLASEKHYFEpfaecvdhiiaa 4596
Cdd:PRK08008  242 TFVLLEKySARAFWGQVCKYratitecipmmIRTLMVQPP-SANDrqhclrevmfYLNLSDQEKDAFE------------ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4597 geqliatrmlrdmlARHQVTLHNHYGPSEThVVTMYTvDPDTDQELQP-IGKPISNTEIFILNEAGTLQPVGIVGELCIS 4675
Cdd:PRK08008  309 --------------ERFGVRLLTSYGMTET-IVGIIG-DRPGDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIK 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4676 GV---SLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--V 4750
Cdd:PRK08008  373 GVpgkTIFKEYYLDPKATAKVLEADGW------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHpkI 446
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4751 QEAVVLAKENT--DGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK08008  447 QDIVVVGIKDSirDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1798-2236 7.32e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 105.62  E-value: 7.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGivlm 1877
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPD---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1878 qrdvrkqlAYEGVTVLLDDessyhqdgsdlapisdvshlAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVY--VKGEK 1955
Cdd:cd05910    77 --------AFIGIPKADEP--------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYgiRPGEV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1956 --ANFPLYSSISFDLTVTSIFTPLVTGNAIIVydgeDKTALLESIvRDPRVDIIKLTPAHLQVLKEMNIADQ---TAVRR 2030
Cdd:cd05910   129 dlATFPLFALFGPALGLTSVIPDMDPTRPARA----DPQKLVGAI-RQYGVSIVFGSPALLERVARYCAQHGitlPSLRR 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2031 MIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCMIYRYD------AAKDRRESVPIGTAAANTSIYVLD----- 2099
Cdd:cd05910   204 VLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSSIGSREllatttAATSGGAGTCVGRPIPGVRVRIIEiddep 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2100 ----ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEpgAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRG 2175
Cdd:cd05910   284 iaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSE--GFWHRMGDLGYLDDEGRLWFCGRKAHRVITTG 361
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 2176 YRIELGEIEAALLQ-EEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASY 2236
Cdd:cd05910   362 GTLYTEPVERVFNThPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
852-1278 7.94e-23

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 104.98  E-value: 7.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  852 LTPIQ-----HWFFEqkmPHAHHYNQAvMLYSAEG-FKEGPLRRTMERIASHHDALRMIFEKTPDG------YAPRITGT 919
Cdd:cd19543     4 LSPMQegmlfHSLLD---PGSGAYVEQ-MVITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEGLGeplqvvLKDRKLPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  920 DESELFHLevmnykGETDPAQAIAD-KANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFAS 997
Cdd:cd19543    80 RELDLSHL------SEAEQEAELEAlAEEDRERGFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKELFA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  998 GYEQAERRQTIQLPQKTdsfPFwadqlSKYAA---ETDMEEEIAYWTE-LSSIK-PQPLPKDTISEGSLLRDSEEVTIQW 1072
Cdd:cd19543   154 IYAALGEGQPPSLPPVR---PY-----RDYIAwlqRQDKEAAEAYWREyLAGFEePTPLPKELPADADGSYEPGEVSFEL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1073 TKEETEQLLKQAnRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPdaDISRTIGWFTSQYPVVLRMEAGK 1152
Cdd:cd19543   226 SAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELP--GIETMVGLFINTLPVRVRLDPDQ 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1153 NLSQRIKIV-KEGLRRIPDKGMNYSIIKYISGHPEA--DSLqlkpeISF-NY-LGQFDQDLKHQ-ALRISPFStglsmne 1226
Cdd:cd19543   303 TVLELLKDLqAQQLELREHEYVPLYEIQAWSEGKQAlfDHL-----LVFeNYpVDESLEEEQDEdGLRITDVS------- 370
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876 1227 NQERTAvLDLNGMIAEG-TLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAH 1278
Cdd:cd19543   371 AEEQTN-YPLTVVAIPGeELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
4350-4818 8.69e-23

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 105.25  E-value: 8.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4350 AVMFGNQTLTYRQLNERSNQLARVLQDKGAC-TDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDS 4428
Cdd:cd05958     3 CLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4429 GADVLLtCAGHaipplfegevlllddpllyqgrtdnlnLSCSEnDLMYVIYTSGTTGQPKGVQLEHKTM--------TNL 4500
Cdd:cd05958    83 RITVAL-CAHA---------------------------LTASD-DICILAFTSGTTGAPKATMHFHRDPlasadryaVNV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4501 LAYEQDhtqlrfDRVLQFAAMSFdvcyqemfsALSSGGIL---FIIGNEA----KRDIRQLNDFVRTHGIQTAF-LPTAF 4572
Cdd:cd05958   134 LRLRED------DRFVGSPPLAF---------TFGLGGVLlfpFGVGASGvlleEATPDLLLSAIARYKPTVLFtAPTAY 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4573 LKLLASeKHYFEPFAECVDHIIAAGEQLIAT--RMLRDMLArhqVTLHNHYGPSET-HVvtMYTVDPDtdqELQP--IGK 4647
Cdd:cd05958   199 RAMLAH-PDAAGPDLSSLRKCVSAGEALPAAlhRAWKEATG---IPIIDGIGSTEMfHI--FISARPG---DARPgaTGK 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4648 PISNTEIFILNEAGTLQPVGIVGELCISGVSlarGYHnresltletfvpHPYDSNQRMY------KTGDLARYLPEGNIE 4721
Cdd:cd05958   270 PVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCR------------YLADKRQRTYvqggwnITGDTYSRDPDGYFR 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4722 YAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYF-----TAEQSLSISQLKEKLAGQIPGYM 4794
Cdd:cd05958   335 HQGRSDDMIVSGGYNIAPPEVEDVLLQHpaVAECAVVGHPDESRGVVVKAFVvlrpgVIPGPVLARELQDHAKAHIAPYK 414
                         490       500
                  ....*....|....*....|....
gi 166797876 4795 IPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05958   415 YPRAIEFVTELPRTATGKLQRFAL 438
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1797-2258 1.18e-22

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 105.13  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1797 DRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVL 1876
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 MQRdvrkqlayegvtvllddessyhqdgsdlapisdvshlAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKevYVKGEKA 1956
Cdd:cd05940    81 VDA-------------------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFA--GSGGALP 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1957 N------FPLYSSISfdLTVtSIFTPLVTGNA----------------------IIVYDGEdktaLLESIVRDPRVDIIK 2008
Cdd:cd05940   122 SdvlytcLPLYHSTA--LIV-GWSACLASGATlvirkkfsasnfwddirkyqatIFQYIGE----LCRYLLNQPPKPTER 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2009 ltpAHlqvlkemniadqtAVRRMIVGGenlstrLARSIHEQFEGR---IEICNEYGPTETVVGCM-IYRYDAAKDRreSV 2084
Cdd:cd05940   195 ---KH-------------KVRMIFGNG------LRPDIWEEFKERfgvPRIAEFYAATEGNSGFInFFGKPGAIGR--NP 250
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2085 PIGTAAANTSIYVLD-ENMKP----------APIGVPGE-IY-ISGAGVARGYLNrPELTAEKFVDDPFEPGAKMYKTGD 2151
Cdd:cd05940   251 SLLRKVAPLALVKYDlESGEPirdaegrcikVPRGEPGLlISrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGD 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2152 LAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARE-DVHGFKQLCAYYV--SGGQTTAARLRKQ 2228
Cdd:cd05940   330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRAGMAAIVlqPNEEFDLSALAAH 409
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876 2229 LSQTLASYMVPaYFIEL-DEMPLTSNGKINK 2258
Cdd:cd05940   410 LEKNLPGYARP-LFLRLqPEMEITGTFKQQK 439
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1776-2261 1.48e-22

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 105.53  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKD-----RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGA 1850
Cdd:PRK08008    9 LRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1851 YVPIDPEYPQDRIRYMLDDSQAGIVL-------MQRDVRKQLAYEGVTVLLDDESSYHQDGS---------------DLA 1908
Cdd:PRK08008   89 MVPINARLLREESAWILQNSQASLLVtsaqfypMYRQIQQEDATPLRHICLTRVALPADDGVssftqlkaqqpatlcYAP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1909 PIS--DVshlAYVIYTSGSTGRPKGVLIEHGGLT---NYIWW-----AKEVYVKGEKAnFplysSISFDLTVTsifTPLV 1978
Cdd:PRK08008  169 PLStdDT---AEILFTSGTTSRPKGVVITHYNLRfagYYSAWqcalrDDDVYLTVMPA-F----HIDCQCTAA---MAAF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 TGNAIIVydgedktaLLE--------SIVRDPRVDIIKLTPAHLQVL---KEMNIADQTAVRRMIVGgENLSTRLARSIH 2047
Cdd:PRK08008  238 SAGATFV--------LLEkysarafwGQVCKYRATITECIPMMIRTLmvqPPSANDRQHCLREVMFY-LNLSDQEKDAFE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2048 EQFegRIEICNEYGPTETVVGCMiyrYDAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISG-AG--VARGY 2124
Cdd:PRK08008  309 ERF--GVRLLTSYGMTETIVGII---GDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEY 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2125 LNRPELTAEKFvddpfEPGAKMYkTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED- 2203
Cdd:PRK08008  384 YLDPKATAKVL-----EADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDs 457
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166797876 2204 -----VHGFKQLcayyVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK08008  458 irdeaIKAFVVL----NEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK08315 PRK08315
AMP-binding domain protein; Validated
263-744 1.53e-22

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 106.05  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKF--KNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAY 340
Cdd:PRK08315   16 QTIGQLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  341 VPLDPEYPKERLQYLLHDADADVLLVQHHLKNS------------LAFDGP-------------VIDLNDEAS---YHAD 392
Cdd:PRK08315   96 VTINPAYRLSELEYALNQSGCKALIAADGFKDSdyvamlyelapeLATCEPgqlqsarlpelrrVIFLGDEKHpgmLNFD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  393 cSLLSPVAGHSHLAY-----------VI---YTSGTTGKPKGVMVEHGGIVNSlqwkkAFF-----KHSPADRVLVLYPY 453
Cdd:PRK08315  176 -ELLALGRAVDDAELaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNN-----GYFigeamKLTEEDRLCIPVPL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  454 vFDAF--ILNFFGPLISGATLhLLPNEEnketF---AIQNAIKQERITHFSTSPrllkTM-IEQMNREDF---------- 517
Cdd:PRK08315  250 -YHCFgmVLGNLACVTHGATM-VYPGEG----FdplATLAAVEEERCTALYGVP----TMfIAELDHPDFarfdlsslrt 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  518 ---------IHVQHVVvggeqletdtVEKLHSLQprIRInnEYGPTENSVVSTfhpvQSA-DEQI-----TIGSPVANHQ 582
Cdd:PRK08315  320 gimagspcpIEVMKRV----------IDKMHMSE--VTI--AYGMTETSPVST----QTRtDDPLekrvtTVGRALPHLE 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  583 AYILG-AHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGRIDHQV 659
Cdd:PRK08315  382 VKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADgwMH--------TGDLAVMDEEGYVNIVGRIKDMI 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  660 kIRG----YRIEIGEVeaaMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPL 733
Cdd:PRK08315  454 -IRGgeniYPREIEEF---LYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPgaTLTEEDVRDFCRGKIAHYKIPRYIRFV 529
                         570
                  ....*....|.
gi 166797876  734 ERIPLTSNGKI 744
Cdd:PRK08315  530 DEFPMTVTGKI 540
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
266-744 1.60e-22

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 105.66  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  266 YQLFEEQAERTPENAAVKFKNDH-----LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAY 340
Cdd:cd05970    20 YDVVDAMAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  341 VPLDPEYPKERLQYLLHDADADVLL------VQHHLKNSLAFDGPVI--------DLNDEASYHADCSLLSPV------- 399
Cdd:cd05970   100 IPATHQLTAKDIVYRIESADIKMIVaiaednIPEEIEKAAPECPSKPklvwvgdpVPEGWIDFRKLIKNASPDferptan 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  400 --AGHSHLAYVIYTSGTTGKPKgvMVEH------GGIVNSLQWKKAffkhSPADRVLVlypyVFD-----AFILNFFGPL 466
Cdd:cd05970   180 syPCGEDILLVYFSSGTTGMPK--MVEHdftyplGHIVTAKYWQNV----REGGLHLT----VADtgwgkAVWGKIYGQW 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  467 ISGATLHLLpNEENKETFAIQNAIKQERITHFSTSPRLLKTMI-EQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPrI 545
Cdd:cd05970   250 IAGAAVFVY-DYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIrEDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTG-I 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  546 RINNEYGPTENSV-VSTFhPVQSADEQiTIGSPVANHQAYILGAHHQIQPIGIPGELYVGGA-----GVARGYLNRPELT 619
Cdd:cd05970   328 KLMEGFGQTETTLtIATF-PWMEPKPG-SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKT 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  620 EEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLY 699
Cdd:cd05970   406 AEVWHD-------GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVK 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876  700 AYYVGEPSLTAAqfrEELSRELPN--------YMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05970   479 ATIVLAKGYEPS---EELKKELQDhvkkvtapYKYPRIVEFVDELPKTISGKI 528
PRK13382 PRK13382
bile acid CoA ligase;
4337-4821 1.65e-22

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 105.61  E-value: 1.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4337 LFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPEL 4416
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4417 PEKRRAFMLKDSGADVLL---------------TCAGHAIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLmyVIYTS 4481
Cdd:PRK13382  128 AGPALAEVVTREGVDTVIydeefsatvdraladCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRV--ILLTS 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4482 GTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQFAAmsfdvcyqEMFSALSSGGILF-------IIgneAKRDIR-- 4552
Cdd:PRK13382  206 GTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVA--------PMFHAWGFSQLVLaaslactIV---TRRRFDpe 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4553 ---QLNDFVRTHGIqtAFLPTAFLKLLASEKHYFEPFAECVDHIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVV 4629
Cdd:PRK13382  275 atlDLIDRHRATGL--AVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMI 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4630 TMYTVD-----PDTdqelqpIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESltletfvphpYDSNQR 4704
Cdd:PRK13382  353 ATATPAdlraaPDT------AGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST----------KDFHDG 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4705 MYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTD-GQSdLYAY--FTAEQSLSI 4779
Cdd:PRK13382  417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHpdVAEAAVIGVDDEQyGQR-LAAFvvLKPGASATP 495
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 166797876 4780 SQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMP 4821
Cdd:PRK13382  496 ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1770-2261 1.78e-22

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 105.69  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1770 PFPQTP----VHQLFEEQSQrtPDQAAVIDKDR--QLTYGELNKRANRLARTLRAK-GVQTDQPVAIITRNSIESVVGIL 1842
Cdd:PLN02574   33 PLPSDPnldaVSFIFSHHNH--NGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1843 AVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESSYHQDGSD---------------- 1906
Cdd:PLN02574  111 AVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIefpkfyelikedfdfv 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1907 LAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIwwakEVYVKGEKANFPLYSSISFDLTVTSIF---------TPL 1977
Cdd:PLN02574  191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMV----ELFVRFEASQYEYPGSDNVYLAALPMFhiyglslfvVGL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1978 VT-GNAIIVYDGEDKTALLESIVRdprvdiIKLTpaHLQVLKEMNIADQTAVRRmiVGGENL------STRLA----RSI 2046
Cdd:PLN02574  267 LSlGSTIVVMRRFDASDMVKVIDR------FKVT--HFPVVPPILMALTKKAKG--VCGEVLkslkqvSCGAAplsgKFI 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2047 HE--QFEGRIEICNEYGPTE-TVVGCMiyRYDAAKDRRESvPIGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVAR 2122
Cdd:PLN02574  337 QDfvQTLPHVDFIQGYGMTEsTAVGTR--GFNTEKLSKYS-SVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMK 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2123 GYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARE 2202
Cdd:PLN02574  414 GYLNNPKATQSTIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVP 487
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 2203 DVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PLN02574  488 DKECGEIPVAFVVrrQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
3300-3781 2.16e-22

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 104.10  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3300 TAVVFEGKQFTYEELNRRANQLARTLQAKGVQA-DQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILND 3378
Cdd:cd05958     2 TCLRSPEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3379 SSISVLLYCGKL--QDDIGfsgtcidlmeehfyhekdsSLAlsyqssqlayaiYTSGTTGKPKGTLIEHRQVIHLIEGLS 3456
Cdd:cd05958    82 ARITVALCAHALtaSDDIC-------------------ILA------------FTSGTTGAPKATMHFHRDPLASADRYA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3457 RQVYSAYDAELNIAmLAPYYFDASVQQMYASLLS-GHTLFIVPKEIVSDGAALCRYYRqhsIDITDGTPAHLKLLIAAGD 3535
Cdd:cd05958   131 VNVLRLREDDRFVG-SPPLAFTFGLGGVLLFPFGvGASGVLLEEATPDLLLSAIARYK---PTVLFTAPTAYRAMLAHPD 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3536 LQGVTLQHLLI---GGEALSKTTVNKLKQLFGehgaAPGITNVyGPTEtcvdasLFNIECSsdawARSQNYVP--IGKPL 3610
Cdd:cd05958   207 AAGPDLSSLRKcvsAGEALPAALHRAWKEATG----IPIIDGI-GSTE------MFHIFIS----ARPGDARPgaTGKPV 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3611 GRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGylnlpelTDEKFVADPFvpEDRMYRTGDLARLLPDGNIEYIGRIDHQ 3690
Cdd:cd05958   272 PGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY-------LADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDM 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3691 VKIQGFRIELGEIESVMLNVPDIQE-----AAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQL 3765
Cdd:cd05958   343 IVSGGYNIAPPEVEDVLLQHPAVAEcavvgHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFV 422
                         490
                  ....*....|....*.
gi 166797876 3766 DKMPLTPNGKLNRQLL 3781
Cdd:cd05958   423 TELPRTATGKLQRFAL 438
PRK06164 PRK06164
acyl-CoA synthetase; Validated
4331-4818 2.50e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 105.21  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4331 PTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFL 4410
Cdd:PRK06164    9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4411 PIDPELPEKRRAFMLKDSGADVL-------------------------------LTCAGHAIP-PLFEGEVLLLDDPllY 4458
Cdd:PRK06164   89 AVNTRYRSHEVAHILGRGRARWLvvwpgfkgidfaailaavppdalpplraiavVDDAADATPaPAPGARVQLFALP--D 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4459 QGRTDNLNLSCSENDLMYVIYT-SGTTGQPKGVQleHKTMTNL---------LAYEQDHtqlrfdRVLQFAAMSFDVCYQ 4528
Cdd:PRK06164  167 PAPPAAAGERAADPDAGALLFTtSGTTSGPKLVL--HRQATLLrharaiaraYGYDPGA------VLLAALPFCGVFGFS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4529 EMFSALSSGGILFIIGN-EAKRDIRQLndfvRTHGIQTAFLPTAFLKLLASEKHYFEPFAECVDHIIAAgeqlIATRMlR 4607
Cdd:PRK06164  239 TLLGALAGGAPLVCEPVfDAARTARAL----RRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS----FAPAL-G 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4608 DMLAR---HQVTLHNHYGPSETH-VVTMYTVDPDTDQELQPIGKPIS-NTEIFILN-EAGTLQPVGIVGELCISGVSLAR 4681
Cdd:PRK06164  310 ELAALaraRGVPLTGLYGSSEVQaLVALQPATDPVSVRIEGGGRPASpEARVRARDpQDGALLPDGESGEIEIRAPSLMR 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4682 GYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKE 4759
Cdd:PRK06164  390 GYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALpgVAAAQVVGAT 463
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 4760 NtDGQSDLYAYFTAEQSLSISQ--LKEKLAGQIPGYMIPSYFIQLEKLPLT--GNG-KVNRRAL 4818
Cdd:PRK06164  464 R-DGKTVPVAFVIPTDGASPDEagLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
4339-4813 2.52e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 105.24  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4339 EQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKG-ACTDQVVAVLTDRSAHMIIgILAILKAGAAFLPIDPELP 4417
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGvGFGDRVLILMLNRTEFVES-VLAANMLGAIAVPVNFRLT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4418 EKRRAFMLKDSGADVLLT--------CAGHAIPPLF----------EGEVLLLDDpLLYQGRTDNLNLSCSENDLMYVIY 4479
Cdd:PRK07786  103 PPEIAFLVSDCGAHVVVTeaalapvaTAVRDIVPLLstvvvaggssDDSVLGYED-LLAEAGPAHAPVDIPNDSPALIMY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4480 TSGTTGQPKGVQLEHktmTNLLAyeQDHTQLRFDRVLQFAAMSFdvCYQEMF--SALSSGGILFIIGneAKRDIRQLNdf 4557
Cdd:PRK07786  182 TSGTTGRPKGAVLTH---ANLTG--QAMTCLRTNGADINSDVGF--VGVPLFhiAGIGSMLPGLLLG--APTVIYPLG-- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4558 vrthgiqtAFLPTAFLKLLASEK---HYFEPF---AECVD----------HIIAAGEQLIATRMLRDMLARHQVTLH-NH 4620
Cdd:PRK07786  251 --------AFDPGQLLDVLEAEKvtgIFLVPAqwqAVCAEqqarprdlalRVLSWGAAPASDTLLRQMAATFPEAQIlAA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4621 YGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYD 4700
Cdd:PRK07786  323 FGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4701 SnqrmyktGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVlakentdGQSD---------LY 4768
Cdd:PRK07786  403 S-------GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHpdiVEVAVI-------GRADekwgevpvaVA 468
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 166797876 4769 AYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:PRK07786  469 AVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
261-649 2.56e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 105.90  E-value: 2.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  261 GSRTVYQLFEEQAERTPENAAVKFKN------DHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVW 334
Cdd:PRK12582   47 YPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAM 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  335 KAGGAYVPLDPEYP-----KERLQYLLHDADADVLLVQH------HLKNSLAFDGPVI----DLNDEASYHADCSLLSPV 399
Cdd:PRK12582  127 QAGVPAAPVSPAYSlmshdHAKLKHLFDLVKPRVVFAQSgapfarALAALDLLDVTVVhvtgPGEGIASIAFADLAATPP 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  400 A----------GHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVL-----YPYVFDAFIlNFFG 464
Cdd:PRK12582  207 TaavaaaiaaiTPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSldwmpWNHTMGGNA-NFNG 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  465 PLISGATLHLLPNEENKETFA--IQNaIKQERITHFSTSPRLLKTMIEQMNRED------FIHVQHVVVGGEQLETDTVE 536
Cdd:PRK12582  286 LLWGGGTLYIDDGKPLPGMFEetIRN-LREISPTVYGNVPAGYAMLAEAMEKDDalrrsfFKNLRLMAYGGATLSDDLYE 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  537 KLHSLQ-----PRIRINNEYGPTENSVVSTfhPVQSADEQI-TIGSPVAnhqayilGAHHQIQPIGIPGELYVGGAGVAR 610
Cdd:PRK12582  365 RMQALAvrttgHRIPFYTGYGATETAPTTT--GTHWDTERVgLIGLPLP-------GVELKLAPVGDKYEVRVKGPNVTP 435
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876  611 GYLNRPELTEEKFVEhlhvpgQKMYKTGDLARWL----P------DGRI 649
Cdd:PRK12582  436 GYHKDPELTAAAFDE------EGFYRLGDAARFVdpddPekglifDGRV 478
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
3302-3715 2.68e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 104.06  E-value: 2.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3302 VVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSi 3381
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3382 SVLLYCGKLQDdigfsgtcidlmeehfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQV-Y 3460
Cdd:cd05914    80 AKAIFVSDEDD--------------------------------VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVlL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3461 SAYDAELNI-----------AMLAPYYFDASVqqMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTP----A 3525
Cdd:cd05914   128 GKGDKILSIlplhhiypltfTLLLPLLNGAHV--VFLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPkltlK 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3526 HLKLLIAAG---------------DLQGVTLQHLLIGGEALSKTTVNKLKQL-FgehgaapGITNVYGPTETcvdASLFn 3589
Cdd:cd05914   206 KFKFKLAKKinnrkirklafkkvhEAFGGNIKEFVIGGAKINPDVEEFLRTIgF-------PYTIGYGMTET---APII- 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3590 iecSSDAWARSQnYVPIGKPLGRNRMYILDSkkrlQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRT 3669
Cdd:cd05914   275 ---SYSPPNRIR-LGSAGKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHT 340
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 3670 GDLARLLPDGNIEYIGRIDHQ-VKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05914   341 GDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLE 387
PRK07638 PRK07638
acyl-CoA synthetase; Validated
4333-4818 2.83e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 104.48  E-value: 2.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKgACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPI 4412
Cdd:PRK07638    2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEK-ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4413 DPELPEKRRAFMLKDSGADVLLTCAGHAIP-PLFEGEVLLLDD--PLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKG 4489
Cdd:PRK07638   81 DIKWKQDELKERLAISNADMIVTERYKLNDlPDEEGRVIEIDEwkRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4490 -VQLEHKTMTNLLAYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFI----IGNEAKRDIRQLNDFVrthgIQ 4564
Cdd:PRK07638  161 fLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLmrkfIPNQVLDKLETENISV----MY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4565 TafLPT---AFLKLlasekhyfEPFAECVDHIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTmYTVDPDTDQE 4641
Cdd:PRK07638  237 T--VPTmleSLYKE--------NRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVT-ALVDEESERR 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4642 LQPIGKPISNTEIFILNEAG-TLQPvGIVGELCISGVSLARGYHNRESLTLETfvphpydsNQRMYKT-GDLARYLPEGN 4719
Cdd:PRK07638  306 PNSVGRPFHNVQVRICNEAGeEVQK-GEIGTVYVKSPQFFMGYIIGGVLAREL--------NADGWMTvRDVGYEDEEGF 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4720 IEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFtaEQSLSISQLKEKLAGQIPGYMIPS 4797
Cdd:PRK07638  377 IYIVGREKNMILFGGINIFPEEIESVLHEHpaVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKSFCLQRLSSFKIPK 454
                         490       500
                  ....*....|....*....|.
gi 166797876 4798 YFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK07638  455 EWHFVDEIPYTNSGKIARMEA 475
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1785-2256 2.83e-22

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 105.34  E-value: 2.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVI------DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI---- 1854
Cdd:cd05966    64 KERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfagf 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPEYPQDRIrymlDDSQAGIVL-----MQR------------------DVRKQLAY----------EGVTVLLDDESSYH 1901
Cdd:cd05966   144 SAESLADRI----NDAQCKLVItadggYRGgkviplkeivdealekcpSVEKVLVVkrtggevpmtEGRDLWWHDLMAKQ 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1902 QDGSDLAPIsDVSHLAYVIYTSGSTGRPKGVLIEHGGltnYIWWAKEV--YVkgekanfplyssisFDLTVTSIF----- 1974
Cdd:cd05966   220 SPECEPEWM-DSEDPLFILYTSGSTGKPKGVVHTTGG---YLLYAATTfkYV--------------FDYHPDDIYwctad 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1975 TPLVTGNAIIVY----DGEdKTALLE------------SIVRDPRVDIIKLTPahlqvlkemniadqTAVRRMIVGGE-- 2036
Cdd:cd05966   282 IGWITGHSYIVYgplaNGA-TTVMFEgtptypdpgrywDIVEKHKVTIFYTAP--------------TAIRALMKFGDew 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2037 ----NLST-RLARSIHEQF-------------EGRIEICNEYGPTETVvGCMIYRYDAAKDRRE---SVPI-GTAAAnts 2094
Cdd:cd05966   347 vkkhDLSSlRVLGSVGEPInpeawmwyyevigKERCPIVDTWWQTETG-GIMITPLPGATPLKPgsaTRPFfGIEPA--- 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2095 iyVLDENMKPAPIGVPGEIYISGA--GVARGYLNRPEltaeKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVK 2172
Cdd:cd05966   423 --ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVIN 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2173 IRGYRIELGEIEAALLQEEVIKEAVVTARED-VHGfKQLCAYYV--SGGQTT---AARLRKQLSQTLASYMVPAYFIELD 2246
Cdd:cd05966   497 VSGHRLGTAEVESALVAHPAVAEAAVVGRPHdIKG-EAIYAFVTlkDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVP 575
                         570
                  ....*....|
gi 166797876 2247 EMPLTSNGKI 2256
Cdd:cd05966   576 GLPKTRSGKI 585
PRK07470 PRK07470
acyl-CoA synthetase; Validated
273-755 3.23e-22

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 104.74  E-value: 3.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVQ-----H---------HLKNSLAFDGPVIDLNDEA--SYHADCSLLSPVAGHSHLAYVIYTSGTTG 416
Cdd:PRK07470   97 AYLAEASGARAMICHadfpeHaaavraaspDLTHVVAIGGARAGLDYEAlvARHLGARVANAAVDHDDPCWFFFTSGTTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  417 KPKGVMVEHGG----IVNSLqwKKAFFKHSPADRVLVLYPYVFDAFIlNFFGPLISGATLHLLPNE--ENKETFAIqnaI 490
Cdd:PRK07470  177 RPKAAVLTHGQmafvITNHL--ADLMPGTTEQDASLVVAPLSHGAGI-HQLCQVARGAATVLLPSErfDPAEVWAL---V 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  491 KQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVVVGGEQL-ETDTVEKLHSLQPRIRinNEYGPTE---NSVVST--F 562
Cdd:PRK07470  251 ERHRVTNLFTVPTILKMLVEHpaVDRYDHSSLRYVIYAGAPMyRADQKRALAKLGKVLV--QYFGLGEvtgNITVLPpaL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  563 HPVQSADE-QI-TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDL 640
Cdd:PRK07470  329 HDAEDGPDaRIgTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRD-------GWFRTGDL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  641 ARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAV----------------VAREDAdgakqlyayyvg 704
Cdd:PRK07470  402 GHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlgvpdpvwgevgvavcVARDGA------------ 469
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876  705 epSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADEN 755
Cdd:PRK07470  470 --PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEE 518
PRK07787 PRK07787
acyl-CoA synthetase; Validated
3300-3715 3.85e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 103.53  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3300 TAVVFEGKQFTYEELNRRANQLARTLQAKGvqadqLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDS-PSERiRYILND 3378
Cdd:PRK07787   17 DAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSgVAER-RHILAD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3379 SSISVLLycGKLQDDI-GFSGTCIDLMEE--HFYHEKDSSLAlsyqssqlAYAIYTSGTTGKPKGTLIEHRQVIHLIEGL 3455
Cdd:PRK07787   91 SGAQAWL--GPAPDDPaGLPHVPVRLHARswHRYPEPDPDAP--------ALIVYTSGTTGPPKGVVLSRRAIAADLDAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3456 SRQ-VYSAYDA-----------ELNIAMLAPYYFDASVQ-------QMYASLLS--GHTLFIVP---KEIVSDGAAlcry 3511
Cdd:PRK07787  161 AEAwQWTADDVlvhglplfhvhGLVLGVLGPLRIGNRFVhtgrptpEAYAQALSegGTLYFGVPtvwSRIAADPEA---- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3512 yrqhsiditdgtpahlklliaAGDLQGVTLqhLLIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETcvdasLFNIE 3591
Cdd:PRK07787  237 ---------------------ARALRGARL--LVSGSAALPVPVFDRLAALTGHR-----PVERYGMTET-----LITLS 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3592 CSSDAwARSQNYVpiGKPLGRNRMYILDSKKRLQPKGVQ--GELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRT 3669
Cdd:PRK07787  284 TRADG-ERRPGWV--GLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRT 354
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 3670 GDLARLLPDGNIEYIGR--IDhQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:PRK07787  355 GDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVRE 401
PRK07798 PRK07798
acyl-CoA synthetase; Validated
4333-4816 3.97e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 104.20  E-value: 3.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPI 4412
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4413 -----DPELpekrrAFMLKDSGADVL----------------LTCAGHAI-------PPLFEGEVLLLDdpLLYQGRTDN 4464
Cdd:PRK07798   84 nyryvEDEL-----RYLLDDSDAVALvyerefaprvaevlprLPKLRTLVvvedgsgNDLLPGAVDYED--ALAAGSPER 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4465 LNLSCSENDLmYVIYTSGTTGQPKGVQLEHKTM-------TNLLAYEQDHT-QLRFDRVLQFAAMSFDVCYQEM------ 4530
Cdd:PRK07798  157 DFGERSPDDL-YLLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGEPIEDeEELAKRAAAGPGMRRFPAPPLMhgagqw 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4531 --FSALSSGGILfIIGNEAKRDIRQLNDFVRTHGIQTAFLP-TAFLKLLASEKHYFEPF-AECVDHIIAAGEQLiaTRML 4606
Cdd:PRK07798  236 aaFAALFSGQTV-VLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPYdLSSLFAIASGGALF--SPSV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4607 RDMLARH--QVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNTeiFILNEAGT-LQP-VGIVGELCISGvSLARG 4682
Cdd:PRK07798  313 KEALLELlpNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRT--VVLDEDGNpVEPgSGEIGWIARRG-HIPLG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4683 YHNRESLTLETFvphPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH-------V----- 4750
Cdd:PRK07798  390 YYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHpdvadalVvgvpd 466
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 4751 ----QE--AVVLAKENTdgqsdlyayftaeqSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRR 4816
Cdd:PRK07798  467 erwgQEvvAVVQLREGA--------------RPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
PRK08316 PRK08316
acyl-CoA synthetase; Validated
3280-3780 4.19e-22

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 104.24  E-value: 4.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3280 PREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA 3359
Cdd:PRK08316    8 ARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3360 YLPIDPDSPSERIRYILNDSSISVLL------------YCGKLQDDIGFS---------GTCIDlMEEHFYHEKDSSLAL 3418
Cdd:PRK08316   88 HVPVNFMLTGEELAYILDHSGARAFLvdpalaptaeaaLALLPVDTLILSlvlggreapGGWLD-FADWAEAGSVAEPDV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3419 SYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHliEGLSRQV---YSAYDAELNiAMlaPYYFDAsvqQMYA----SLLSG 3491
Cdd:PRK08316  167 ELADDDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVagdMSADDIPLH-AL--PLYHCA---QLDVflgpYLYVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3492 HTLFIVPKeivSDGAALCRYYRQHSIDITDGTPA-HLKLL----IAAGDLQgvTLQHLLIGGEALSKTTVNKLKQLFgeh 3566
Cdd:PRK08316  239 ATNVILDA---PDPELILRTIEAERITSFFAPPTvWISLLrhpdFDTRDLS--SLRKGYYGASIMPVEVLKELRERL--- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3567 gaaPGIT--NVYGPTETCVDASLFNIEcssDAWARSQNyvpIGKPLGRNRMYILDSKKRLQPKGVQGELyiagdgVGR-- 3642
Cdd:PRK08316  311 ---PGLRfyNCYGQTEIAPLATVLGPE---EHLRRPGS---AGRPVLNVETRVVDDDGNDVAPGEVGEI------VHRsp 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3643 ----GYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaa 3718
Cdd:PRK08316  376 qlmlGYWDDPEKTAEAF-------RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAE--- 445
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 3719 AALKDADDEYYLCGYFA-----ADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK-LNRQL 3780
Cdd:PRK08316  446 VAVIGLPDPKWIEAVTAvvvpkAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKiLKREL 513
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1785-2261 4.74e-22

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 103.61  E-value: 4.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPqDRIR 1864
Cdd:cd05929     3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP-RAEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1865 YMLDDSQAGIVLMQRDvrkqLAYEGVTVLLDDESSyhQDGSDLAPISDVSHLAYVIYTSGSTGRPKGVLIEHGG------ 1938
Cdd:cd05929    82 CAIIEIKAAALVCGLF----TGGGALDGLEDYEAA--EGGSPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGgppdnd 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 -----LTNYIWWAKEVYVkgekANFPLYSSISFdltvTSIFTPLVTGNAIIVYDGEDKTALLESIVRDpRVDIIKLTPAH 2013
Cdd:cd05929   156 tlmaaALGFGPGADSVYL----SPAPLYHAAPF----RWSMTALFMGGTLVLMEKFDPEEFLRLIERY-RVTFAQFVPTM 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2014 LQVLKEMniadQTAVRrmivGGENLSTrLARSIH-------EQFEGRI----EICNE-YGPTETVVGCMIYRYDAAKdRR 2081
Cdd:cd05929   227 FVRLLKL----PEAVR----NAYDLSS-LKRVIHaaapcppWVKEQWIdwggPIIWEyYGGTEGQGLTIINGEEWLT-HP 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2082 ESVpiGTAAANtSIYVLDENMKPAPIGVPGEIYISGAGvARGYLNRPELTAEKFVDDPFEpgakmyKTGDLAKWLADGNI 2161
Cdd:cd05929   297 GSV--GRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2162 EYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED------VHGFKQlCAYYVSGGQTTAARLRKQLSQTLAS 2235
Cdd:cd05929   367 YLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDeelgqrVHAVVQ-PAPGADAGTALAEELIAFLRDRLSR 445
                         490       500
                  ....*....|....*....|....*.
gi 166797876 2236 YMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05929   446 YKCPRSIEFVAELPRDDTGKLYRRLL 471
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
258-744 4.85e-22

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 104.52  E-value: 4.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  258 DFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLR-NCGVQPDTLVAILADRSLEMIVSIIAVWKA 336
Cdd:PRK12492   19 DLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQqHTDLVPGDRIAVQMPNVLQYPIAVFGALRA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  337 GGAYVPLDPEYPKERLQYLLHDADADVL--------LVQHHLKNS---LAFDGPVIDLNDEA-----------------S 388
Cdd:PRK12492   99 GLIVVNTNPLYTAREMRHQFKDSGARALvylnmfgkLVQEVLPDTgieYLIEAKMGDLLPAAkgwlvntvvdkvkkmvpA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  389 YH--------------ADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQWKKAFFKHSPADRVLV---- 449
Cdd:PRK12492  179 YHlpqavpfkqalrqgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVaNMLQVRACLSQLGPDGQPLMkegq 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  450 ------LYPYVFDAFILNFFGPLISGATLHLLPNEENketfaIQNAIKQERITHFSTSPRLLKTMIEQMNRE-----DFI 518
Cdd:PRK12492  259 evmiapLPLYHIYAFTANCMCMMVSGNHNVLITNPRD-----IPGFIKELGKWRFSALLGLNTLFVALMDHPgfkdlDFS 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  519 HVQHVVVGGEQLETDTVEKLHSLQPrIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIP 598
Cdd:PRK12492  334 ALKLTNSGGTALVKATAERWEQLTG-CTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGER 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  599 GELYVGGAGVARGYLNRPELTEEKfvehlhVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNL 678
Cdd:PRK12492  413 GELCIKGPQVMKGYWQQPEATAEA------LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAH 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  679 ENVREAAVVAREDADGAKQLYAYYVG-EPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK12492  487 PKVANCAAIGVPDERSGEAVKLFVVArDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
289-744 5.13e-22

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 102.65  E-value: 5.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPldpeypkerlqyllhdadADVLLVQH 368
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNSLAFDGPVIDLNDEASyHADCSLLspvaghshlayVIYTSGTTGKPKgvMVEHG------GIVNSLQWkkafFKHS 442
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDENT-HADDPML-----------LYFTSGTTSKPK--LVEHThrsypvGHLSTMYW----IGLK 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  443 PADRVL-VLYPYVFDAFILNFFGPLISGATLHLLpNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQ 521
Cdd:cd05974   125 PGDVHWnISSPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLR 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  522 HVVVGGEQLETDTVEKLHSLQpRIRINNEYGPTENSVVSTFHPVQSADEQiTIGSPVANHQAYILgahhqiQPIGIP--- 598
Cdd:cd05974   204 EVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALVGNSPGQPVKAG-SMGRPLPGYRVALL------DPDGAPate 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  599 GE--LYVGG---AGVARGYLNRPELTEekfvehlHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEA 673
Cdd:cd05974   276 GEvaLDLGDtrpVGLMKGYAGDPDKTA-------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  674 AMFNLENVREAAVVAREDADGAKQLYAYYV----GEPSLTAAQFREELSRElpnymipsRFIPLERI--------PLTSN 741
Cdd:cd05974   349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragYEPSPETALEIFRFSRE--------RLAPYKRIrrlefaelPKTIS 420

                  ...
gi 166797876  742 GKI 744
Cdd:cd05974   421 GKI 423
PRK07798 PRK07798
acyl-CoA synthetase; Validated
3284-3775 5.42e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 103.81  E-value: 5.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPI 3363
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3364 DPDSPSERIRYILNDSSISVLLYcgklqdDIGFSGTCIDLMEE-----HFYHEKDSS------LALSYQSSqLA------ 3426
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVY------EREFAPRVAEVLPRlpklrTLVVVEDGSgndllpGAVDYEDA-LAagsper 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3427 ----------YAIYTSGTTGKPKGTLIEHRQV---------------IHLIEGLSRQVysAYDAELNIAMLAPYYFDASV 3481
Cdd:PRK07798  157 dfgerspddlYLLYTGGTTGMPKGVMWRQEDIfrvllggrdfatgepIEDEEELAKRA--AAGPGMRRFPAPPLMHGAGQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3482 QQMYASLLSGHTLFIVPKEiVSDGAALCRYYRQH---SIDIT-DgtpAHLKLLIAA----GDLQGVTLQHLLIGGEALSK 3553
Cdd:PRK07798  235 WAAFAALFSGQTVVLLPDV-RFDADEVWRTIEREkvnVITIVgD---AMARPLLDAlearGPYDLSSLFAIASGGALFSP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3554 TTvnklKQLFGEHgaAPG--ITNVYGPTETCVDASLFNiecSSDAWARSQNYVPIGKplgrnRMYILDSKKRLQPKGVQG 3631
Cdd:PRK07798  311 SV----KEALLEL--LPNvvLTDSIGSSETGFGGSGTV---AKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3632 ELYIAGDG-VGRGYLNLPELTDEKFvadpFVPEDRMYR-TGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLN 3709
Cdd:PRK07798  377 IGWIARRGhIPLGYYKDPEKTAETF----PTIDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKA 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3710 VPDI--------------QEAAAAALkdaddeyylcgyFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK 3775
Cdd:PRK07798  453 HPDVadalvvgvpderwgQEVVAVVQ------------LREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3284-3776 5.80e-22

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 104.20  E-value: 5.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVFEG------KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAG 3357
Cdd:cd17634    54 LAANALDRHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3358 GAYLPI----DPDSPSERI------------------RYI-----------LNDSSISVLLYCGKLQDDIGFSGTcidlm 3404
Cdd:cd17634   134 AVHSVIfggfAPEAVAGRIidsssrllitadggvragRSVplkknvddalnPNVTSVEHVIVLKRTGSDIDWQEG----- 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3405 EEHFYHEKDSSLALSYQSSQLA-----YAIYTSGTTGKPKGtliehrqVIHLIEGLSrqVYSAYDAElNIAMLAP---YY 3476
Cdd:cd17634   209 RDLWWRDLIAKASPEHQPEAMNaedplFILYTSGTTGKPKG-------VLHTTGGYL--VYAATTMK-YVFDYGPgdiYW 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3477 FDASVQQM-------YASLLSGHTLFIVP-KEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDlqgvtlqhlligg 3548
Cdd:cd17634   279 CTADVGWVtghsyllYGPLACGATTLLYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGD------------- 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3549 EALSKTTVNKLKQLFG--------------EHGAAPG--ITNVYGPTETcvdaslfniecssdAWARSQNyVPIGKPLGR 3612
Cdd:cd17634   346 DAIEGTDRSSLRILGSvgepinpeayewywKKIGKEKcpVVDTWWQTET--------------GGFMITP-LPGAIELKA 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3613 N---------RMYILDSKKRLQPKGVQGELYIAGD--GVGRGYLNlpelTDEKFVADPFVPEDRMYRTGDLARLLPDGNI 3681
Cdd:cd17634   411 GsatrpvfgvQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFG----DHERFEQTYFSTFKGMYFSGDGARRDEDGYY 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3682 EYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS-----ELRKRMARHLPGY 3756
Cdd:cd17634   487 WITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelyaELRNWVRKEIGPL 566
                         570       580
                  ....*....|....*....|
gi 166797876 3757 MIPAHFVQLDKMPLTPNGKL 3776
Cdd:cd17634   567 ATPDVVHWVDSLPKTRSGKI 586
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3309-3781 5.99e-22

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 102.60  E-value: 5.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3309 FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPI----DPDSPSERIRyilndSSISVL 3384
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGPKAIEHRLR-----TSGARL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3385 LYCGKLQddigfsgtcidlmeehfYHEKDSSLALSyqssqlayaIYTSGTTGKPKGTLIEHRQVihliegLSRQVYSAY- 3463
Cdd:cd05973    76 VVTDAAN-----------------RHKLDSDPFVM---------MFTSGTTGLPKGVPVPLRAL------AAFGAYLRDa 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3464 ------DAELNIA----MLAPYYfdasvqQMYASLLSGHtlfivpKEIVSDGA----ALCRYYRQHSIDITDGTPAHLKL 3529
Cdd:cd05973   124 vdlrpeDSFWNAAdpgwAYGLYY------AITGPLALGH------PTILLEGGfsveSTWRVIERLGVTNLAGSPTAYRL 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3530 LIAAG----DLQGVTLQHLLIGGEALSKTTVnklkQLFGEHGAAPgITNVYGPTEtcvdasLFNIECSSDAWARSQNYVP 3605
Cdd:cd05973   192 LMAAGaevpARPKGRLRRVSSAGEPLTPEVI----RWFDAALGVP-IHDHYGQTE------LGMVLANHHALEHPVHAGS 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3606 IGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVG----RGYLNLPELTdekfvadpfvPEDRMYRTGDLARLLPDGNI 3681
Cdd:cd05973   261 AGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSF 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3682 EYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAA----ALKDADDEYY--LCGYFAADKTIQiSEL----RKRMAR 3751
Cdd:cd05973   331 SFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIgvpdPERTEVVKAFvvLRGGHEGTPALA-DELqlhvKKRLSA 409
                         490       500       510
                  ....*....|....*....|....*....|
gi 166797876 3752 HlpGYMIPAHFVqlDKMPLTPNGKLNRQLL 3781
Cdd:cd05973   410 H--AYPRTIHFV--DELPKTPSGKIQRFLL 435
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
3286-3912 8.27e-22

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 104.79  E-value: 8.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3286 HELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDP 3365
Cdd:COG3319     4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3366 DSPSERIRYILNDSSISVLLYCGKLQDDIGFSGTcIDLMEEHFYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEH 3445
Cdd:COG3319    84 LALALAAAAAALLLAALALLLALLAALALALLAL-LLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3446 RQVIHLIEGLSRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITDGTPA 3525
Cdd:COG3319   163 VLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3526 HLKLLIAAGDLQGVTLQHLLIGGEALSKTTVNKLKQLFGEHGAAPGITNVYGPTETCVDASLFNIECSSDAWArsqnyVP 3605
Cdd:COG3319   243 LLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGAL-----GP 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3606 IGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF--VPEDRMYRTGDLARLLPDGNIEY 3683
Cdd:COG3319   318 IGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAgaGARGRLRRGGDRGRRLGGGLLLG 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3684 IGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFV 3763
Cdd:COG3319   398 LGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALL 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3764 QLDKMPLTPNGKLNRQLLPAPVKkRDSGIEYVPPQTSAEIQLTAIWEDVLGLEQVGIRDHFFEIGGHSLRATALIAKIQK 3843
Cdd:COG3319   478 LLLLLLLLLLLAALLLAAAAPAA-AAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLA 556
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 3844 QMHVQIPLRDVFRFPTIEQLARTITKTELTGYAAIPAIEKRpyypvSSAQKRLYILNHLEGGELSYNML 3912
Cdd:COG3319   557 LLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRA-----GGSGPPLFCVHPAGGNVLCYRPL 620
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
250-691 8.30e-22

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 103.82  E-value: 8.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  250 FDFNDTVRDFSGSRT-----VYQLFEEQAERTPEN-AAVKFKNDH----LTYRELNEKASRLARTLRNCGVQPDTLVAIL 319
Cdd:PRK04319   25 FSWEEVEKEFSWLETgkvniAYEAIDRHADGGRKDkVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  320 ADRSLEMIVSIIAVWKAGGAYVPL----DPEYPKERLQyllhDADADVL-----LVQH-------HLKNSLAFDGPV--- 380
Cdd:PRK04319  105 MPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRLE----DSEAKVLittpaLLERkpaddlpSLKHVLLVGEDVeeg 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  381 ---IDLN---DEASYHADCSLLSPVAGhshlAYVIYTSGTTGKPKGVMVEHGGIVnsLQWKKAFFkhspadrVLVLYPYv 454
Cdd:PRK04319  181 pgtLDFNalmEQASDEFDIEWTDREDG----AILHYTSGSTGKPKGVLHVHNAML--QHYQTGKY-------VLDLHED- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  455 fDAF---------------IlnfFGPLISGATLHLLPNEENKETFaiQNAIKQERITHFSTSP----RLLKTMIEQMNRE 515
Cdd:PRK04319  247 -DVYwctadpgwvtgtsygI---FAPWLNGATNVIDGGRFSPERW--YRILEDYKVTVWYTAPtairMLMGAGDDLVKKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  516 DFIHVQHVVVGGEQLETDTV---EKLHSLqpriRINNEYGPTENS--VVSTFhpvqsADEQITIGS---PVANHQAYILG 587
Cdd:PRK04319  321 DLSSLRHILSVGEPLNPEVVrwgMKVFGL----PIHDNWWMTETGgiMIANY-----PAMDIKPGSmgkPLPGIEAAIVD 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  588 AHHQIQPIGIPGELYV--GGAGVARGYLNRPELTEEKFVEHLhvpgqkmYKTGDLARWLPDGRIEYLGRIDHQVKIRGYR 665
Cdd:PRK04319  392 DQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGDW-------YVSGDSAYMDEDGYFWFQGRVDDVIKTSGER 464
                         490       500
                  ....*....|....*....|....*.
gi 166797876  666 IEIGEVEAAMFNLENVREAAVVARED 691
Cdd:PRK04319  465 VGPFEVESKLMEHPAVAEAGVIGKPD 490
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
4328-4818 8.46e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 103.57  E-value: 8.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4328 KRIPTTI-------HQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGIL 4400
Cdd:PRK06710   13 EEIPSTIsydiqplHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4401 AILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLtCAGHAIPPLFE---------------GEVLLLDDPLLY---QGRT 4462
Cdd:PRK06710   93 GTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL-CLDLVFPRVTNvqsatkiehvivtriADFLPFPKNLLYpfvQKKQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4463 DNLNLSCS-------------------------ENDLMYVIYTSGTTGQPKGVQLEHKTMTN--LLAYEQDHTQLRFDRV 4515
Cdd:PRK06710  172 SNLVVKVSesetihlwnsvekevntgvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSntLMGVQWLYNCKEGEEV 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4516 LQFAAMSFDVCYQEMFSALS--SGGILFIIgneAKRDIRQLNDFVRTHGIqTAF--LPTAFLKLLASE--KHY-FEPFAE 4588
Cdd:PRK06710  252 VLGVLPFFHVYGMTAVMNLSimQGYKMVLI---PKFDMKMVFEAIKKHKV-TLFpgAPTIYIALLNSPllKEYdISSIRA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4589 CVdhiiaAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTMYTVdpdTDQELQP--IGKPISNTEIFILN-EAGTLQP 4665
Cdd:PRK06710  328 CI-----SGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNF---LWEKRVPgsIGVPWPDTEAMIMSlETGEALP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4666 VGIVGELCISGVSLARGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAA 4745
Cdd:PRK06710  400 PGEIGEIVVKGPQIMKGYWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 4746 LLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSIS--QLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK06710  473 LYEHekVQEVVTIGVPDPYRGETVKAFVVLKEGTECSeeELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
3279-3789 8.99e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 103.57  E-value: 8.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3279 YPRE---------KTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVG 3349
Cdd:PRK06710   11 YPEEipstisydiQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3350 ILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL---------------------YCGKLQDDIGF------------ 3396
Cdd:PRK06710   91 YYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsatkiehvIVTRIADFLPFpknllypfvqkk 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3397 -SGTCIDLMEEHFYH-----EKDSSLALSY---QSSQLAYAIYTSGTTGKPKGTLIEHRQVI-HLIEGLsRQVYSAYDAE 3466
Cdd:PRK06710  171 qSNLVVKVSESETIHlwnsvEKEVNTGVEVpcdPENDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGV-QWLYNCKEGE 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3467 LNIAMLAPYYFDASVQQ-MYASLLSGHTLFIVPKeivSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHL- 3544
Cdd:PRK06710  250 EVVLGVLPFFHVYGMTAvMNLSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIr 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3545 --LIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETC-VDASLFNIEcssdawARSQNYVPIGKPLGRNRMYILDSK 3621
Cdd:PRK06710  327 acISGSAPLPVEVQEKFETVTGGK-----LVEGYGLTESSpVTHSNFLWE------KRVPGSIGVPWPDTEAMIMSLETG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3622 KRLQPkGVQGELYIAGDGVGRGYLNLPELTDEkfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELG 3701
Cdd:PRK06710  396 EALPP-GEIGEIVVKGPQIMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPR 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3702 EIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS--ELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQ 3779
Cdd:PRK06710  468 EVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSeeELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
                         570
                  ....*....|
gi 166797876 3780 LLPAPVKKRD 3789
Cdd:PRK06710  548 VLIEEEKRKN 557
PRK07529 PRK07529
AMP-binding domain protein; Validated
4307-4818 9.87e-22

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 103.88  E-value: 9.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4307 MMTKEEERDIQQlFNDTAVAEKRIPTTIHQLFEQQAERNPDHEAVMF--------GNQTLTYRQLNERSNQLARVLQDKG 4378
Cdd:PRK07529    1 MPAFATLADIEA-IEAVPLAARDLPASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4379 ACTDQVVAVLTDRSAHMIIGILAILKAGAAFlPIDPELPEKRRAFMLKDSGADVLLTCAG--------------HAIPPL 4444
Cdd:PRK07529   80 VGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwqkvaevlAALPEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4445 ---------------------------------FEGEVLLLDDPLLYQGRtdnlnlSCSENDLMYVIYTSGTTGQPKGVQ 4491
Cdd:PRK07529  159 rtvvevdlarylpgpkrlavplirrkaharildFDAELARQPGDRLFSGR------PIGPDDVAAYFHTGGTTGMPKLAQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4492 LEHKTMT------NLLAYEQDhtqlrfDRVLQFAAMSFDV--CYQEMFSALSSGGILFIIGNEAKRDIRQLNDF---VRT 4560
Cdd:PRK07529  233 HTHGNEVanawlgALLLGLGP------GDTVFCGLPLFHVnaLLVTGLAPLARGAHVVLATPQGYRGPGVIANFwkiVER 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4561 HGIqTAF--LPTAFLKLLA---------SEKhyfepFAECvdhiiaaGEQLIATRMLRDMLARHQVTLHNHYGPSETHVV 4629
Cdd:PRK07529  307 YRI-NFLsgVPTVYAALLQvpvdghdisSLR-----YALC-------GAAPLPVEVFRRFEAATGVRIVEGYGLTEATCV 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4630 TmyTVDP-DTDQELQPIGKPISNTE--IFILNEAGTLQ---PVGIVGELCISGVSLARGY----HNReSLTLEtfvphpy 4699
Cdd:PRK07529  374 S--SVNPpDGERRIGSVGLRLPYQRvrVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYleaaHNK-GLWLE------- 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4700 dsnQRMYKTGDLARYLPEGNIEYAGRRDHQVkIR-GYRVELGEVEAALLKH--VQEAVVLakentdGQSDLYA------Y 4770
Cdd:PRK07529  444 ---DGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHpaVALAAAV------GRPDAHAgelpvaY 513
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876 4771 FT--AEQSLSISQLKEKLAGQIPG-YMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK07529  514 VQlkPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPAL 564
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
4923-5335 9.97e-22

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 101.62  E-value: 9.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4923 VYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRT-VVEMVREEAVQVIKSQV----- 4996
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTgFTWRDRAEPLQYVRDDLappwa 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4997 --EFSMERYEATADEVEECF---RAfvRPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYD-- 5069
Cdd:cd19547    81 llDWSGEDPDRRAELLERLLaddRA--AGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEel 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5070 --GKE--LAPLRiQYKDFTEWKHQKEQREriKSQEEYWLGVFHEELPSfelpkDFARPPVRS---FDGKRHNFTldKTVT 5142
Cdd:cd19547   159 ahGREpqLSPCR-PYRDYVRWIRARTAQS--EESERFWREYLRDLTPS-----PFSTAPADRegeFDTVVHEFP--EQLT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5143 QGIKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTPIAGRPH--ADLEPIIGMFVNTLAIRTAPMAEKTFLDYITE 5220
Cdd:cd19547   229 RLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLET 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5221 TKETMLKAFEHQEYPFEELVEKLGVKRdLSRNPLFDTMFVLQNTEQTDIEVDSLAVRP---YEQTETAAKFDLqlnFLID 5297
Cdd:cd19547   309 IHRDLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIidlHAQEKTEYPIGL---IVLP 384
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 166797876 5298 QDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNP 5335
Cdd:cd19547   385 LQKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2829-3139 1.38e-21

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 101.41  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGML-----FHSLLDEASSSYFEqasFDLQGeLKIDWFKASLERLFETYAVLRTRFYsgwNDTPLQIVYKTQTP 2903
Cdd:cd19535     3 PLTDVQYAYWigrqdDQELGGVGCHAYLE---FDGED-LDPDRLERAWNKLIARHPMLRAVFL---DDGTQQILPEVPWY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2904 QIHFADLRDIEEHLREDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKEVFDHYSA 2983
Cdd:cd19535    76 GITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYED 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2984 LQEGREPEPLSavpYSDYIEWLDRQDQGA---AKRYWSGYLEgykgetTL-----LHKIAQHEQ-KEYAYANLICRFDHE 3054
Cdd:cd19535   156 PGEPLPPLELS---FRDYLLAEQALRETAyerARAYWQERLP------TLppapqLPLAKDPEEiKEPRFTRREHRLSAE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3055 QTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADV-----VFGsvvsgRPAEIPDVEQMIGLFINTIPVRIRCDEDST 3129
Cdd:cd19535   227 QWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFllnltLFN-----RLPLHPDVNDVVGDFTSLLLLEVDGSEGQS 301
                         330
                  ....*....|
gi 166797876 3130 FADTMQMVQQ 3139
Cdd:cd19535   302 FLERARRLQQ 311
PRK07470 PRK07470
acyl-CoA synthetase; Validated
4336-4818 1.45e-21

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 102.43  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4336 QLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPE 4415
Cdd:PRK07470   11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4416 LPEKRRAFMLKDSGADVLLTCAG--------HAIPPLFEGeVLLLDDP---LLYQGRTD-NL-----NLSCSENDLMYVI 4478
Cdd:PRK07470   91 QTPDEVAYLAEASGARAMICHADfpehaaavRAASPDLTH-VVAIGGAragLDYEALVArHLgarvaNAAVDHDDPCWFF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4479 YTSGTTGQPKGVQLEHKTM----TNLLA-YEQDHTQLrfDRVLQFAAMSFDV-CYQEMFSALSSGGILfiIGNEaKRDIR 4552
Cdd:PRK07470  170 FTSGTTGRPKAAVLTHGQMafviTNHLAdLMPGTTEQ--DASLVVAPLSHGAgIHQLCQVARGAATVL--LPSE-RFDPA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4553 QLNDFVRTHGIQTAFLPTAFLKLLASEkhyfePFAECVDH-----IIAAG------EQLIATRMLRDMLARHqvtlhnhY 4621
Cdd:PRK07470  245 EVWALVERHRVTNLFTVPTILKMLVEH-----PAVDRYDHsslryVIYAGapmyraDQKRALAKLGKVLVQY-------F 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4622 GPSE-THVVT-----MYTVDPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFV 4695
Cdd:PRK07470  313 GLGEvTGNITvlppaLHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4696 phpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLA-KENTDGQSDLYAYFT 4772
Cdd:PRK07470  393 -------DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHpaVSEVAVLGvPDPVWGEVGVAVCVA 465
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 4773 AE-QSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK07470  466 RDgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
4470-4818 1.47e-21

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 102.02  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4470 SENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLA-YEQDHTQLRF---DRVLQ----FAAMSFDVCyqeMFSALSSGGILF 4541
Cdd:cd05909   145 QPDDPAVILFTSGSEGLPKGVVLSHK---NLLAnVEQITAIFDPnpeDVVFGalpfFHSFGLTGC---LWLPLLSGIKVV 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4542 IIGNEAkrDIRQLNDFVRTHGIqTAFLPT-AFLKLLASEKHYfEPFAEcVDHIIAAGEQLIATrmLRDM-LARHQVTLHN 4619
Cdd:cd05909   219 FHPNPL--DYKKIPELIYDKKA-TILLGTpTFLRGYARAAHP-EDFSS-LRLVVAGAEKLKDT--LRQEfQEKFGIRILE 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4620 HYGPSETH-VVTMYTvdPDTDQELQPIGKPISNTEIFILNEAG-TLQPVGIVGELCISGVSLARGYHNRESLTLETFVPH 4697
Cdd:cd05909   292 GYGTTECSpVISVNT--PQSPNKEGTVGRPLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDG 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4698 PYDsnqrmykTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKHVQEAVVLAKENT-DGQ-SDLYAYFTAEQ 4775
Cdd:cd05909   370 WYD-------TGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVpDGRkGEKIVLLTTTT 442
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 166797876 4776 SLSISQLKEKL-AGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05909   443 DTDPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
256-751 1.59e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 102.38  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  256 VRDFS-GSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVW 334
Cdd:PRK13383   27 LREASrGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  335 KAGGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSLAFDGPVIDLNDEASYHA-DCSLLSPVAGHSHLayVIYTSG 413
Cdd:PRK13383  107 LLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAeESGGRPAVAAPGRI--VLLTSG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  414 TTGKPKGV----MVEHG-GIVNSLQWKKAFFKHSpadRVLVLYPyVFDAFILNFFGPLIS-GATLhLLPNEENKETFAIQ 487
Cdd:PRK13383  185 TTGKPKGVprapQLRSAvGVWVTILDRTRLRTGS---RISVAMP-MFHGLGLGMLMLTIAlGGTV-LTHRHFDAEAALAQ 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  488 NAIkqERITHFSTSPRLLKTMIEQMN----REDFIHVQHVVVGGEQLETDTVEKLHSLQPRIrINNEYGPTENSVVSTFH 563
Cdd:PRK13383  260 ASL--HRADAFTAVPVVLARILELPPrvraRNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALAT 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  564 PVQSADEQITIGSPVANHQAYILGAHHqiQPIG--IPGELYVGGAGVARGYLNrpelTEEKFVehlhVPGqkMYKTGDLA 641
Cdd:PRK13383  337 PADLRDAPETVGKPVAGCPVRILDRNN--RPVGprVTGRIFVGGELAGTRYTD----GGGKAV----VDG--MTSTGDMG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  642 RWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSR 719
Cdd:PRK13383  405 YLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPgsGVDAAQLRDYLKD 484
                         490       500       510
                  ....*....|....*....|....*....|..
gi 166797876  720 ELPNYMIPSRFIPLERIPLTSNGKIDLKALPA 751
Cdd:PRK13383  485 RVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
3297-3781 1.75e-21

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 101.99  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLycgklqddigfsgtcIDlmEEHFYHEKDSS-----LALSYQSSQLAYAI-YTSGTTGKPKGTLIEHRqvih 3450
Cdd:cd12118    98 RHSEAKVLF---------------VD--REFEYEDLLAEgdpdfEWIPPADEWDPIALnYTSGTTGRPKGVVYHHR---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3451 lieglsrqvySAYdaeLNiAMLAPYYFDASVQQMYASLL----------------SGHTLFIVPKeivSDGAALCRYYRQ 3514
Cdd:cd12118   157 ----------GAY---LN-ALANILEWEMKQHPVYLWTLpmfhcngwcfpwtvaaVGGTNVCLRK---VDAKAIYDLIEK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3515 HSIDITDGTPAHLKLLIAAGDLQGVTLQ---HLLIGGEALSKTTVNKLKQLFGEHGAAPGITNVYGPTETCvdaslfnie 3591
Cdd:cd12118   220 HKVTHFCGAPTVLNMLANAPPSDARPLPhrvHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGPATVC--------- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3592 cssdAWARSQNYVPI---GKPLGRN--RMYILDSKKRLQPKGVQ---------GELYIAGDGVGRGYLNLPELTDEKFva 3657
Cdd:cd12118   291 ----AWKPEWDELPTeerARLKARQgvRYVGLEEVDVLDPETMKpvprdgktiGEIVFRGNIVMKGYLKNPEATAEAF-- 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3658 dpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFA-- 3735
Cdd:cd12118   365 -----RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVElk 439
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876 3736 ADKTIQISELRKRMARHLPGYMIPAHFVQLDkMPLTPNGKLNRQLL 3781
Cdd:cd12118   440 EGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
4334-4818 1.88e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 102.53  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4334 IHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKgacTD----QVVAVLTDRSAHMIIGILAILKAGAAF 4409
Cdd:PRK05677   26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQH---TDlkpgDRIAVQLPNVLQYPVAVFGAMRAGLIV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4410 LPIDPELPEKRRAFMLKDSGADVLLTCAGHA-----------IPPLFEGEVLLLDDPL---------------------- 4456
Cdd:PRK05677  103 VNTNPLYTAREMEHQFNDSGAKALVCLANMAhlaekvlpktgVKHVIVTEVADMLPPLkrllinavvkhvkkmvpayhlp 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4457 --------LYQGRTDNLN-LSCSENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLAyeqdhtqlrfdRVLQFAAMsfdvcy 4527
Cdd:PRK05677  183 qavkfndaLAKGAGQPVTeANPQADDVAVLQYTGGTTGVAKGAMLTHR---NLVA-----------NMLQCRAL------ 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4528 qeMFSALSSG--------------------GILFIIGNEAK--RDIRQLNDFVRTHGIQ--TAF--LPTAFLKLLASEKh 4581
Cdd:PRK05677  243 --MGSNLNEGceiliaplplyhiyaftfhcMAMMLIGNHNIliSNPRDLPAMVKELGKWkfSGFvgLNTLFVALCNNEA- 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4582 yFEPFAECVDHIIAAGE---QLIATRMLRdmlarhQVT---LHNHYGPSETHVVTmyTVDPDTDQELQPIGKPISNTEIF 4655
Cdd:PRK05677  320 -FRKLDFSALKLTLSGGmalQLATAERWK------EVTgcaICEGYGMTETSPVV--SVNPSQAIQVGTIGIPVPSTLCK 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4656 ILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpyDSNQRMyKTGDLARYLPEGNIEYAGRRDHQVKIRGY 4735
Cdd:PRK05677  391 VIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL-----DSDGWL-KTGDIALIQEDGYMRIVDRKKDMILVSGF 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RV---ELGEVEAALLKHVQEAVVLAKENTDGQS-DLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNG 4811
Cdd:PRK05677  465 NVypnELEDVLAALPGVLQCAAIGVPDEKSGEAiKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVG 544

                  ....*..
gi 166797876 4812 KVNRRAL 4818
Cdd:PRK05677  545 KILRREL 551
PRK09088 PRK09088
acyl-CoA synthetase; Validated
3292-3781 1.90e-21

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 101.81  E-value: 1.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3292 QAHRTPDNTAVV--FEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPS 3369
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3370 ERIRYILNDSSISVLLycgklQDDIGFSGTCIDLMEEHFYHEKDS---SLALSYQSSQLAYAIYTSGTTGKPKGTLIEHR 3446
Cdd:PRK09088   84 SELDALLQDAEPRLLL-----GDDAVAAGRTDVEDLAAFIASADAlepADTPSIPPERVSLILFTSGTSGQPKGVMLSER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3447 QVIHLIEGLSrqVYSAYDAELNIAMLAP-YYFDASVQQMYASLLSGHTLfivpkeIVSDG---AALCRYYRQHSIDITD- 3521
Cdd:PRK09088  159 NLQQTAHNFG--VLGRVDAHSSFLCDAPmFHIIGLITSVRPVLAVGGSI------LVSNGfepKRTLGRLGDPALGITHy 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3522 -GTPAHLKLLIAAGDLQGVTLQHL--LIGGEA--LSKTTVNKLKQlfgehgaapGITNV--YGPTETcvdASLFNIECSS 3594
Cdd:PRK09088  231 fCVPQMAQAFRAQPGFDAAALRHLtaLFTGGAphAAEDILGWLDD---------GIPMVdgFGMSEA---GTVFGMSVDC 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3595 DAWARSQNYVPIGKPLGRNRmyILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLAR 3674
Cdd:PRK09088  299 DVIRAKAGAAGIPTPTVQTR--VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIAR 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3675 LLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDAD--DEYYLCGYFAADKTIQISELRKRMARH 3752
Cdd:PRK09088  371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwgEVGYLAIVPADGAPLDLERIRSHLSTR 450
                         490       500
                  ....*....|....*....|....*....
gi 166797876 3753 LPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK09088  451 LAKYKVPKHLRLVDALPRTASGKLQKARL 479
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1801-2261 2.65e-21

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 101.83  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1801 TYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVL---- 1876
Cdd:cd17642    46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFcskk 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 -MQR--DVRKQLAYEGVTVLLDDESSYHQ----------------DGSDLAPIS--DVSHLAYVIYTSGSTGRPKGVLIE 1935
Cdd:cd17642   126 gLQKvlNVQKKLKIIKTIIILDSKEDYKGyqclytfitqnlppgfNEYDFKPPSfdRDEQVALIMNSSGSTGLPKGVQLT 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1936 HggltnyiwwaKEVYVKGEKANFPLY-SSISFD---LTV----------TSIFTPLVTGNAIIVYDGEDKTALleSIVRD 2001
Cdd:cd17642   206 H----------KNIVARFSHARDPIFgNQIIPDtaiLTVipfhhgfgmfTTLGYLICGFRVVLMYKFEEELFL--RSLQD 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2002 PRVDIIKLTPAHLQVLKEMNIADQ---TAVRRMIVGGENLStrlaRSIHEQFEGRIE---ICNEYGPTETVVGCMIYryD 2075
Cdd:cd17642   274 YKVQSALLVPTLFAFFAKSTLVDKydlSNLHEIASGGAPLS----KEVGEAVAKRFKlpgIRQGYGLTETTSAILIT--P 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2076 AAKDRRESVpiGTAAANTSIYVLDENMKPApIGV--PGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLA 2153
Cdd:cd17642   348 EGDDKPGAV--GKVVPFFYAKVVDLDTGKT-LGPneRGELCVKGPMIMKGYVNNPEATKALIDKDGW------LHSGDIA 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2154 KWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED------------VHGFKQLCAY----YVSG 2217
Cdd:cd17642   419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDedagelpaavvvLEAGKTMTEKevmdYVAS 498
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 166797876 2218 GQTTAARLRKQLsqtlasymvpayfIELDEMPLTSNGKINKKGL 2261
Cdd:cd17642   499 QVSTAKRLRGGV-------------KFVDEVPKGLTGKIDRRKI 529
PRK13382 PRK13382
bile acid CoA ligase;
268-751 2.73e-21

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 101.76  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  268 LFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEY 347
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  348 PKERLQYLLHDADADVLLVQHHLKNSL--AFDG-P----VIDLNDEASYHADCSL------LSPVAGHSHLAYVIYTSGT 414
Cdd:PRK13382  128 AGPALAEVVTREGVDTVIYDEEFSATVdrALADcPqatrIVAWTDEDHDLTVEVLiaahagQRPEPTGRKGRVILLTSGT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  415 TGKPKGVMVEHGGIVNSLqwkKAFFKHSP--ADRVLVLYPYVFDA-------FILNFFGPLIS------GATLHLlpnee 479
Cdd:PRK13382  208 TGTPKGARRSGPGGIGTL---KAILDRTPwrAEEPTVIVAPMFHAwgfsqlvLAASLACTIVTrrrfdpEATLDL----- 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  480 nketfaiqnaIKQERITHFSTSP----RLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLhslQPRIR--INNEYGP 553
Cdd:PRK13382  280 ----------IDRHRATGLAVVPvmfdRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAF---MDQFGdvIYNNYNA 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  554 TENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRpelTEEKFVEhlhvpgqK 633
Cdd:PRK13382  347 TEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFHD-------G 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  634 MYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTAAQ- 712
Cdd:PRK13382  417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPe 496
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 166797876  713 -FREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPA 751
Cdd:PRK13382  497 tLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
PRK07529 PRK07529
AMP-binding domain protein; Validated
1772-2258 2.80e-21

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 102.34  E-value: 2.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1772 PQTpVHQLFEEQSQRTPDQAAVI--------DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILA 1843
Cdd:PRK07529   24 PAS-TYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1844 VLKSGGAyVPIDPEYPQDRIRYMLDDSQAGIV----------LMQR--DVRKQLAyEGVTVLLDDESSY----------- 1900
Cdd:PRK07529  103 GEAAGIA-NPINPLLEPEQIAELLRAAGAKVLvtlgpfpgtdIWQKvaEVLAALP-ELRTVVEVDLARYlpgpkrlavpl 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1901 ---------HQDGSDLAPISDVSH----------LAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKAN---- 1957
Cdd:PRK07529  181 irrkahariLDFDAELARQPGDRLfsgrpigpddVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTvfcg 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1958 FPLYSSisFDLTVTsIFTPLVTGNAIIV-----YDGEDKTALLESIVRDPRVDIIKLTPAHLQVLKEMNI--ADQTAVRR 2030
Cdd:PRK07529  261 LPLFHV--NALLVT-GLAPLARGAHVVLatpqgYRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVdgHDISSLRY 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2031 MIVGGENLSTRLARSiheqFEGR--IEICNEYGPTETVVGCMIYRYDAAKdRRESVPIGTAAANTSIYVLDEN---MKPA 2105
Cdd:PRK07529  338 ALCGAAPLPVEVFRR----FEAAtgVRIVEGYGLTEATCVSSVNPPDGER-RIGSVGLRLPYQRVRVVILDDAgryLRDC 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2106 PIGVPGEIYISGAGVARGYLNrPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVkIR-GYRIELGEIE 2184
Cdd:PRK07529  413 AVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGW------LNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIE 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2185 AALLQEEVIKEAVVTAREDVHGFKQLCAY--YVSGGQTTAARL----RKQLSQTLAsymVPAYFIELDEMPLTSNGKINK 2258
Cdd:PRK07529  485 EALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELlafaRDHIAERAA---VPKHVRILDALPKTAVGKIFK 561
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
4339-4813 3.10e-21

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 101.22  E-value: 3.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4339 EQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPE 4418
Cdd:cd12118    11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4419 KRRAFMLKDSGADVLLTcaghaiPPLFEGEVLLL---DDPLLYQGRtdnlnlscSENDLMYVIYTSGTTGQPKGVQLEHK 4495
Cdd:cd12118    91 EEIAFILRHSEAKVLFV------DREFEYEDLLAegdPDFEWIPPA--------DEWDPIALNYTSGTTGRPKGVVYHHR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4496 -----TMTNLLAYEQDHTQLRFDRVLQFAAMSFdvCYQEMFSALssGGILFIIgneAKRDIRQLNDFVRTHGIqTAF--L 4568
Cdd:cd12118   157 gaylnALANILEWEMKQHPVYLWTLPMFHCNGW--CFPWTVAAV--GGTNVCL---RKVDAKAIYDLIEKHKV-THFcgA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4569 PTAFLKLLASEKHYFEPFAECVdHIIAAGEQLIAtRMLRDMLARHQVTLHNhYGPSETH-VVTMYTVDPDTD---QELQP 4644
Cdd:cd12118   229 PTVLNMLANAPPSDARPLPHRV-HVMTAGAPPPA-AVLAKMEELGFDVTHV-YGLTETYgPATVCAWKPEWDelpTEERA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4645 IGKPISNTEIFILNE-----AGTLQPV----GIVGELCISGVSLARGYHNRESLTLETFvphpydsnqR--MYKTGDLAR 4713
Cdd:cd12118   306 RLKARQGVRYVGLEEvdvldPETMKPVprdgKTIGEIVFRGNIVMKGYLKNPEATAEAF---------RggWFHSGDLAV 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4714 YLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLS------ISQLKEK 4785
Cdd:cd12118   377 IHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHpaVLEAAVVARPDEKWGEVPCAFVELKEGAKvteeeiIAFCREH 456
                         490       500
                  ....*....|....*....|....*...
gi 166797876 4786 LagqiPGYMIPSYFIQLEkLPLTGNGKV 4813
Cdd:cd12118   457 L----AGFMVPKTVVFGE-LPKTSTGKI 479
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
4477-4818 3.79e-21

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 98.17  E-value: 3.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4477 VIYTSGTTGQPKGVQLehkTMTNLLAyeqdhtqlRFDRVLQFaaMSFD------VC--------YQEMFSALSSGGILFI 4542
Cdd:cd17630     5 VILTSGSTGTPKAVVH---TAANLLA--------SAAGLHSR--LGFGggdswlLSlplyhvggLAILVRSLLAGAELVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4543 IgnEAKRDIRQ-LNDFVRTHgiqTAFLPTAFLKLLASekHYFEPFAECVDHIIAAGEQLiaTRMLRDMLARHQVTLHNHY 4621
Cdd:cd17630    72 L--ERNQALAEdLAPPGVTH---VSLVPTQLQRLLDS--GQGPAALKSLRAVLLGGAPI--PPELLERAADRGIPLYTTY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4622 GPSEThVVTMYTVDPDtDQELQPIGKPISNTEIFILNEagtlqpvgivGELCISGVSLARGYHNResltletfVPHPYDS 4701
Cdd:cd17630   143 GMTET-ASQVATKRPD-GFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRG--------QLVPEFN 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4702 NQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVL-AKENTDGQSdLYAYFTAEQSLS 4778
Cdd:cd17630   203 EDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHpaVRDAFVVgVPDEELGQR-PVAVIVGRGPAD 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 166797876 4779 ISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd17630   282 PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
3289-3804 4.39e-21

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 101.49  E-value: 4.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3289 FEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA--------- 3359
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVvallntqqr 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3360 --------------YLPIDPDSpSERIRYILNDSSISVLLYCGKlQDDIGFSGTCIDLMEE-HFYHEKDSSLALSYQSSQ 3424
Cdd:PRK08279  123 gavlahslnlvdakHLIVGEEL-VEAFEEARADLARPPRLWVAG-GDTLDDPEGYEDLAAAaAGAPTTNPASRSGVTAKD 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3425 LAYAIYTSGTTGKPKGTLIEHRQVI-------HLIeGLSRQ--VYSAydaelniamLAPYYFDASVQQMYASLLSGHTLF 3495
Cdd:PRK08279  201 TAFYIYTSGTTGLPKAAVMSHMRWLkamggfgGLL-RLTPDdvLYCC---------LPLYHNTGGTVAWSSVLAAGATLA 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3496 IVPK--------EIVSDGAA-------LCRYYRQHSIDITDGtpAH-LKLLIAAGdlqgvtlqhlliggeaLSKTTVNKL 3559
Cdd:PRK08279  271 LRRKfsasrfwdDVRRYRATafqyigeLCRYLLNQPPKPTDR--DHrLRLMIGNG----------------LRPDIWDEF 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3560 KQLFGEhgaaPGITNVYGPTETCVdaSLFNIecssDAWARSQNYVPIgkPLGRN----------RMYILDSKKRLQP--K 3627
Cdd:PRK08279  333 QQRFGI----PRILEFYAASEGNV--GFINV----FNFDGTVGRVPL--WLAHPyaivkydvdtGEPVRDADGRCIKvkP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3628 GVQGELyiagdgVGR--------GYLNlPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGRIdhqvkiqG--FR 3697
Cdd:PRK08279  401 GEVGLL------IGRitdrgpfdGYTD-PEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRL-------GdtFR 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3698 -----IELGEIESVMLNVPDIQEAAAaalkdaddeyY---------LCGyFAA-----DKTIQISELRKRMARHLPGYMI 3758
Cdd:PRK08279  467 wkgenVATTEVENALSGFPGVEEAVV----------YgvevpgtdgRAG-MAAivladGAEFDLAALAAHLYERLPAYAV 535
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3759 PAhFVQL-DKMPLTPNGKLNRQLL------PA----PVKKRDSGIE-YVP--PQTSAEIQ 3804
Cdd:PRK08279  536 PL-FVRLvPELETTGTFKYRKVDLrkegfdPSkvddPLYVLDPGSGgYVPltAELYAEIA 594
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
4332-4818 4.56e-21

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 101.36  E-value: 4.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4332 TTIHQLFEQQAERNPDHEAVMfGNQ--TLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAF 4409
Cdd:PRK06087   23 ASLADYWQQTARAMPDKIAVV-DNHgaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4410 LPIDPELPEKRRAFMLKDSGA---------------DVLLTCAgHAIPPLfeGEVLLLD-------DPLLYQGRTDNLNL 4467
Cdd:PRK06087  102 VPLLPSWREAELVWVLNKCQAkmffaptlfkqtrpvDLILPLQ-NQLPQL--QQIVGVDklapatsSLSLSQIIADYEPL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4468 S----CSENDLMYVIYTSGTTGQPKGVQLEHktmTNLLAYEQdhtqlRFDRVLQFAAMsfDVCYqeMFSALSSG-----G 4538
Cdd:PRK06087  179 TtaitTHGDELAAVLFTSGTEGLPKGVMLTH---NNILASER-----AYCARLNLTWQ--DVFM--MPAPLGHAtgflhG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4539 IL--FIIGNEAKrdirqlndfvrthgIQTAFLPTAFLKLLASEK----HYFEPFA-ECVDHIIAAGEQL----------- 4600
Cdd:PRK06087  247 VTapFLIGARSV--------------LLDIFTPDACLALLEQQRctcmLGATPFIyDLLNLLEKQPADLsalrfflcggt 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4601 -IATRMLRDMLaRHQVTLHNHYGPSET--HVVtmytVDPDTDQEL--QPIGKPISNTEIFILNEAGTLQPVGIVGELCIS 4675
Cdd:PRK06087  313 tIPKKVARECQ-QRGIKLLSVYGSTESspHAV----VNLDDPLSRfmHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASR 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4676 GVSLARGYHNRESLTLETFvphpydSNQRMYKTGDLARYLPEGNIEYAGRRDhQVKIR-GYRVELGEVEAALLKH---VQ 4751
Cdd:PRK06087  388 GPNVFMGYLDEPELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKK-DIIVRgGENISSREVEDILLQHpkiHD 460
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4752 EAVVLAKENTDGQ-SDLYAYFTA-EQSLSISQLKEKLAGQ-IPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK06087  461 ACVVAMPDERLGErSCAYVVLKApHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
257-771 4.87e-21

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 101.62  E-value: 4.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  257 RDFSGSR--TVYQLFEEQAER-TPENAA------VKFKNDHLTYRELNEKASRLARTLRNCGVQ------------PDTL 315
Cdd:cd05967    42 RWFVGGRlnTCYNALDRHVEAgRGDQIAliydspVTGTERTYTYAELLDEVSRLAGVLRKLGVVkgdrviiympmiPEAA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  316 VAILADRSLEMIVSIIAvwkaGGAYVP-----LDPEYPK------------ERLQY--LLHDA-------DADVLLVQH- 368
Cdd:cd05967   122 IAMLACARIGAIHSVVF----GGFAAKelasrIDDAKPKlivtascgiepgKVVPYkpLLDKAlelsghkPHHVLVLNRp 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 HLKNSLAFDGPVIDLNDE---ASYHaDCSllsPVAGHsHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKA-------- 437
Cdd:cd05967   198 QVPADLTKPGRDLDWSELlakAEPV-DCV---PVAAT-DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRniygikpg 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  438 --FFKHSPADRVlvlypyVFDAFILnfFGPLISGATLHLLpneENKETF-----AIQNAIKQERITHFSTSP---RLLK- 506
Cdd:cd05967   273 dvWWAASDVGWV------VGHSYIV--YGPLLHGATTVLY---EGKPVGtpdpgAFWRVIEKYQVNALFTAPtaiRAIRk 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  507 --TMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNeYGPTENSVVSTFHPVQSADEQITIGS---PVANH 581
Cdd:cd05967   342 edPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDH-WWQTETGWPITANPVGLEPLPIKAGSpgkPVPGY 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  582 QAYILGAHHQIQPIGIPGELYVGGA---GVARGYLNRPELTEEKFVEHLhvPGqkMYKTGDLARWLPDGRIEYLGRIDHQ 658
Cdd:cd05967   421 QVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYLSKF--PG--YYDTGDAGYKDEDGYLFIMGRTDDV 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  659 VKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIP-SRF---IP 732
Cdd:cd05967   497 INVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEgvKITAEELEKELVALVREQIGPvAAFrlvIF 576
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 166797876  733 LERIPLTSNGKIDLKALPAAdentrAENEYIAPRNTIEE 771
Cdd:cd05967   577 VKRLPKTRSGKILRRTLRKI-----ADGEDYTIPSTIED 610
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
258-744 5.14e-21

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 101.11  E-value: 5.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  258 DFSGSRTVYQLFEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKA 336
Cdd:PRK08751   20 DLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  337 GGAYVPLDPEYPKERLQYLLHDADADVLLVQHHLKNSLA---FDGPV-----IDLNDE--------------------AS 388
Cdd:PRK08751  100 GLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQqviADTPVkqvitTGLGDMlgfpkaalvnfvvkyvkklvPE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  389 YHADCSL-------------LSPVA-GHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQ----WKKAFFKHSPADRVLV- 449
Cdd:PRK08751  180 YRINGAIrfrealalgrkhsMPTLQiEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqWLAGTGKLEEGCEVVIt 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  450 -LYPYVFDAFILNFFGPLISGATLHLLPNEENKETFAIQnaIKQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVVVG 526
Cdd:PRK08751  260 aLPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKE--LKKTRFTAFTGVNTLFNGLLNTpgFDQIDFSSLKMTLGG 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  527 GEQLETDTVEKLHSLQpRIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGA 606
Cdd:PRK08751  338 GMAVQRSVAERWKQVT-GLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  607 GVARGYLNRPELTEEKfvehlhVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAV 686
Cdd:PRK08751  417 QVMKGYWKRPEETAKV------MDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAA 490
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  687 VAREDADGAKQLYAYYV-GEPSLTAAQFREELSRELPNYMIPsRFIPLER-IPLTSNGKI 744
Cdd:PRK08751  491 VGVPDEKSGEIVKVVIVkKDPALTAEDVKAHARANLTGYKQP-RIIEFRKeLPKTNVGKI 549
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
4473-4815 5.60e-21

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 98.10  E-value: 5.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 DLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHtQLRF---DRVLQFAAMSFDVCYQEMFSALSSGGiLFIIGNEAKR 4549
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKE-GLNWvvgDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGENTT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4550 -----DIRQLNDFVrthgiQTAFLPTAFLKLLASEKHYFEpFAECVDHIIAAGEQLIATRMlRDMLARHQVTLHNHYGPS 4624
Cdd:cd17635    80 ykslfKILTTNAVT-----TTCLVPTLLSKLVSELKSANA-TVPSLRLIGYGGSRAIAADV-RFIEATGLTNTAQVYGLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4625 ETHVVTMYTVDPDTdQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpydsnQR 4704
Cdd:cd17635   153 ETGTALCLPTDDDS-IEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4705 MYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLK--HVQEAVV--LAKENTDGQSDLYAYFTAEQSLS-I 4779
Cdd:cd17635   225 WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGvsGVQECACyeISDEEFGELVGLAVVASAELDENaI 304
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 166797876 4780 SQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd17635   305 RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
251-744 8.24e-21

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 100.78  E-value: 8.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   251 DFNDTVRDFSGSRT--VYQLFEEQAERTPENAAVKFKND------HLTYRELNEKASRLARTLRNCGVQPDTLVAILADR 322
Cdd:TIGR02188   43 SFPPFYKWFVGGELnvSYNCVDRHLEARPDKVAIIWEGDepgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPM 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   323 SLEMIVSIIAVWKAGGA----YVPLDPEYPKERLQyllhDADADVL---------------------------------L 365
Cdd:TIGR02188  123 IPEAAIAMLACARIGAIhsvvFGGFSAEALADRIN----DAGAKLVitadeglrggkviplkaivdealekcpvsvehvL 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   366 VQHHLKNSLAF--DGPVIDLNDE-ASYHADCSLlSPVaGHSHLAYVIYTSGTTGKPKGVMVEHGGIvnsLQWKKAFFKhs 442
Cdd:TIGR02188  199 VVRRTGNPVVPwvEGRDVWWHDLmAKASAYCEP-EPM-DSEDPLFILYTSGSTGKPKGVLHTTGGY---LLYAAMTMK-- 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   443 padrvlvlypYVFD-------------------AFILnfFGPLISGATLHLL---PNEENKETFAiqNAIKQERITHFST 500
Cdd:TIGR02188  272 ----------YVFDikdgdifwctadvgwitghSYIV--YGPLANGATTVMFegvPTYPDPGRFW--EIIEKHKVTIFYT 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   501 SPRLLKTMIEQMNredfihvQHVvvggEQLETDTVEKLHSL-QPrirINNE----Y----GPTENSVVSTFHPVQSADEQ 571
Cdd:TIGR02188  338 APTAIRALMRLGD-------EWV----KKHDLSSLRLLGSVgEP---INPEawmwYykvvGKERCPIVDTWWQTETGGIM 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   572 IT---------IGS---PVANHQAYILGAHHqiQPIGIPGElyvGGA--------GVARGYLNRPelteEKFVEHLHVPG 631
Cdd:TIGR02188  404 ITplpgatptkPGSatlPFFGIEPAVVDEEG--NPVEGPGE---GGYlvikqpwpGMLRTIYGDH----ERFVDTYFSPF 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   632 QKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLTA- 710
Cdd:TIGR02188  475 PGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPd 554
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 166797876   711 AQFREEL----SRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:TIGR02188  555 DELRKELrkhvRKEIGPIAKPDKIRFVPGLPKTRSGKI 592
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
4952-5234 8.28e-21

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 99.10  E-value: 8.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4952 LETEGK-LPLNRLLTAFQRLMQGHEPLRTVVEmvrEEAVQVIKSQV-EFSMERY---EATADEVEECFRAfVRP------ 5020
Cdd:cd19535    30 LEFDGEdLDPDRLERAWNKLIARHPMLRAVFL---DDGTQQILPEVpWYGITVHdlrGLSEEEAEAALEE-LRErlshrv 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5021 FDLSQAPLLRAGLIELEQD---LHiFMFDMhhIITDGASMNIFVEKLIQLYD--GKELAPLRIQYKDFTEWKHQKEQRER 5095
Cdd:cd19535   106 LDVERGPLFDIRLSLLPEGrtrLH-LSIDL--LVADALSLQILLRELAALYEdpGEPLPPLELSFRDYLLAEQALRETAY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5096 IKSQeEYWLgvfhEELPSF----ELPkdFARPP--VRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFSAYSILLA 5169
Cdd:cd19535   183 ERAR-AYWQ----ERLPTLppapQLP--LAKDPeeIKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLA 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 5170 KYSGQDDIVVGTPIAGRP--HADLEPIIGMFVNT--LAIRTApmAEKTFLDYITETKETMLKAFEHQEY 5234
Cdd:cd19535   256 RWSGQPRFLLNLTLFNRLplHPDVNDVVGDFTSLllLEVDGS--EGQSFLERARRLQQQLWEDLDHSSY 322
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2370-2554 9.24e-21

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 98.97  E-value: 9.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2370 WFFEQTTTDQHYYNQAVMLHApEG-FQETQLRQTLQKLAEHHDALRMTFRTtENGCEAQneEIAQSGLYRLEVMNLKEDP 2448
Cdd:cd19531    12 WFLDQLEPGSAAYNIPGALRL-RGpLDVAALERALNELVARHEALRTTFVE-VDGEPVQ--VILPPLPLPLPVVDLSGLP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2449 DPGRTIEAKA---DEIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLP- 2523
Cdd:cd19531    88 EAEREAEAQRlarEEARRPFDLARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPp 167
                         170       180       190
                  ....*....|....*....|....*....|....
gi 166797876 2524 ---QKTDsFQLWAKrlsEYAQSETIKQEQEYWTK 2554
Cdd:cd19531   168 lpiQYAD-YAVWQR---EWLQGEVLERQLAYWRE 197
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
4626-4907 1.34e-20

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 95.97  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4626 THVVTMYTVDPDTDQELQPIGKPISNTEIFILNEAGtlQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYDSNQRM 4705
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDL--QGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4706 YKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKHVQEAVVLAKENTDGQSD-----LYAYFTAEQSLSIS 4780
Cdd:COG3433    79 GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAgvgllLIVGAVAALDGLAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4781 QLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPE-AGLQTGTDYVAPRTNM---EEQLICIWQDVLKVK--E 4854
Cdd:COG3433   159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAaAEALLAAASPAPALETaltEEELRADVAELLGVDpeE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876 4855 IGVKDNFFDLGGHSLRGMTLIAKIHKQFSkNISLREVFQCPTVGEMAQAIAEA 4907
Cdd:COG3433   239 IDPDDNLFDLGLDSIRLMQLVERWRKAGL-DVSFADLAEHPTLAAWWALLAAA 290
PRK09274 PRK09274
peptide synthase; Provisional
271-687 1.35e-20

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 99.59  E-value: 1.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  271 EQAERTPENAAV----------KFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAY 340
Cdd:PRK09274   14 RAAQERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  341 VPLDPEYPKERLQYLLHDADADVLLVQ---HHLK-----------------NSLAFDGPVIDlndEASYHADCSLLSPVA 400
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAQPDAFIGIpkaHLARrlfgwgkpsvrrlvtvgGRLLWGGTTLA---TLLRDGAAAPFPMAD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  401 -GHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyvfdAFILnfFGPLISGATlhLLPNEE 479
Cdd:PRK09274  171 lAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFP----LFAL--FGPALGMTS--VIPDMD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  480 -------NKEtfAIQNAIKQERITHFSTSPRLLKTMIE--QMNREDFIHVQHVVVGGEQLETDTVEKLHS-LQPRIRINN 549
Cdd:PRK09274  243 ptrpatvDPA--KLFAAIERYGVTNLFGSPALLERLGRygEANGIKLPSLRRVISAGAPVPIAVIERFRAmLPPDAEILT 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  550 EYGPTENSVVST------FHPVQSADEQ---ITIGSPVANHQAYIL----GAHHQIQ-----PIGIPGELYVGGAGVARG 611
Cdd:PRK09274  321 PYGATEALPISSiesreiLFATRAATDNgagICVGRPVDGVEVRIIaisdAPIPEWDdalrlATGEIGEIVVAGPMVTRS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  612 YLNRPELTE-----EKFVEHLHvpgqkmyKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEaAMFN-LENVREAA 685
Cdd:PRK09274  401 YYNRPEATRlakipDGQGDVWH-------RMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCE-RIFNtHPGVKRSA 472

                  ..
gi 166797876  686 VV 687
Cdd:PRK09274  473 LV 474
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
3308-3781 1.48e-20

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 99.24  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3308 QFTYEELNRRANQLARTLQAKGVQADQLVGIM---TERSLEMVVGILGVlkagGAYL-PIDPDSPSERIRYILNDSSISV 3383
Cdd:cd12119    25 RYTYAEVAERARRLANALRRLGVKPGDRVATLawnTHRHLELYYAVPGM----GAVLhTINPRLFPEQIAYIINHAEDRV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3384 LLY-------CGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSY---------------QSSQLAYAI-YTSGTTGKPKG 3440
Cdd:cd12119   101 VFVdrdflplLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYeellaaespeydwpdFDENTAAAIcYTSGTTGNPKG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3441 TLIEHRQ-VIHLIEGLSRQVY--SAYDAELNIAmlaPYYFDASVQQMYASLLSGHTLfIVPKEIVsDGAALCRYYRQHSI 3517
Cdd:cd12119   181 VVYSHRSlVLHAMAALLTDGLglSESDVVLPVV---PMFHVNAWGLPYAAAMVGAKL-VLPGPYL-DPASLAELIEREGV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3518 DITDGTPAHLKLLIAAGDLQGVTLQHL---LIGGEALSKTTVNKLKQLFGEhgaapgITNVYGPTETC-------VDASL 3587
Cdd:cd12119   256 TFAAGVPTVWQGLLDHLEANGRDLSSLrrvVIGGSAVPRSLIEAFEERGVR------VIHAWGMTETSplgtvarPPSEH 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3588 FNIECSSD-AWARSQNYVPIGKplgrnRMYILDSKKRLQPK--GVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpED 3664
Cdd:cd12119   330 SNLSEDEQlALRAKQGRPVPGV-----ELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALT-------ED 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3665 RMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdaddeyylcgyfAA-------- 3736
Cdd:cd12119   398 GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAE-------------------AAvigvphpk 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 3737 -------------DKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd12119   459 wgerplavvvlkeGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1919-2258 1.57e-20

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 96.42  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKGVLIEH-GGLTNYIWWAKEVYVKgEKANF----PLYSSISFDltvTSIFTPLVTGNAIIVYDGEDKTA 1993
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHrQTLRAAAAWADCADLT-EDDRYliinPFFHTFGYK---AGIVACLLTGATVVPVAVFDVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1994 LLESIVRDpRVDIIKLTPAHLQVL---KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFeGRIEICNEYGPTETVVGCM 2070
Cdd:cd17638    81 ILEAIERE-RITVLPGPPTLFQSLldhPGRKKFDLSSLRAAVTGAATVPVELVRRMRSEL-GFETVLTAYGLTEAGVATM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2071 IYRYDAAKDRRESVpiGTAAANTSIYVLDenmkpapigvPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTG 2150
Cdd:cd17638   159 CRPGDDAETVATTC--GRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGW------LHTG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2151 DLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVS-GGQT-TAARLRKQ 2228
Cdd:cd17638   221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVArPGVTlTEEDVIAW 300
                         330       340       350
                  ....*....|....*....|....*....|
gi 166797876 2229 LSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:cd17638   301 CRERLANYKVPRFVRFLDELPRNASGKVMK 330
PRK08162 PRK08162
acyl-CoA synthetase; Validated
1762-2272 1.99e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 99.25  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1762 QTLNDTAAPF-PQTPVHQLfeeqsQRT----PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNS-- 1834
Cdd:PRK08162    6 QGLDRNAANYvPLTPLSFL-----ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIpa 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1835 -IES---VVGILAVLKSggAYVPIDPEypqdRIRYMLDDSQAGIVL-------MQRDVRKQLAYEGVTVLLDDESSYhqd 1903
Cdd:PRK08162   81 mVEAhfgVPMAGAVLNT--LNTRLDAA----SIAFMLRHGEAKVLIvdtefaeVAREALALLPGPKPLVIDVDDPEY--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1904 gSDLAPISDVSHLAYVI---------------------YTSGSTGRPKGVLIEHGG-----LTNYIWWA---KEVYVkge 1954
Cdd:PRK08162  152 -PGGRFIGALDYEAFLAsgdpdfawtlpadewdaialnYTSGTTGNPKGVVYHHRGaylnaLSNILAWGmpkHPVYL--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1955 kANFPLY--SSISFDLTV-----TSIFTPLVtgnaiivydgeDKTALLESIvRDPRVDIIKLTPAHLQVLKEMNIADQTA 2027
Cdd:PRK08162  228 -WTLPMFhcNGWCFPWTVaaragTNVCLRKV-----------DPKLIFDLI-REHGVTHYCGAPIVLSALINAPAEWRAG 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2028 ----VRRMIVGGENLSTRLARSIHEQFEgrieICNEYGPTET---VVGCmiyrydAAKDRRESVPIGTAAANTS------ 2094
Cdd:PRK08162  295 idhpVHAMVAGAAPPAAVIAKMEEIGFD----LTHVYGLTETygpATVC------AWQPEWDALPLDERAQLKArqgvry 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2095 -----IYVLD-ENMKPapigVP------GEIYISGAGVARGYLNRPELTAEKFVDDPFEpgakmykTGDLAKWLADGNIE 2162
Cdd:PRK08162  365 plqegVTVLDpDTMQP----VPadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYIK 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2163 YAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPA 2240
Cdd:PRK08162  434 IKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVElkDGASATEEEIIAHCREHLAGFKVPK 513
                         570       580       590
                  ....*....|....*....|....*....|..
gi 166797876 2241 yFIELDEMPLTSNGKINKkglpapdFELQDRA 2272
Cdd:PRK08162  514 -AVVFGELPKTSTGKIQK-------FVLREQA 537
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
4335-4912 2.01e-20

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 100.55  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4335 HQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDP 4414
Cdd:COG3319     4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4415 ELPEKRRAFMLKDSGADVLLTCAGHAIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSE----NDLMYVIYTSGTTGQPKGV 4490
Cdd:COG3319    84 LALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAaaaaAAALAAAAGLGGGGGGAGV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4491 QLEHKTMTNLLAYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAFLPT 4570
Cdd:COG3319   164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4571 AFLKLLASEKHYFEPFAECVDHIIAAGEQLIATRMLRDMLARHQVTLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPIS 4650
Cdd:COG3319   244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPG 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4651 NTEIFILNEAGTLQPVGIVGEL--CISGVSLARGYHNRESLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDH 4728
Cdd:COG3319   324 LLVLLVLLVLLLPLLLGVGGGGggGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRL 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4729 QVKIRGYRVELGEVEAALLKHVQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLT 4808
Cdd:COG3319   404 QRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLL 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4809 GNGKVNRRALPMPEAGLQ-TGTDYVAPRTNMEEQLICIWQDVLKVKEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNIS 4887
Cdd:COG3319   484 LLLLLAALLLAAAAPAAAaAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLL 563
                         570       580
                  ....*....|....*....|....*
gi 166797876 4888 LREVFQCPTVGEMAQAIAEAETNGP 4912
Cdd:COG3319   564 LLALLLAPTLAALAAALAAAAAAAA 588
PLN02574 PLN02574
4-coumarate--CoA ligase-like
289-757 2.30e-20

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 99.15  E-value: 2.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNC-GVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ 367
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  368 HHLKNSLAFDG-PVIDLNDEASYHA----------------DCsLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVN 430
Cdd:PLN02574  147 PENVEKLSPLGvPVIGVPENYDFDSkriefpkfyelikedfDF-VPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIA 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  431 SLQ----WKKAFFKHSPADRVLVLYPYVFDAFILNFF--GPLISGATLHLLPNEENKEtfaIQNAIKQERITHFSTSPRL 504
Cdd:PLN02574  226 MVElfvrFEASQYEYPGSDNVYLAALPMFHIYGLSLFvvGLLSLGSTIVVMRRFDASD---MVKVIDRFKVTHFPVVPPI 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  505 LKTMIEQMN---REDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVST--FHPVQSADEQiTIGSPVA 579
Cdd:PLN02574  303 LMALTKKAKgvcGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYS-SVGLLAP 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  580 NHQAYILG-AHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGRID 656
Cdd:PLN02574  382 NMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDgwLR--------TGDIAYFDEDGYLYIVDRLK 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  657 HQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAAQFREELSRELPNYMIPSRFIPLE 734
Cdd:PLN02574  454 EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQgsTLSQEAVINYVAKQVAPYKKVRKVVFVQ 533
                         490       500
                  ....*....|....*....|....*.
gi 166797876  735 RIPLTSNGKI---DLKALPAADENTR 757
Cdd:PLN02574  534 SIPKSPAGKIlrrELKRSLTNSVSSR 559
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1799-2235 2.66e-20

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 98.31  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1799 QLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQ 1878
Cdd:cd05932     6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1879 R-----DVRKQLAYEGVTVLLD--DESSYHQDGSDL---------APISDVSHLAYVIYTSGSTGRPKGVLIEHGgltNY 1942
Cdd:cd05932    86 KlddwkAMAPGVPEGLISISLPppSAANCQYQWDDLiaqhppleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFG---SF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1943 IWWAKEVYVK-GEKANFPLYSSISFDLTVTSIFtplVTGNAIIvydGEDKTALLESI---VRD------------PRV-- 2004
Cdd:cd05932   163 AWAAQAGIEHiGTEENDRMLSYLPLAHVTERVF---VEGGSLY---GGVLVAFAESLdtfVEDvqrarptlffsvPRLwt 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2005 ----DII-KLTPAHLQVLKEMNIADQTaVRRMIVGGENL-STRLARS---------IHEQFEGRIEICNEYGPTETVVgc 2069
Cdd:cd05932   237 kfqqGVQdKIPQQKLNLLLKIPVVNSL-VKRKVLKGLGLdQCRLAGCgsapvppalLEWYRSLGLNILEAYGMTENFA-- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2070 miYRYDAAKDRRESVPIGTAAANTSIYVLDEnmkpapigvpGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKT 2149
Cdd:cd05932   314 --YSHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF------LRT 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2150 GDLAKWLADGNIEYAGRIDEQVKI-RGYRIELGEIEAALLQEEVIKEAVVTAR--EDVHGFKQLCAYYVSGGQTTA-ARL 2225
Cdd:cd05932   376 GDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRADAFArAEL 455
                         490
                  ....*....|
gi 166797876 2226 RKQLSQTLAS 2235
Cdd:cd05932   456 EASLRAHLAR 465
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1795-2265 3.54e-20

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 98.43  E-value: 3.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1795 DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGI 1874
Cdd:PRK04319   69 SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKV 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1875 V-----LMQRDVRKQLAyEGVTVLLDDESSYHQDG-----------SDLAPI--SDVSHLAYVIYTSGSTGRPKGVLIEH 1936
Cdd:PRK04319  149 LittpaLLERKPADDLP-SLKHVLLVGEDVEEGPGtldfnalmeqaSDEFDIewTDREDGAILHYTSGSTGKPKGVLHVH 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1937 GG-LTNY-------------IWW--AKEVYVKGekanfplyssisfdlTVTSIFTPLVTGNAIIVYDGEDKTALLESIVR 2000
Cdd:PRK04319  228 NAmLQHYqtgkyvldlheddVYWctADPGWVTG---------------TSYGIFAPWLNGATNVIDGGRFSPERWYRILE 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2001 DPRVDIIKLTPAHLQVLkeMNIADQTAVR------RMIVG-GENLSTRLARSIHEQFEGRIEicNEYGPTETvvGC-MIY 2072
Cdd:PRK04319  293 DYKVTVWYTAPTAIRML--MGAGDDLVKKydlsslRHILSvGEPLNPEVVRWGMKVFGLPIH--DNWWMTET--GGiMIA 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2073 RYDAAKDRRESV--PI-GTAAAntsiyVLDENMKPAPIGVPGEIYISgAG---VARGYLNRPELTAEKFVDDpfepgakM 2146
Cdd:PRK04319  367 NYPAMDIKPGSMgkPLpGIEAA-----IVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFAGD-------W 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2147 YKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED-VHGfkQLCAYYVS--GGQTTAA 2223
Cdd:PRK04319  434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDpVRG--EIIKAFVAlrPGYEPSE 511
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2224 RLRKQLSQ----TLASYMVPAYfIE-LDEMPLTSNGKINKK-------GLPAPD 2265
Cdd:PRK04319  512 ELKEEIRGfvkkGLGAHAAPRE-IEfKDKLPKTRSGKIMRRvlkawelGLPEGD 564
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1800-2258 3.71e-20

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 97.25  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPidpeypqdrirymlddsqAGIVLMQR 1879
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1880 DVRKQLAYEGVTVLLDDESSYHQDgsdlaPIsdvshLAYviYTSGSTGRPKGVLIEH-----GGLTNYIW---------- 1944
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDENTHADD-----PM-----LLY--FTSGTTSKPKLVEHTHrsypvGHLSTMYWiglkpgdvhw 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1945 ------WAKEVYvkgekanfplyssisfdltvTSIFTPLVTGNAIIVYDGE--DKTALLESIVRdPRVDIIKLTPAHLQV 2016
Cdd:cd05974   131 nisspgWAKHAW--------------------SCFFAPWNAGATVFLFNYArfDAKRVLAALVR-YGVTTLCAPPTVWRM 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2017 LKEMNIAD-QTAVRRMIVGGENLSTRLARSIHEQFEgrIEICNEYGPTETVvgCMIYRYDAAKDRRESvpIGTAAANTSI 2095
Cdd:cd05974   190 LIQQDLASfDVKLREVVGAGEPLNPEVIEQVRRAWG--LTIRDGYGQTETT--ALVGNSPGQPVKAGS--MGRPLPGYRV 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2096 YVLDENMKPAPigvPGEIYIS-----GAGVARGYLNRPELTAEKFvddpfepGAKMYKTGDLAKWLADGNIEYAGRIDEQ 2170
Cdd:cd05974   264 ALLDPDGAPAT---EGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDV 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2171 VKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQ---TTAARLRKQLSQTLASYMvPAYFIEL 2245
Cdd:cd05974   334 FKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlrAGYEpspETALEIFRFSRERLAPYK-RIRRLEF 412
                         490
                  ....*....|...
gi 166797876 2246 DEMPLTSNGKINK 2258
Cdd:cd05974   413 AELPKTISGKIRR 425
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
3922-4168 4.14e-20

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 96.74  E-value: 4.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3922 DRDKLQ---QAFRTLILRHESLRTGFkMADG--EPVQYVLDHAAFEAEWYQ-GEEDDADLYIRQFIRPFH----LDEPPL 3991
Cdd:cd19544    34 SRARLDaflAALQQVIDRHDILRTAI-LWEGlsEPVQVVWRQAELPVEELTlDPGDDALAQLRARFDPRRyrldLRQAPL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3992 LRVGLIElQPDRG--ILMFDMHHIISDGTSMSVLIKEFIRIYEGET--LPPLrIQYKDYaVWQtgeARLQ-QIQKQEAYW 4066
Cdd:cd19544   113 LRAHVAE-DPANGrwLLLLLFHHLISDHTSLELLLEEIQAILAGRAaaLPPP-VPYRNF-VAQ---ARLGaSQAEHEAFF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4067 LELYsGDV--PVlhLP---ADyIRPSARDFAGAtmHFTLDKQKSDGLKQLASQtestlYMVLLAS-----YTLLLSKYSG 4136
Cdd:cd19544   187 REML-GDVdePT--APfglLD-VQGDGSDITEA--RLALDAELAQRLRAQARR-----LGVSPASlfhlaWALVLARCSG 255
                         250       260       270
                  ....*....|....*....|....*....|....
gi 166797876 4137 QEDIIVGSPIAGRPHA--DLEPIIGMFVNTLAMR 4168
Cdd:cd19544   256 RDDVVFGTVLSGRMQGgaGADRALGMFINTLPLR 289
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
4353-4815 4.91e-20

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 97.13  E-value: 4.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4353 FGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADV 4432
Cdd:cd05914     3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4433 LLTcaghaipplfegevlllddpllyqgrTDNlnlscseNDLMYVIYTSGTTGQPKGVQLEHKT-MTN-------LLAYE 4504
Cdd:cd05914    83 IFV--------------------------SDE-------DDVALINYTSGTTGNSKGVMLTYRNiVSNvdgvkevVLLGK 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4505 QDHT----------QLRFDRVLQFAAMSFDVCYQEMFSALSSG------------GILFIIGNEAKRDIrqLNDFVRTHG 4562
Cdd:cd05914   130 GDKIlsilplhhiyPLTFTLLLPLLNGAHVVFLDKIPSAKIIAlafaqvtptlgvPVPLVIEKIFKMDI--IPKLTLKKF 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4563 IQTAFLP---TAFLKLLASEKHyfEPFAECVDHIIAAGEQLIA--TRMLRDMlarhQVTLHNHYGPSETHVVTMYTvdPD 4637
Cdd:cd05914   208 KFKLAKKinnRKIRKLAFKKVH--EAFGGNIKEFVIGGAKINPdvEEFLRTI----GFPYTIGYGMTETAPIISYS--PP 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4638 TDQELQPIGKPISNTEIFILNEagtlQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPE 4717
Cdd:cd05914   280 NRIRLGSAGKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAE 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4718 GNIEYAGRRDHQ-VKIRGYRVELGEVEAALLkhvQEAVVLAKE----NTDGQSDLYAYFTAEQSLSISQ------LKE-- 4784
Cdd:cd05914   350 GYLYIRGRKKEMiVLSSGKNIYPEEIEAKIN---NMPFVLESLvvvqEKKLVALAYIDPDFLDVKALKQrniidaIKWev 426
                         490       500       510
                  ....*....|....*....|....*....|....
gi 166797876 4785 --KLAGQIPGY-MIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd05914   427 rdKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
PRK05850 PRK05850
acyl-CoA synthetase; Validated
263-663 6.97e-20

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 97.71  E-value: 6.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKFKN---------DHLTYRELNEKASRLARTLRNCGVQPDTlVAILADRSLEMIVSIIAV 333
Cdd:PRK05850    1 SSVPSLLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  334 WKAGGAYVPLDPEYP---KERLQYLLHDADADVLL--------VQHHLKNSLAFDGPVI---DLNDEASyhaDCSLLSPV 399
Cdd:PRK05850   80 LQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLttsavvddVTEYVAPQPGQSAPPVievDLLDLDS---PRGSDARP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  400 AGHSHLAYVIYTSGTTGKPKGVMVEHGG-IVNSLQWKKAFFKHS----PADRVLVLY-PYVFD-AFILNFFGPLISGAT- 471
Cdd:PRK05850  157 RDLPSTAYLQYTSGSTRTPAGVMVSHRNvIANFEQLMSDYFGDTggvpPPDTTVVSWlPFYHDmGLVLGVCAPILGGCPa 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  472 ---------------LHLL----------PNeenketFAIQNAIKqerithfstsprllKTMIEQMNREDFIHVQHVVVG 526
Cdd:PRK05850  237 vltspvaflqrparwMQLLasnphafsaaPN------FAFELAVR--------------KTSDDDMAGLDLGGVLGIISG 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  527 GEQLETDTVEKL------HSLQPRIrINNEYGPTENSV-VSTFHPVQSAD------EQITIGS--PVANHQAYILGAHHQ 591
Cdd:PRK05850  297 SERVHPATLKRFadrfapFNLRETA-IRPSYGLAEATVyVATREPGQPPEsvrfdyEKLSAGHakRCETGGGTPLVSYGS 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  592 IQ---------------PIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLH-----VPGQKMYKTGDLArWLPDGRIEY 651
Cdd:PRK05850  376 PRsptvrivdpdtciecPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVdpspgTPEGPWLRTGDLG-FISEGELFI 454
                         490
                  ....*....|..
gi 166797876  652 LGRIDHQVKIRG 663
Cdd:PRK05850  455 VGRIKDLLIVDG 466
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1919-2258 7.21e-20

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 94.63  E-value: 7.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKGVLIEHGGL---TNYIWWAKEVYVKGEKANFPLYssISFDLTVTSIFTPLVTGNAIIVY-DGEDKTAL 1994
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTFfavPDILQKEGLNWVVGDVTYLPLP--ATHIGGLWWILTCLIHGGLCVTGgENTTYKSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1995 LESIVRDpRVDIIKLTPAHLQVLKEM---NIADQTAVRRMIVGGENLSTRLARSIheQFEGRIEICNEYGPTETVVGCMI 2071
Cdd:cd17635    84 FKILTTN-AVTTTCLVPTLLSKLVSElksANATVPSLRLIGYGGSRAIAADVRFI--EATGLTNTAQVYGLSETGTALCL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2072 yryDAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmyKTGD 2151
Cdd:cd17635   161 ---PTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------NTGD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2152 LAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLRKQ--- 2228
Cdd:cd17635   231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALkht 310
                         330       340       350
                  ....*....|....*....|....*....|
gi 166797876 2229 LSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:cd17635   311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
259-744 8.40e-20

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 97.63  E-value: 8.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  259 FSGSRT--VYQLFEEQAERTPENAAVKFKND------HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSI 330
Cdd:cd05966    47 FEGGKLniSYNCLDRHLKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAM 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  331 IAVWKAG-------GAYVPldpeypkERLQYLLHDADADVL--------------------------------LVQHHLK 371
Cdd:cd05966   127 LACARIGavhsvvfAGFSA-------ESLADRINDAQCKLVitadggyrggkviplkeivdealekcpsvekvLVVKRTG 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  372 NSLAF-DGPVIDLNDE-ASYHADCSllsPVAGHS-HLAYVIYTSGTTGKPKGVMVEHGGIvnsLQWKKAFFKhspadrvl 448
Cdd:cd05966   200 GEVPMtEGRDLWWHDLmAKQSPECE---PEWMDSeDPLFILYTSGSTGKPKGVVHTTGGY---LLYAATTFK-------- 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  449 vlypYVFDA-------------------FILnfFGPLISGATLHLL---PNEENKETFaiQNAIKQERITHFSTSP---- 502
Cdd:cd05966   266 ----YVFDYhpddiywctadigwitghsYIV--YGPLANGATTVMFegtPTYPDPGRY--WDIVEKHKVTIFYTAPtair 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  503 ------------------RLLKTMIEQMNREDFiHVQHVVVGGE---------QLETDTveklhslqprIRINNEYGPTE 555
Cdd:cd05966   338 almkfgdewvkkhdlsslRVLGSVGEPINPEAW-MWYYEVIGKErcpivdtwwQTETGG----------IMITPLPGATP 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  556 ---NSVVSTFHPVQSA--DEQitiGSPVANHQAyilgahhqiqpigipGELYVGGA--GVARGYLNRPELTEEKFVEHlh 628
Cdd:cd05966   407 lkpGSATRPFFGIEPAilDEE---GNEVEGEVE---------------GYLVIKRPwpGMARTIYGDHERYEDTYFSK-- 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  629 VPGqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSL 708
Cdd:cd05966   467 FPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGE 544
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 166797876  709 TAAQ-FREEL----SRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd05966   545 EPSDeLRKELrkhvRKEIGPIATPDKIQFVPGLPKTRSGKI 585
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
4356-4755 9.62e-20

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 96.54  E-value: 9.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:cd05904    31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 CAGHA--IPPL---------FEGEVLLLDDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHK---TMTNLL 4501
Cdd:cd05904   111 TAELAekLASLalpvvlldsAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRnliAMVAQF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4502 AYEQDHTQLRFDRVLQFAAM----SFDVCyqeMFSALSSGGILFIIGneaKRDIRQLNDFVRTHGIQTAFL-PTAFLKLl 4576
Cdd:cd05904   191 VAGEGSNSDSEDVFLCVLPMfhiyGLSSF---ALGLLRLGATVVVMP---RFDLEELLAAIERYKVTHLPVvPPIVLAL- 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4577 asekhyfepfaecVDHIIAAGEQLIATRML--------RDMLAR-----HQVTLHNHYGPSE-THVVTMYTVDPDTDQEL 4642
Cdd:cd05904   264 -------------VKSPIVDKYDLSSLRQImsgaaplgKELIEAfrakfPNVDLGQGYGMTEsTGVVAMCFAPEKDRAKY 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4643 QPIGKPISNTEIFILN-EAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPhpydsnQRMYKTGDLARYLPEGNIE 4721
Cdd:cd05904   331 GSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK------EGWLHTGDLCYIDEDGYLF 404
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 166797876 4722 YAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVV 4755
Cdd:cd05904   405 IVDRLKELIKYKGFQVAPAELEALLLSHpeILDAAV 440
PRK06188 PRK06188
acyl-CoA synthetase; Validated
3295-3713 1.60e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 96.21  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3295 RTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRY 3374
Cdd:PRK06188   24 RYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3375 ILNDSSISVLLY---------------CGKLQD--DIGFSGTCIDLMEEhFYHEKDSSLALSYQSSQLAYAIYTSGTTGK 3437
Cdd:PRK06188  104 VLEDAGISTLIVdpapfveralallarVPSLKHvlTLGPVPDGVDLLAA-AAKFGPAPLVAAALPPDIAGLAYTGGTTGK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3438 PKGTLIEHRQVIHLIEGLsrqvYSAYDAELNIAMLAPYYFD-ASVQQMYASLLSGHTLFIVPKeivSDGAALCRYYRQHS 3516
Cdd:PRK06188  183 PKGVMGTHRSIATMAQIQ----LAEWEWPADPRFLMCTPLShAGGAFFLPTLLRGGTVIVLAK---FDPAEVLRAIEEQR 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3517 IDITDGTPAHLKLLIAAGDLQGV---TLQHLLIGGEALSKTTVNKLKQLFGehgaaPGITNVYGPTETCVDAS-LFNIEC 3592
Cdd:PRK06188  256 ITATFLVPTMIYALLDHPDLRTRdlsSLETVYYGASPMSPVRLAEAIERFG-----PIFAQYYGQTEAPMVITyLRKRDH 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3593 SSDAWARSQNyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDL 3672
Cdd:PRK06188  331 DPDDPKRLTS---CGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGWLHTGDV 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 166797876 3673 ARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:PRK06188  401 AREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV 441
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
258-749 1.61e-19

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 95.90  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  258 DFSGSRTVYQLFEEQAERTPENAAVKFKN-----DHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIA 332
Cdd:PRK08008    2 DIVGGQHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  333 VWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ---------------HHLKNSL-------AFDGpVIDLNDEASYH 390
Cdd:PRK08008   82 LAKIGAIMVPINARLLREESAWILQNSQASLLVTSaqfypmyrqiqqedaTPLRHICltrvalpADDG-VSSFTQLKAQQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  391 ADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEH-----GGIVNSlqWKKAFFKHspaDRVLVLYPyvfdAFILNF--- 462
Cdd:PRK08008  161 PATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYSA--WQCALRDD---DVYLTVMP----AFHIDCqct 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  463 --FGPLISGATLHLLpneENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNRED-----------FIHVQhvvvggEQ 529
Cdd:PRK08008  232 aaMAAFSAGATFVLL---EKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANdrqhclrevmfYLNLS------DQ 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  530 lETDTVEKLHSlqprIRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGG-AG- 607
Cdd:PRK08008  303 -EKDAFEERFG----VRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGk 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  608 -VARGYLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREA 684
Cdd:PRK08008  378 tIFKEYYLDPKATAKVLEADgwLH--------TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDI 449
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876  685 AVVAREDADGAKQLYAYYV---GEpSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK08008  450 VVVGIKDSIRDEAIKAFVVlneGE-TLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1788-2261 1.71e-19

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 95.62  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQpVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:PRK07638   15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDVRKQLAYEGVTVLLDDE-----SSYHQDGsdlAPISDVSHLA-YVIYTSGSTGRPKGVLIEHGG-LT 1940
Cdd:PRK07638   94 AISNADMIVTERYKLNDLPDEEGRVIEIDEwkrmiEKYLPTY---APIENVQNAPfYMGFTSGSTGKPKAFLRAQQSwLH 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1941 NYIWWAKEVYVKGE-KANFP--------LYSSIS---FDLTVTSI--FTPLVTGNAIivyDGEDktallesivrdprVDI 2006
Cdd:PRK07638  171 SFDCNVHDFHMKREdSVLIAgtlvhslfLYGAIStlyVGQTVHLMrkFIPNQVLDKL---ETEN-------------ISV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2007 IKLTPAHLQVLKEMNIADQTAVrRMIVGGENLSTRLARSIHEQFEgRIEICNEYGPTEtvVGCMIYRYDAAKDRRESvPI 2086
Cdd:PRK07638  235 MYTVPTMLESLYKENRVIENKM-KIISSGAKWEAEAKEKIKNIFP-YAKLYEFYGASE--LSFVTALVDEESERRPN-SV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2087 GTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELtaekfvddPFEPGAKMYKTGDLAKWL-ADGNIEYAG 2165
Cdd:PRK07638  310 GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL--------ARELNADGWMTVRDVGYEdEEGFIYIVG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2166 RIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYvsGGQTTAARLRKQLSQTLASYMVPAYFIEL 2245
Cdd:PRK07638  382 REKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKSFCLQRLSSFKIPKEWHFV 459
                         490
                  ....*....|....*.
gi 166797876 2246 DEMPLTSNGKINKKGL 2261
Cdd:PRK07638  460 DEIPYTNSGKIARMEA 475
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1778-2261 1.81e-19

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 96.24  E-value: 1.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1778 QLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:PRK07059   27 DLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDS--QAGIVL------MQRDVRKQ-------------LAYEGVTV--------------LLDDESSYHQ 1902
Cdd:PRK07059  107 YTPRELEHQLKDSgaEAIVVLenfattVQQVLAKTavkhvvvasmgdlLGFKGHIVnfvvrrvkkmvpawSLPGHVRFND 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1903 -----DGSDLAPIS-DVSHLAYVIYTSGSTGRPKGVLIEHGG-LTNYIW---WAKEVYVKG---EKANF----PLYSSis 1965
Cdd:PRK07059  187 alaegARQTFKPVKlGPDDVAFLQYTGGTTGVSKGATLLHRNiVANVLQmeaWLQPAFEKKprpDQLNFvcalPLYHI-- 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1966 FDLTVTSIFTPLVTGNAIIVYDGEDKTALLESIVRD-----PRV-----------DIIKLTPAHLQVLKEMNIADQTAVr 2029
Cdd:PRK07059  265 FALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYqvhifPAVntlynallnnpDFDKLDFSKLIVANGGGMAVQRPV- 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2030 rmivgGENLSTRLARSIHEQfegrieicneYGPTET--VVGCmiYRYDAAKdrrESVPIGTAAANTSIYVLDENMKPAPI 2107
Cdd:PRK07059  344 -----AERWLEMTGCPITEG----------YGLSETspVATC--NPVDATE---FSGTIGLPLPSTEVSIRDDDGNDLPL 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2108 GVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAAL 2187
Cdd:PRK07059  404 GEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 2188 LQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQT-TAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK07059  478 ASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPAlTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
289-771 1.82e-19

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 96.00  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLV-- 366
Cdd:cd05932     7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  367 -------QHHLKNSLA--FDGPVIDLNDEASYHADCSLLSPVAGHS-----HLAYVIYTSGTTGKPKGVMVEHGGIVNSL 432
Cdd:cd05932    87 lddwkamAPGVPEGLIsiSLPPPSAANCQYQWDDLIAQHPPLEERPtrfpeQLATLIYTSGTTGQPKGVMLTFGSFAWAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  433 QWKKAFFKHSPADRVLVLYP--YVFDAfILNFFGPLISGATLHLLpneENKETFaIQNaIKQERITHFSTSPRLLKTMie 510
Cdd:cd05932   167 QAGIEHIGTEENDRMLSYLPlaHVTER-VFVEGGSLYGGVLVAFA---ESLDTF-VED-VQRARPTLFFSVPRLWTKF-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  511 QMNREDFI-----------------------------HVQHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTENSVVSt 561
Cdd:cd05932   239 QQGVQDKIpqqklnlllkipvvnslvkrkvlkglgldQCRLAGCGSAPVPPALLEWYRSLG--LNILEAYGMTENFAYS- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  562 fHPVQSADEQI-TIGSPVANHQAyilgahhqiqPIGIPGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGDL 640
Cdd:cd05932   316 -HLNYPGRDKIgTVGNAGPGVEV----------RISEDGEILVRSPALMMGYYKDPEATAEAFTA------DGFLRTGDK 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  641 ARWLPDGRIEYLGRIDHQVKI-RGYRIEIGEVEAAMFNLENVrEAAVVAREDAdGAKQLYAYYVGEPSLTA-AQFREELS 718
Cdd:cd05932   379 GELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGL-PAPLALVVLSEEARLRAdAFARAELE 456
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876  719 RELPNYmipsrfipLERIpltsNGKID----LKALPAADENTRAENEYIAP-----RNTIEE 771
Cdd:cd05932   457 ASLRAH--------LARV----NSTLDsheqLAGIVVVKDPWSIDNGILTPtlkikRNVLEK 506
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
3283-3781 1.84e-19

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 96.43  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3283 KTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAK-GVQADQLVGIMTERSLEMVVGILGVLKAGGAYL 3361
Cdd:PRK12492   24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3362 PIDPDSPSERIRYILNDSSISVLLYC---GKLQDDIgFSGTCIDLMEEHFYHEKDSSL---------------------- 3416
Cdd:PRK12492  104 NTNPLYTAREMRHQFKDSGARALVYLnmfGKLVQEV-LPDTGIEYLIEAKMGDLLPAAkgwlvntvvdkvkkmvpayhlp 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3417 -ALSYQSS-----------------QLAYAIYTSGTTGKPKGTLIEHRQVIHLIEglsrQVYSAYDA----------ELN 3468
Cdd:PRK12492  183 qAVPFKQAlrqgrglslkpvpvgldDIAVLQYTGGTTGLAKGAMLTHGNLVANML----QVRACLSQlgpdgqplmkEGQ 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3469 IAMLAP------YYFDASVQQMyasLLSG-HTLFIV-PKEIvsdgAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVT 3540
Cdd:PRK12492  259 EVMIAPlplyhiYAFTANCMCM---MVSGnHNVLITnPRDI----PGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLD 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3541 LQHLLI---GGEALSKTTVNKLKQLFGehgaaPGITNVYGPTETCVDASlfniecsSDAWARSQNYVPIGKPLGRNRMYI 3617
Cdd:PRK12492  332 FSALKLtnsGGTALVKATAERWEQLTG-----CTIVEGYGLTETSPVAS-------TNPYGELARLGTVGIPVPGTALKV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3618 LDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEYIGRIDHQVKIQGFR 3697
Cdd:PRK12492  400 IDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFN 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3698 IELGEIESVMLNVPDIQE-AAAAALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKL 3776
Cdd:PRK12492  474 VYPNEIEDVVMAHPKVANcAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553

                  ....*
gi 166797876 3777 NRQLL 3781
Cdd:PRK12492  554 LRREL 558
PRK09274 PRK09274
peptide synthase; Provisional
1782-2166 2.87e-19

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 95.74  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1782 EQSQRTPDQAAVIDKD----------RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAY 1851
Cdd:PRK09274   14 RAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1852 VPIDPEYPQDRIRYMLDDSQA----GIVLMQ----------RDVRKQLAYE-----GVTVLldDESSYHQDGSDLAPI-S 1911
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAQPdafiGIPKAHlarrlfgwgkPSVRRLVTVGgrllwGGTTL--ATLLRDGAAAPFPMAdL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1912 DVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVY--VKGEK--ANFPLYSSISFDLTVTSIFTPLVTGNAIIVyd 1987
Cdd:PRK09274  172 APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYgiEPGEIdlPTFPLFALFGPALGMTSVIPDMDPTRPATV-- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1988 geDKTALLESIvRDPRVDIIKLTPAHLQVL----KEMNIADQTaVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPT 2063
Cdd:PRK09274  250 --DPAKLFAAI-ERYGVTNLFGSPALLERLgrygEANGIKLPS-LRRVISAGAPVPIAVIERFRAMLPPDAEILTPYGAT 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2064 ETVVGCMI------YRYDAAKDRRESVPIGTAAANTSIYVLD---------ENMKPAPIGVPGEIYISGAGVARGYLNRP 2128
Cdd:PRK09274  326 EALPISSIesreilFATRAATDNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRP 405
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 166797876 2129 ELTAEKFVDDPfePGAKMYKTGDLAkWL-ADGNIEYAGR 2166
Cdd:PRK09274  406 EATRLAKIPDG--QGDVWHRMGDLG-YLdAQGRLWFCGR 441
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
4333-4813 2.92e-19

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 95.72  E-value: 2.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMF------GNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAG 4406
Cdd:cd17634    54 LAANALDRHLRENGDRTAIIYegddtsQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4407 AAFLPIDPELPEKRRAFMLKDSGADVLLTC-----AGHAIPPLFEGE------------VLLLD---------------- 4453
Cdd:cd17634   134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITAdggvrAGRSVPLKKNVDdalnpnvtsvehVIVLKrtgsdidwqegrdlww 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4454 DPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQleHKTMTNLLAYEQDHTQLrFDRVLQFAAMSF-DVCYQEMFS 4532
Cdd:cd17634   214 RDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMKYV-FDYGPGDIYWCTaDVGWVTGHS 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4533 ALSSGGIL------FIIGNEAKRDIRQLNDFVRTHGIQTAFL-PTAFLKLLASEKHYFEPFAECVDHII-AAGEQL--IA 4602
Cdd:cd17634   291 YLLYGPLAcgattlLYEGVPNWPTPARMWQVVDKHGVNILYTaPTAIRALMAAGDDAIEGTDRSSLRILgSVGEPInpEA 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4603 TRMLRDMLARHQVTLHNHYGPSEThvvTMYTVDPDTDQELQPIG---KPISNTEIFILNEAGTLQPVGIVGELCIsGVSL 4679
Cdd:cd17634   371 YEWYWKKIGKEKCPVVDTWWQTET---GGFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVI-TDPW 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4680 ---ARGYHNRESLTLETFvphpYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQE-A 4753
Cdd:cd17634   447 pgqTRTLFGDHERFEQTY----FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHpkVAEaA 522
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 4754 VVLAKENTDGQSdLYAYFTAEQSLSIS-----QLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:cd17634   523 VVGIPHAIKGQA-PYAYVVLNHGVEPSpelyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK05857 PRK05857
fatty acid--CoA ligase;
1771-2263 3.02e-19

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 95.46  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1771 FPQTPVHQLFEeQSQRTPDQAAV--IDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSG 1848
Cdd:PRK05857   12 LPSTVLDRVFE-QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1849 GAYVPIDPEYPQDRIRYMLDDSQAGIVLMQRD--VRKQLAYEGVTVLLDDESSYHQDGSDLAPISDVSHLA--------- 1917
Cdd:PRK05857   91 AIAVMADGNLPIAAIERFCQITDPAAALVAPGskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAgnadqgsed 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1918 --YVIYTSGSTGRPKGVL------------IEHGGLtNYIWWakevyVKGEKANFPLYSSISFDLtvTSIFTPLVTGNAI 1983
Cdd:PRK05857  171 plAMIFTSGTTGEPKAVLlanrtffavpdiLQKEGL-NWVTW-----VVGETTYSPLPATHIGGL--WWILTCLMHGGLC 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1984 IVydGEDKTALLESIVRDPRVDIIKLTPAHL-QVLKEMNIADQT--AVRRMIVGGENLSTRLARSIHeqfEGRIEICNEY 2060
Cdd:PRK05857  243 VT--GGENTTSLLEILTTNAVATTCLVPTLLsKLVSELKSANATvpSLRLVGYGGSRAIAADVRFIE---ATGVRTAQVY 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2061 GPTETvvGCM---IYRYDAAKDRRESVPIGTAAANTSIYVLDEN------MKPAPIGVPGEIYISGAGVARGYLNRPELT 2131
Cdd:PRK05857  318 GLSET--GCTalcLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERT 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2132 AEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAalLQEEV--IKEAVVTAREDVH---- 2205
Cdd:PRK05857  396 AEVLIDG-------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDR--IAEGVsgVREAACYEIPDEEfgal 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 2206 -GFKQLCAYYVSGG------QTTAARLRKQlSQTLASymvPAYFIELDEMPLTSNGKINKKGLPA 2263
Cdd:PRK05857  467 vGLAVVASAELDESaaralkHTIAARFRRE-SEPMAR---PSTIVIVTDIPRTQSGKVMRASLAA 527
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
281-749 3.20e-19

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 95.29  E-value: 3.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  281 AVKFKNDH----LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:cd17642    33 TIAFTDAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLLVQH-------HLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHS------------------HLAYVIYT 411
Cdd:cd17642   113 NISKPTIVFCSKkglqkvlNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLppgfneydfkppsfdrdeQVALIMNS 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  412 SGTTGKPKGVMVEHGGIVnslqwkkAFFKH----------SPADRVLVLYPYvFDAF-ILNFFGPLISGATLHLLPNEEn 480
Cdd:cd17642   193 SGSTGLPKGVQLTHKNIV-------ARFSHardpifgnqiIPDTAILTVIPF-HHGFgMFTTLGYLICGFRVVLMYKFE- 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  481 KETFAiqNAIKQERITHFSTSPRLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTVEklhSLQPRIRIN---NEYGPTE 555
Cdd:cd17642   264 EELFL--RSLQDYKVQSALLVPTLFAFFAKStlVDKYDLSNLHEIASGGAPLSKEVGE---AVAKRFKLPgirQGYGLTE 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  556 NSVVSTFHPvQSADEQITIGSPVANHQAYI--------LGAHHQiqpigipGELYVGGAGVARGYLNRPELTEEKFVEH- 626
Cdd:cd17642   339 TTSAILITP-EGDDKPGAVGKVVPFFYAKVvdldtgktLGPNER-------GELCVKGPMIMKGYVNNPEATKALIDKDg 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  627 -LHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGE 705
Cdd:cd17642   411 wLH--------SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876  706 PSLTAAQfreelsRELPNYmIPSRFIPLER----------IPLTSNGKIDLKAL 749
Cdd:cd17642   483 AGKTMTE------KEVMDY-VASQVSTAKRlrggvkfvdeVPKGLTGKIDRRKI 529
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
3294-3781 3.74e-19

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 95.06  E-value: 3.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3294 HRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAG---------------G 3358
Cdd:PRK10946   34 HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGvapvnalfshqrselN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3359 AY-LPIDP-----------------------DSPSERIRYILNDSSISVLLycgklqddigfsgtciDLMEehfyHEKDS 3414
Cdd:PRK10946  114 AYaSQIEPalliadrqhalfsdddflntlvaEHSSLRVVLLLNDDGEHSLD----------------DAIN----HPAED 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3415 SLALSYQSSQLAYAIYTSGTTGKPKgtLI--EHRQVIHLIEGlsrqvySAYDAELN------IAMLAPYYFDASVQQMYA 3486
Cdd:PRK10946  174 FTATPSPADEVAFFQLSGGSTGTPK--LIprTHNDYYYSVRR------SVEICGFTpqtrylCALPAAHNYPMSSPGALG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3487 SLLSGHTLFIVPkeivSDGAALC-RYYRQHSIDITDGTPAHLKLLIAAGDLQG-----VTLQHLLIGGEALSKTTVN--- 3557
Cdd:PRK10946  246 VFLAGGTVVLAP----DPSATLCfPLIEKHQVNVTALVPPAVSLWLQAIAEGGsraqlASLKLLQVGGARLSETLARrip 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3558 -----KLKQLFGehgAAPGITNvYgpteTCVDAS---LFNiecssdawarSQnyvpiGKPL-GRNRMYILDSKKRLQPKG 3628
Cdd:PRK10946  322 aelgcQLQQVFG---MAEGLVN-Y----TRLDDSderIFT----------TQ-----GRPMsPDDEVWVADADGNPLPQG 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3629 VQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVML 3708
Cdd:PRK10946  379 EVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL 452
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 3709 NVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRkrmaRHLPG-----YMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK10946  453 RHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLR----RFLREqgiaeFKLPDRVECVDSLPLTAVGKVDKKQL 526
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1787-2279 3.95e-19

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 95.46  E-value: 3.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1787 TPDQAAVI------DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSG-------GAYVP 1853
Cdd:cd05967    64 RGDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1854 ------ID---PEY---------PQDRIRY--MLDD--SQAG------IVLMQRDVRKQLAYEGVTVLLDDESSYHQDgS 1905
Cdd:cd05967   144 kelasrIDdakPKLivtascgiePGKVVPYkpLLDKalELSGhkphhvLVLNRPQVPADLTKPGRDLDWSELLAKAEP-V 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1906 DLAPIsDVSHLAYVIYTSGSTGRPKGVLIEHGG---LTNY------------IWW-AKEV-YVKGekanfplYSSIsfdl 1968
Cdd:cd05967   223 DCVPV-AATDPLYILYTSGTTGKPKGVVRDNGGhavALNWsmrniygikpgdVWWaASDVgWVVG-------HSYI---- 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1969 tvtsIFTPLVTGNAIIVYDGE-----DKTALLeSIVRDPRVDIIKLTPAHLQVLK-------EMNIADQTAVRRMIVGGE 2036
Cdd:cd05967   291 ----VYGPLLHGATTVLYEGKpvgtpDPGAFW-RVIEKYQVNALFTAPTAIRAIRkedpdgkYIKKYDLSSLRTLFLAGE 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2037 NLSTRLARSIHEQFegRIEICNEYGPTETvvGCMIyrydAAKDR-RESVPIGTAAANTSIY-----VLDENMKPAPIGVP 2110
Cdd:cd05967   366 RLDPPTLEWAENTL--GVPVIDHWWQTET--GWPI----TANPVgLEPLPIKAGSPGKPVPgyqvqVLDEDGEPVGPNEL 437
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2111 GEIYISGAgVARGYLNRPELTAEKFVDDPFE--PGakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALL 2188
Cdd:cd05967   438 GNIVIKLP-LPPGCLLTLWKNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2189 QEEVIKE-AVVTAREDVHGfkQL-CAYYV--SGGQTTAARLRKQLSQTLASYMVP-AYF---IELDEMPLTSNGKINKKG 2260
Cdd:cd05967   515 SHPAVAEcAVVGVRDELKG--QVpLGLVVlkEGVKITAEELEKELVALVREQIGPvAAFrlvIFVKRLPKTRSGKILRRT 592
                         570
                  ....*....|....*....
gi 166797876 2261 LPApdfeLQDRAEYKAPRT 2279
Cdd:cd05967   593 LRK----IADGEDYTIPST 607
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
268-744 4.61e-19

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 95.12  E-value: 4.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  268 LFEEQAERTPENAAvkFKN--DHLTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLD 344
Cdd:PRK08974   28 MFEQAVARYADQPA--FINmgEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  345 PEYPKERLQYLLHDADADVLLVQHHLKNSL---AFDGPV-----IDLNDEAS--------------------YHADCSL- 395
Cdd:PRK08974  106 PLYTPRELEHQLNDSGAKAIVIVSNFAHTLekvVFKTPVkhvilTRMGDQLStakgtlvnfvvkyikrlvpkYHLPDAIs 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  396 -------------LSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIV-NSLQWKKAFfkhSPADRV--------LVLYpY 453
Cdd:PRK08974  186 frsalhkgrrmqyVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAY---GPLLHPgkelvvtaLPLY-H 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  454 VFdAFILNFFGPLISGATLHLLPNEENKETFAIQnaIKQERITHFSTSPRLLKTMI--EQMNREDFIHVQHVVVGGEQLE 531
Cdd:PRK08974  262 IF-ALTVNCLLFIELGGQNLLITNPRDIPGFVKE--LKKYPFTAITGVNTLFNALLnnEEFQELDFSSLKLSVGGGMAVQ 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  532 TDTVEKLHSLQPRiRINNEYGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARG 611
Cdd:PRK08974  339 QAVAERWVKLTGQ-YLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLG 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  612 YLNRPELTEEkfvehlhVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVARED 691
Cdd:PRK08974  418 YWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPS 490
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876  692 ADGAKQLYAYYVG-EPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK08974  491 EVSGEAVKIFVVKkDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
3593-3867 4.62e-19

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 91.35  E-value: 4.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3593 SSDAWARSQNYVPIGKPLGRNRMYILDskkrLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDL 3672
Cdd:COG3433     9 APPTPDEPPPVIPPAIVQARALLLIVD----LQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3673 ARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVML----NVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRKR 3748
Cdd:COG3433    85 LRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLvlraAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3749 MARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKKRDSGIEYVPPQTSAEI---QLTAIWEDVLGL--EQVGIRDH 3823
Cdd:COG3433   165 LDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALteeELRADVAELLGVdpEEIDPDDN 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 166797876 3824 FFEIGGHSLRATALIAKIQKQmHVQIPLRDVFRFPTIEQLARTI 3867
Cdd:COG3433   245 LFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALL 287
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1787-2260 4.73e-19

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 94.81  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1787 TPDQAAVIDKD-----RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY--- 1858
Cdd:cd05921     8 APDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslm 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 PQD--RIRYMLDDSQAGIVLMQ-----RDVRKQLAYEGVTVL-----LDDESSYHQDgSDLA--PISDVSHL-------- 1916
Cdd:cd05921    88 SQDlaKLKHLFELLKPGLVFAQdaapfARALAAIFPLGTPLVvsrnaVAGRGAISFA-ELAAtpPTAAVDAAfaavgpdt 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1917 -AYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVY-VKGEKA---------NFPLYSSISFDLTvtsiftpLVTGNAIIV 1985
Cdd:cd05921   167 vAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYpFFGEEPpvlvdwlpwNHTFGGNHNFNLV-------LYNGGTLYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1986 YDGEDKTALLESIVRDPRvdiiKLTP-AHLQVLK--EMNIA----DQTAVRR-------MIVGGENLST----RLARSIH 2047
Cdd:cd05921   240 DDGKPMPGGFEETLRNLR----EISPtVYFNVPAgwEMLVAalekDEALRRRffkrlklMFYAGAGLSQdvwdRLQALAV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2048 EQFEGRIEICNEYGPTETVVGCMIYRYDAAKDRRESVPI-GTAaantsiyvldenMKPAPIGVPGEIYISGAGVARGYLN 2126
Cdd:cd05921   316 ATVGERIPMMAGLGATETAPTATFTHWPTERSGLIGLPApGTE------------LKLVPSGGKYEVRVKGPNVTPGYWR 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2127 RPELTAEKFVDDPFepgakmYKTGDLAKwLADGN-----IEYAGRIDEQVKIR-GYRIELGEIEAALLQE--EVIKEAVV 2198
Cdd:cd05921   384 QPELTAQAFDEEGF------YCLGDAAK-LADPDdpakgLVFDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHDAVV 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2199 TA--RE--------DVHGFKQLcayyvSGGQ-------TTAARLRKQLSQTLA--------SYMVPAYFIELDEMPLTSN 2253
Cdd:cd05921   457 AGedRAevgalvfpDLLACRRL-----VGLQeasdaevLRHAKVRAAFRDRLAalngeatgSSSRIARALLLDEPPSIDK 531

                  ....*..
gi 166797876 2254 GKINKKG 2260
Cdd:cd05921   532 GEITDKG 538
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
4347-4828 5.07e-19

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 94.96  E-value: 5.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4347 DHEAVMF----GNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIdpelpekRRA 4422
Cdd:PRK04319   59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL-------FEA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4423 FM-------LKDSGADVLLTcaghaIPPLFE----GE------VLLLDDPLLYQGRTDNLN------------LSCSEND 4473
Cdd:PRK04319  132 FMeeavrdrLEDSEAKVLIT-----TPALLErkpaDDlpslkhVLLVGEDVEEGPGTLDFNalmeqasdefdiEWTDRED 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4474 LMYVIYTSGTTGQPKGVQLEHKTMTNLLA---YEQDhtqLRFDRVLQFAA-------MSFDVcyqemFSALSSGGILFII 4543
Cdd:PRK04319  207 GAILHYTSGSTGKPKGVLHVHNAMLQHYQtgkYVLD---LHEDDVYWCTAdpgwvtgTSYGI-----FAPWLNGATNVID 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4544 GNE--AKRDIRQLNDFvrthGIQ---TAflPTAFLKLLaseKHYFEPFAE----CVDHIIAAGEQL--IATRMLRDMLAR 4612
Cdd:PRK04319  279 GGRfsPERWYRILEDY----KVTvwyTA--PTAIRMLM---GAGDDLVKKydlsSLRHILSVGEPLnpEVVRWGMKVFGL 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4613 hqvTLHNHYGPSET--HVVTMYtvdPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCI-SG-VSLARGYHNRES 4688
Cdd:PRK04319  350 ---PIHDNWWMTETggIMIANY---PAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNPE 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4689 LTLETFVPHpydsnqrMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAK-------- 4758
Cdd:PRK04319  424 KYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHpaVAEAGVIGKpdpvrgei 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4759 -----------ENTDgqsdlyayftaEQSLSISQL-KEKLAGQIPgymiPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQ 4826
Cdd:PRK04319  497 ikafvalrpgyEPSE-----------ELKEEIRGFvKKGLGAHAA----PREIEFKDKLPKTRSGKIMRRVLKAWELGLP 561

                  ..
gi 166797876 4827 TG 4828
Cdd:PRK04319  562 EG 563
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
4473-4815 5.19e-19

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 91.70  E-value: 5.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 DLMYVIYTSGTTGQPKGVQLEHKT-MTNLLAYEQDHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIIGN-EAKRD 4550
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSwIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKfNPKSW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4551 IRQLNdfvrTHGIQTAFLPTAFLKLLASEKhyfEPFAECVdhIIAAGEQLIATRMLRDmLARH--QVTLHNHYGPSETHV 4628
Cdd:cd17633    81 IRKIN----QYNATVIYLVPTMLQALARTL---EPESKIK--SIFSSGQKLFESTKKK-LKNIfpKANLIEFYGTSELSF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4629 VTmYTVDpdtdQELQP---IGKPISNTEIFILNEAGtlqpvGIVGELCISGVSLARGYHNRESLtletfvphpydSNQRM 4705
Cdd:cd17633   151 IT-YNFN----QESRPpnsVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFS-----------NPDGW 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4706 YKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQsLSISQLK 4783
Cdd:cd17633   210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIpgIEEAIVVGIPDARFGEIAVALYSGDK-LTYKQLK 288
                         330       340       350
                  ....*....|....*....|....*....|..
gi 166797876 4784 EKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd17633   289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
3304-3776 5.95e-19

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 93.94  E-value: 5.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3304 FEGKQFTYEELNRRANQLARTLQaKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISV 3383
Cdd:cd05909     3 TLGTSLTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3384 LL------------------------YCGKLQDDIGFSGTCIDLMEEHFYHEkdSSLALSY----QSSQLAYAIYTSGTT 3435
Cdd:cd05909    82 VLtskqfieklklhhlfdveydarivYLEDLRAKISKADKCKAFLAGKFPPK--WLLRIFGvapvQPDDPAVILFTSGSE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3436 GKPKGTLIEHRQVIHLIEglsrQVYSAYDAELNIAMLAPYYFDAS---VQQMYASLLSGHTLFIVPKEIvsDGAALCRYY 3512
Cdd:cd05909   160 GLPKGVVLSHKNLLANVE----QITAIFDPNPEDVVFGALPFFHSfglTGCLWLPLLSGIKVVFHPNPL--DYKKIPELI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3513 RQHSIDITDGTPAHLKLLI-AAGDLQGVTLQHLLIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETCVDASLfNIE 3591
Cdd:cd05909   234 YDKKATILLGTPTFLRGYArAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-----ILEGYGTTECSPVISV-NTP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3592 CSsdawARSQNYVpiGKPLgRNRMYILDSKKRLQPK--GVQGELYIAGDGVGRGYLNLPELTDekfvadpFVPEDRMYRT 3669
Cdd:cd05909   308 QS----PNKEGTV--GRPL-PGMEVKIVSVETHEEVpiGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDT 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3670 GDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELRkRM 3749
Cdd:cd05909   374 GDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLN-DI 452
                         490       500
                  ....*....|....*....|....*....
gi 166797876 3750 ARH--LPGYMIPAHFVQLDKMPLTPNGKL 3776
Cdd:cd05909   453 LKNagISNLAKPSYIHQVEEIPLLGTGKP 481
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
3424-3781 5.98e-19

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 91.62  E-value: 5.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3424 QLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVysAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLfivpkeIVS 3503
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL--GFGGGDSWLLSLPLYHVGGLAILVRSLLAGAEL------VLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3504 DGAALCRYYRQHS-IDITDGTPAHLKLLIAAGDLQG--VTLQHLLIGGEALSKTTVNKLKQLfgehgAAPGITnVYGPTE 3580
Cdd:cd17630    73 ERNQALAEDLAPPgVTHVSLVPTQLQRLLDSGQGPAalKSLRAVLLGGAPIPPELLERAADR-----GIPLYT-TYGMTE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3581 T--CVDASLFNIECSSDAwarsqnyvpiGKPLGRNRMYILDskkrlqpkgvQGELYIAGDGVGRGYLNLPELtdekfvad 3658
Cdd:cd17630   147 TasQVATKRPDGFGRGGV----------GVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLV-------- 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3659 PFVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdaddeyyLCGYFAADK 3738
Cdd:cd17630   199 PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD--------------AFVVGVPDE 264
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3739 T--------------IQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd17630   265 ElgqrpvavivgrgpADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
4333-4818 6.05e-19

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 94.70  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPI 4412
Cdd:PRK07059   24 SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4413 DPELPEKRRAFMLKDSGAD--VLLTCAGHAIPPLFE------------GEVLLLDDPL---------------------- 4456
Cdd:PRK07059  104 NPLYTPRELEHQLKDSGAEaiVVLENFATTVQQVLAktavkhvvvasmGDLLGFKGHIvnfvvrrvkkmvpawslpghvr 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4457 ----LYQGRTDNLN-LSCSENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLA-YEQDHTQL-----RFDRVLQFAAM---- 4521
Cdd:PRK07059  184 fndaLAEGARQTFKpVKLGPDDVAFLQYTGGTTGVSKGATLLHR---NIVAnVLQMEAWLqpafeKKPRPDQLNFVcalp 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4522 -----SFDVCYqemFSALSSGGILFIIGNeaKRDIRqlnDFVRT-HGIQTAFLP---TAFLKLLASE---KHYFEPFaec 4589
Cdd:PRK07059  261 lyhifALTVCG---LLGMRTGGRNILIPN--PRDIP---GFIKElKKYQVHIFPavnTLYNALLNNPdfdKLDFSKL--- 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4590 vdhIIAAG-----EQLIATRMLrdmlarhQVT---LHNHYGPSETHVVTmyTVDP-DTDQELQPIGKPISNTEIFILNEA 4660
Cdd:PRK07059  330 ---IVANGggmavQRPVAERWL-------EMTgcpITEGYGLSETSPVA--TCNPvDATEFSGTIGLPLPSTEVSIRDDD 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4661 GTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELG 4740
Cdd:PRK07059  398 GNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPN 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4741 EVEAALLKH--VQE-AVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRA 4817
Cdd:PRK07059  472 EIEEVVASHpgVLEvAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRE 551

                  .
gi 166797876 4818 L 4818
Cdd:PRK07059  552 L 552
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1919-2258 8.44e-19

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 91.18  E-value: 8.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKGVLIEHGGL------TNYIWW--AKEVYVkgekANFPLYSSISFDLTvtsiFTPLVTGNAIIVYDGED 1990
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLiaanlqLIHAMGltEADVYL----NMLPLFHIAGLNLA----LATFHAGGANVVMEKFD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1991 KTALLESIvRDPRVDIIKLTPAHLQVLKEMNIADQTAVR--RMIVGGENLSTrlarsIhEQFEgriEICNE-----YGPT 2063
Cdd:cd17637    77 PAEALELI-EEEKVTLMGSFPPILSNLLDAAEKSGVDLSslRHVLGLDAPET-----I-QRFE---ETTGAtfwslYGQT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2064 ETvvgCMIYRYDAAKDRRESVpiGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDpfepg 2143
Cdd:cd17637   147 ET---SGLVTLSPYRERPGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG----- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2144 akMYKTGDLAKWLADGNIEYAGRIDEQ--VKIRGYRIELGEIEAALLQEEVIKEAVVTAREDV---HGFKQLCAyyVSGG 2218
Cdd:cd17637   217 --WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPkwgEGIKAVCV--LKPG 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 166797876 2219 QT-TAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:cd17637   293 ATlTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1800-2161 8.75e-19

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 93.82  E-value: 8.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQT--DQPVAIITRNSIESVVGILAVLKSGGAYVPIdpeYPQ---DRIRYMLDDSQAGI 1874
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPL---YDTlgpEAIEYILNHAEISI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1875 VLMQRDVRkqlayegvTVLLDD-ESSYHQDGSDLAPiSDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKG 1953
Cdd:cd05927    83 VFCDAGVK--------VYSLEEfEKLGKKNKVPPPP-PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1954 EKANfPLYSSISFdLTVTSIFTPLV------TGNAIIVYDGEDKTaLLESI--------VRDPRV-----DIIKLTPAHL 2014
Cdd:cd05927   154 NKIN-PTDVYISY-LPLAHIFERVVealflyHGAKIGFYSGDIRL-LLDDIkalkptvfPGVPRVlnriyDKIFNKVQAK 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2015 QVLKEM--NIADQTAVRRMIVGGENLSTRLAR----SIHEQFEGRI------------------------EICNEYGPTE 2064
Cdd:cd05927   231 GPLKRKlfNFALNYKLAELRSGVVRASPFWDKlvfnKIKQALGGNVrlmltgsaplspevleflrvalgcPVLEGYGQTE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2065 TVVGCMIYRYD------------AAKDRRESVPigtaaaNTSIYVLDENMKpapigvpGEIYISGAGVARGYLNRPELTA 2132
Cdd:cd05927   311 CTAGATLTLPGdtsvghvggplpCAEVKLVDVP------EMNYDAKDPNPR-------GEVCIRGPNVFSGYYKDPEKTA 377
                         410       420
                  ....*....|....*....|....*....
gi 166797876 2133 EKFVDDPFepgakmYKTGDLAKWLADGNI 2161
Cdd:cd05927   378 EALDEDGW------LHTGDIGEWLPNGTL 400
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
402-749 9.11e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 91.77  E-value: 9.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  402 HSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYP--YVFdAFILNFFGPLISGATLHLLPNEE 479
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlfHVN-GSVVTLLTPLASGAHVVLAGPAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  480 NKETFAIQN---AIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLetdTVEKLHSLQPR--IRINNEYGPT 554
Cdd:cd05944    80 YRNPGLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPL---PVELRARFEDAtgLPVVEGYGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  555 ENSVVSTFHPVQSADEQITIGSPVANHQAYIL---GAHHQIQPIGIP--GELYVGGAGVARGYLNRpELTEEKFVEHLHV 629
Cdd:cd05944   157 EATCLVAVNPPDGPKRPGSVGLRLPYARVRIKvldGVGRLLRDCAPDevGEICVAGPGVFGGYLYT-EGNKNAFVADGWL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  630 pgqkmyKTGDLARWLPDGRIEYLGRIDHQVkIR-GYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP-- 706
Cdd:cd05944   236 ------NTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPga 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 166797876  707 SLTAAQFREELSRELPNY-MIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05944   309 VVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PLN02574 PLN02574
4-coumarate--CoA ligase-like
3288-3713 9.38e-19

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 94.14  E-value: 9.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3288 LFEEQAHrtPDNTAVV--FEGKQFTYEELNRRANQLARTL-QAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPID 3364
Cdd:PLN02574   46 IFSHHNH--NGDTALIdsSTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMN 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3365 PDSPSERIRYILNDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQS----------------SQLAYA 3428
Cdd:PLN02574  124 PSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYElikedfdfvpkpvikqDDVAAI 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3429 IYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYDA----ELNIAMLaPYYFDASVQQMYASLLS-GHTLFIVPKEIVS 3503
Cdd:PLN02574  204 MYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYpgsdNVYLAAL-PMFHIYGLSLFVVGLLSlGSTIVVMRRFDAS 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3504 DGA-ALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLIGGEALSKTTVNKLKQLFGEHGAAPGitnvYGPTE-T 3581
Cdd:PLN02574  283 DMVkVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQG----YGMTEsT 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3582 CVDASLFNIEcssdawaRSQNYVPIGKPLGRNRMYILD-SKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPF 3660
Cdd:PLN02574  359 AVGTRGFNTE-------KLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW 431
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876 3661 VpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:PLN02574  432 L------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEI 478
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
4341-4813 9.90e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 93.53  E-value: 9.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4341 QAERNPDHEAVMFGN--QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPE 4418
Cdd:PRK13390    6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4419 KRRAFMLKDSGADVLLTCAGhaipplFEGEVLLLDDP----LLYQGRTDNL-----NLSCSENDLM------YVIYTSGT 4483
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAA------LDGLAAKVGADlplrLSFGGEIDGFgsfeaALAGAGPRLTeqpcgaVMLYSSGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4484 TGQPKGVQlehktmTNLLAYEQDHTQlrfDRVLQFAAMSFDVCYQEMF---------SALSSGGILFIIGNE---AKR-D 4550
Cdd:PRK13390  160 TGFPKGIQ------PDLPGRDVDAPG---DPIVAIARAFYDISESDIYyssapiyhaAPLRWCSMVHALGGTvvlAKRfD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4551 IRQLNDFVRTHGIQ-TAFLPTAFLKLLASE----KHYFEPFAECVDHIIAAGEQLIATRMLrDMLARhqvTLHNHYGPSE 4625
Cdd:PRK13390  231 AQATLGHVERYRITvTQMVPTMFVRLLKLDadvrTRYDVSSLRAVIHAAAPCPVDVKHAMI-DWLGP---IVYEYYSSTE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4626 THVVTMYtvdpDTDQELQ---PIGKPISNTeIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVP-HPYDS 4701
Cdd:PRK13390  307 AHGMTFI----DSPDWLAhpgSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPaHPFWT 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4702 NqrmykTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDgqsdlyayfTAEQSLSI 4779
Cdd:PRK13390  382 T-----VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHpaVHDVAVIGVPDPE---------MGEQVKAV 447
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 4780 SQLKEKLAG--------------QIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:PRK13390  448 IQLVEGIRGsdelarelidytrsRIAHYKAPRSVEFVDELPRTPTGKL 495
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
3310-3711 1.09e-18

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 93.43  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3310 TYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGgayLPIDP--DSPSER-IRYILNDSSiSVLLY 3386
Cdd:cd17639     7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTvyATLGEDaLIHSLNETE-CSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3387 CGKLQDDIgfsgTCIdlmeehfyhekdsslalsyqssqlayaIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYS----- 3461
Cdd:cd17639    83 TDGKPDDL----ACI---------------------------MYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEllgpd 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3462 ---------AYDAELNIAMLAPYY------------FDASVQQMYASLLSGH-TLFI-VP-------KEI---VSDGAAL 3508
Cdd:cd17639   132 drylaylplAHIFELAAENVCLYRggtigygsprtlTDKSKRGCKGDLTEFKpTLMVgVPaiwdtirKGVlakLNPMGGL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3509 CR-------YYRQHSIDITDGTPAHLKLLIA-AGDLQGVTLQHLLIGGEALSKTTVNKLKQLFGEhgaapgITNVYGPTE 3580
Cdd:cd17639   212 KRtlfwtayQSKLKALKEGPGTPLLDELVFKkVRAALGGRLRYMLSGGAPLSADTQEFLNIVLCP------VIQGYGLTE 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3581 TCVDASLFNIECssdawarsQNYVPIGKPLGRNRMYILD------SKKRLQPkgvQGELYIAGDGVGRGYLNLPELTDEK 3654
Cdd:cd17639   286 TCAGGTVQDPGD--------LETGRVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKEA 354
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 3655 FVadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQ-GFRIELGEIESVMLNVP 3711
Cdd:cd17639   355 FD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNP 406
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
852-1278 1.42e-18

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 92.05  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  852 LTPIQH--WFFEQKMPHAHHYNQAvmlySAEGFKeGP-----LRRTMERIASHHDALRMIFEKTPDGYAPRItgtDESEL 924
Cdd:cd19533     4 LTSAQRgvWFAEQLDPEGSIYNLA----EYLEIT-GPvdlavLERALRQVIAEAETLRLRFTEEEGEPYQWI---DPYTP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  925 FHLEVMNYKGETDPAQAIAD-KANEIQSSMVLDKGPLMKLGLFQCPDGDHLLIA-IHHLLIDGVSWRILLEDFASGYeQA 1002
Cdd:cd19533    76 VPIRHIDLSGDPDPEGAAQQwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIY-TA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1003 ERRQTIQLPQKTDSFPFWADQLSKYAAETDMEEEIAYWTELSSIKPQPL---PKDTISEGSLLRDSEEVTiqwtkEETEQ 1079
Cdd:cd19533   155 LLKGRPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVslaRRAPGRSLAFLRRTAELP-----PELTR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1080 LLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREpiipDADISRTIGWFTSQYPVVLRMEAGKNLSQRIK 1159
Cdd:cd19533   230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRL----GAAARQTPGMVANTLPLRLTVDPQQTFAELVA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1160 IVKEGLRripdkgmnySIIKyisgHPEADSLQLKPEISfnyLGQFDQDLKHQALRISPFSTGLSMNENQERTAVL----- 1234
Cdd:cd19533   306 QVSRELR---------SLLR----HQRYRYEDLRRDLG---LTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLssgpt 369
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876 1235 -DLN----GMIAEGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAH 1278
Cdd:cd19533   370 nDLSifvyDRDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
4945-5231 1.53e-18

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 91.73  E-value: 1.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4945 PYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVemVRE---EAVQVIKSQVEFSMERYE-ATADEVEECFRAFVRP 5020
Cdd:cd19544    23 PYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAI--LWEglsEPVQVVWRQAELPVEELTlDPGDDALAQLRARFDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5021 ----FDLSQAPLLRAGLIE-LEQDLHIFMFDMHHIITDGASMNIFVE--KLIQLYDGKELAPLrIQYKDFTEWKHQKEQR 5093
Cdd:cd19544   101 rryrLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEeiQAILAGRAAALPPP-VPYRNFVAQARLGASQ 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5094 ERiksQEEYwlgvFHEEL-----PSfeLPkdFARPPVRSfDGKR---HNFTLDKTVTQGIKQLEELTG-STAymILF-SA 5163
Cdd:cd19544   180 AE---HEAF----FREMLgdvdePT--AP--FGLLDVQG-DGSDiteARLALDAELAQRLRAQARRLGvSPA--SLFhLA 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 5164 YSILLAKYSGQDDIVVGTPIAGRPHA--DLEPIIGMFVNTLAIRtAPMAEKTFLDYITETKETM--LKAFEH 5231
Cdd:cd19544   246 WALVLARCSGRDDVVFGTVLSGRMQGgaGADRALGMFINTLPLR-VRLGGRSVREAVRQTHARLaeLLRHEH 316
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
3284-3715 1.71e-18

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 93.16  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPI 3363
Cdd:PRK07059   24 SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3364 DP-DSPSErIRYILNDS---SISVL------------------LYCGKLQDDIGFSGTCIDLMEEHF-----------YH 3410
Cdd:PRK07059  104 NPlYTPRE-LEHQLKDSgaeAIVVLenfattvqqvlaktavkhVVVASMGDLLGFKGHIVNFVVRRVkkmvpawslpgHV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3411 EKDSSLA----LSYQSSQL-----AYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYDA-----ELNIAMLAPYY 3476
Cdd:PRK07059  183 RFNDALAegarQTFKPVKLgpddvAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKkprpdQLNFVCALPLY 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3477 --FDASVQQMYASLLSGHTLFIV-PKEIvsdgAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLI---GGEA 3550
Cdd:PRK07059  263 hiFALTVCGLLGMRTGGRNILIPnPRDI----PGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVangGGMA 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3551 LSKTTVNKLKQLFGEHgaapgITNVYGPTET--CVDASLFNiecsSDAWARSqnyvpIGKPLGRNRMYILDSKKRLQPKG 3628
Cdd:PRK07059  339 VQRPVAERWLEMTGCP-----ITEGYGLSETspVATCNPVD----ATEFSGT-----IGLPLPSTEVSIRDDDGNDLPLG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3629 VQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVML 3708
Cdd:PRK07059  405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478

                  ....*..
gi 166797876 3709 NVPDIQE 3715
Cdd:PRK07059  479 SHPGVLE 485
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
271-749 1.80e-18

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 92.91  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  271 EQAERTPENAAVKFKNDH-----LTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLD 344
Cdd:cd05928    19 EKAGKRPPNPALWWVNGKgdevkWSFRELGSLSRKAANVLSGaCGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  345 PEYPKERLQYLLHDADADVLLVQHHLK---NSLAFDGPVI------------------DLNDEASYHADCsllspVAGHS 403
Cdd:cd05928    99 IQLTAKDILYRLQASKAKCIVTSDELApevDSVASECPSLktkllvseksrdgwlnfkELLNEASTEHHC-----VETGS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 HLAYVIY-TSGTTGKPKgvMVEH-------GGIVNSLQW-----KKAFFKHSPADRVLvlypyvfdAFILNFFGPLISGA 470
Cdd:cd05928   174 QEPMAIYfTSGTTGSPK--MAEHshsslglGLKVNGRYWldltaSDIMWNTSDTGWIK--------SAWSSLFEPWIQGA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  471 TL--HLLPneeNKETFAIQNAIKQERITHFSTSPRLLKTMIEQ-MNREDFIHVQHVVVGGEQLETDTVEKLHSlQPRIRI 547
Cdd:cd05928   244 CVfvHHLP---RFDPLVILKTLSSYPITTFCGAPTVYRMLVQQdLSSYKFPSLQHCVTGGEPLNPEVLEKWKA-QTGLDI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  548 NNEYGPTENSVVSTfhpvQSADEQI---TIGSPVANHQAYILGAHHQIQPIGIPGELYV-----GGAGVARGYLNRPELT 619
Cdd:cd05928   320 YEGYGQTETGLICA----NFKGMKIkpgSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKT 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  620 EEKFVehlhvpgQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLY 699
Cdd:cd05928   396 AATIR-------GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVK 468
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876  700 AYYVgepslTAAQF----REELSRELPN--------YMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:cd05928   469 AFVV-----LAPQFlshdPEQLTKELQQhvksvtapYKYPRKVEFVQELPKTVTGKIQRNEL 525
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2829-3247 2.02e-18

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 91.54  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKgMLFHSLLDEASssYFEQaSFDL--QGELKIDWFKASLERLFETYAVLRTRFY---SGWndtplQIVYKTQTP 2903
Cdd:cd19534     3 PLTPIQR-WFFEQNLAGRH--HFNQ-SVLLrvPQGLDPDALRQALRALVEHHDALRMRFRredGGW-----QQRIRGDVE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2904 QIHFADLRDIEEHLREDAIAAyQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDG--WclSLITKEVFDHY 2981
Cdd:cd19534    74 ELFRLEVVDLSSLAQAAAIEA-LAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW--RILLEDLEAAY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2982 SALQEGrEPEPLSAVPysDYIEWLDRQDQGAAKR-------YWsgylegYKGETTLLHKIAQHEQKEYAYAN-LICRFDH 3053
Cdd:cd19534   151 EQALAG-EPIPLPSKT--SFQTWAELLAEYAQSPalleelaYW------RELPAADYWGLPKDPEQTYGDARtVSFTLDE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3054 EQTKQLQQIANQ-HQVTLNTLIQTLWGVLLQKYSGSADVvfgsVVS----GRPAEIPDVEQM--IGLFINTIPVRIRCDE 3126
Cdd:cd19534   222 EETEALLQEANAaYRTEINDLLLAALALAFQDWTGRAPP----AIFleghGREEIDPGLDLSrtVGWFTSMYPVVLDLEA 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3127 DSTFADTMQMVQQNaLASQ-----SYDTypLYEIQAQTEQKqnLIDHIM--IFENYpIGQ------------QAEETGHH 3187
Cdd:cd19534   298 SEDLGDTLKRVKEQ-LRRIpnkgiGYGI--LRYLTPEGTKR--LAFHPQpeISFNY-LGQfdqgerddalfvSAVGGGGS 371
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3188 GTELNITNFHMqehshYDLNVVVIPGkQLAVHFGFNENEYEKSEVERLRGHFEKLMQQVL 3247
Cdd:cd19534   372 DIGPDTPRFAL-----LDINAVVEGG-QLVITVSYSRNMYHEETIQQLADSYKEALEALI 425
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
858-1277 2.42e-18

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 91.29  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  858 WFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKT-PDGYAPRITGTDESELFHLEVMNykGET 936
Cdd:cd19539    12 WFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDdGGVPRQEILPPGPAPLEVRDLSD--PDS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  937 DPAQAIADKANEIQSSMV-LDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQLPQKT 1014
Cdd:cd19539    90 DRERRLEELLRERESRGFdLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPELR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1015 DSFPFWADQLSKYAAETDMEEEIAYWTE-LSSIKPQPLPKDTISEGSLLRDSEEVTIQWTKEETEQLlKQANRAYNTDIN 1093
Cdd:cd19539   170 QQYKEYAAWQREALAAPRAAELLDFWRRrLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAAL-RELAKRARSSLF 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1094 DLLLTSLGLAVHKWTGTEDIVVNLEGHGREPiiPDADisRTIGWFTSQYPVVLRMEAGKNLSQRIKIV-KEGLRRIPDKG 1172
Cdd:cd19539   249 MVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFE--STVGFFVNLLPLRVDVSDCATFRDLIARVrKALVDAQRHQE 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1173 MNYSIIkyISGHPEADSLQLKP--EISFNYL----GQFDQDLKHQALRISPFSTGlsmnenqertAVLDLN-GMIAEGT- 1244
Cdd:cd19539   325 LPFQQL--VAELPVDRDAGRHPlvQIVFQVTnapaGELELAGGLSYTEGSDIPDG----------AKFDLNlTVTEEGTg 392
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 1245 LSLTLSYSSKQYERSTMAQFARGLKESLQEVIA 1277
Cdd:cd19539   393 LRGSLGYATSLFDEETIQGFLADYLQVLRQLLA 425
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1914-2261 3.21e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 90.23  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1914 SHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKAN----FPLYSSISfdlTVTSIFTPLVTGNAIIV---- 1985
Cdd:cd05944     2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVllcgLPLFHVNG---SVVTLLTPLASGAHVVLagpa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1986 -YDGEDKTALLESIVRDPRVDIIKLTPAHLQVLKEMNI-ADQTAVRRMIVGGENLSTRLARsiheQFEGR--IEICNEYG 2061
Cdd:cd05944    79 gYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVnADISSLRFAMSGAAPLPVELRA----RFEDAtgLPVVEGYG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2062 PTETVVGCMIYRYDAAKdRRESVPIGTAAANTSIYVLD-ENMKPAPIGVP--GEIYISGAGVARGYLNRpELTAEKFVDD 2138
Cdd:cd05944   155 LTEATCLVAVNPPDGPK-RPGSVGLRLPYARVRIKVLDgVGRLLRDCAPDevGEICVAGPGVFGGYLYT-EGNKNAFVAD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2139 PFepgakmYKTGDLAKWLADGNIEYAGRIDEQVkIR-GYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAY--YV 2215
Cdd:cd05944   233 GW------LNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqLK 305
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 166797876 2216 SGGQTTAARL----RKQLSQTLAsymVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05944   306 PGAVVEEEELlawaRDHVPERAA---VPKHIEVLEELPVTAVGKVFKPAL 352
PRK05691 PRK05691
peptide synthase; Validated
4915-5263 3.68e-18

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 93.69  E-value: 3.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4915 IPKAKAKDVYPVSSVQKMVYLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRT-VVEMVREEAVQVI- 4992
Cdd:PRK05691 3249 VPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRAsFSWNAGETMLQVIh 3328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4993 ---KSQVEFSMERyEATADEVEECFRAFVRP-----FDL-SQAPL-LRagLIELEQDLHIFMFDMHHIITD----GASMN 5058
Cdd:PRK05691 3329 kpgRTPIDYLDWR-GLPEDGQEQRLQALHKQereagFDLlNQPPFhLR--LIRVDEARYWFMMSNHHILIDawcrSLLMN 3405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5059 IFVEKLIQLYDGKELA-PLRIQYKDFTEWKhqkeQRERIKSQEEYWlgvfHEELPSFE----LPKDfaRPPVRSFDGKRH 5133
Cdd:PRK05691 3406 DFFEIYTALGEGREAQlPVPPRYRDYIGWL----QRQDLAQARQWW----QDNLRGFErptpIPSD--RPFLREHAGDSG 3475
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5134 NFTLDKTVT----QGIKQLEELTGS---TAYMILFSAYSILLAKYSGQDDIVVGTPIAGRP--HADLEPIIGMFVNTLAI 5204
Cdd:PRK05691 3476 GMVVGDCYTrldaADGARLRELAQAhqlTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvsMPQMQRTVGLFINSIAL 3555
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 5205 RT---APMAEKTFLDYITETKETMLKAFEHQEYPFEELVEKLGVKRDlsrNPLFDTMFVLQN 5263
Cdd:PRK05691 3556 RVqlpAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKG---QPLFDSLFVFEN 3614
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
3293-3789 3.75e-18

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 91.79  E-value: 3.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVF-----EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLP----- 3362
Cdd:cd05970    27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathql 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3363 -------------------IDPDSPSERIRYILNDS-SISVLLYCGKLQDD--IGFSGTCIDlMEEHFYHEKDSSLALSY 3420
Cdd:cd05970   107 takdivyriesadikmivaIAEDNIPEEIEKAAPECpSKPKLVWVGDPVPEgwIDFRKLIKN-ASPDFERPTANSYPCGE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3421 QSSqLAYaiYTSGTTGKPKgtLIEHRQVI---HLIEGLSRQVYSAYDAELNIAMLApyYFDASVQQMYASLLSGHTLFIV 3497
Cdd:cd05970   186 DIL-LVY--FSSGTTGMPK--MVEHDFTYplgHIVTAKYWQNVREGGLHLTVADTG--WGKAVWGKIYGQWIAGAAVFVY 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3498 PKEIVsDGAALCRYYRQHSIDITDGTPAHLKLLIAAG----DLQgvTLQHLLIGGEALSKTTVNKLKQLFGEHgaapgIT 3573
Cdd:cd05970   259 DYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLIREDlsryDLS--SLRYCTTAGEALNPEVFNTFKEKTGIK-----LM 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3574 NVYGPTETCVDASLFniecssdAWARSQnyvP--IGKPLGRNRMYILDSKKRLQPKGVQGELYIAGD-----GVGRGYLN 3646
Cdd:cd05970   331 EGFGQTETTLTIATF-------PWMEPK---PgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3647 LPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADD 3726
Cdd:cd05970   401 DAEKTAEVW-------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 3727 EYYLCGYFAADKTIQISE-LRKRMARHLPG----YMIPAHFVQLDKMPLTPNGKLNRqllpAPVKKRD 3789
Cdd:cd05970   474 GQVVKATIVLAKGYEPSEeLKKELQDHVKKvtapYKYPRIVEFVDELPKTISGKIRR----VEIRERD 537
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
259-744 3.99e-18

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 92.33  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  259 FSGSRTVY--QLFE--EQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQP-DTLVAILADrSLEMIVSIIAV 333
Cdd:cd05943    65 FPGARLNYaeNLLRhaDADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPgDRVAGYLPN-IPEAVVAMLAT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  334 WKAGGAYVPLDPEY-------------PK-----ERLQY--LLHDADADVLLVQHHLKNSLA------------FDGP-- 379
Cdd:cd05943   144 ASIGAIWSSCSPDFgvpgvldrfgqiePKvlfavDAYTYngKRHDVREKVAELVKGLPSLLAvvvvpytvaagqPDLSki 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  380 --VIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVnsLQWKKAFFKH---SPADRvlvLYPYV 454
Cdd:cd05943   224 akALTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTL--LQHLKEHILHcdlRPGDR---LFYYT 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  455 FDAFIL-NFF-GPLISGATLHLL------PNEEnketfAIQNAIKQERITHFSTSPR----LLKTMIEQMNREDFIHVQH 522
Cdd:cd05943   299 TCGWMMwNWLvSGLAVGATIVLYdgspfyPDTN-----ALWDLADEEGITVFGTSAKyldaLEKAGLKPAETHDLSSLRT 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  523 VVVGGEQLETDTVEKLHS-LQPRIRINNEYGPTEnsVVSTF---HPVQSadeqITIGSPvanhQAYILGAHHQI------ 592
Cdd:cd05943   374 ILSTGSPLKPESFDYVYDhIKPDVLLASISGGTD--IISCFvggNPLLP----VYRGEI----QCRGLGMAVEAfdeegk 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  593 QPIGIPGELYVGGAGVAR--GYLNRPELT--EEKFVEHLhvPGqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEI 668
Cdd:cd05943   444 PVWGEKGELVCTKPFPSMpvGFWNDPDGSryRAAYFAKY--PG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGT 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  669 GEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPSLT-----AAQFREELSRELPNYMIPSRFIPLERIPLTSNGK 743
Cdd:cd05943   520 AEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVElddelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599

                  .
gi 166797876  744 I 744
Cdd:cd05943   600 K 600
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
3280-3781 4.10e-18

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 91.74  E-value: 4.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3280 PREKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA 3359
Cdd:PRK06155   18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3360 YLPIDPDSPSERIRYILNDSSISVLL----YCGKLQ--DDIGFSGTCIDLMEEHFYHEKDSSL-------------ALSY 3420
Cdd:PRK06155   98 AVPINTALRGPQLEHILRNSGARLLVveaaLLAALEaaDPGDLPLPAVWLLDAPASVSVPAGWstaplppldapapAAAV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3421 QSSQLAYAIYTSGTTGKPKGTLIEHRQ-------VIHLIEGLSRQVYSAYdaelniamlAPYYFDASVQQMYASLLSGHT 3493
Cdd:PRK06155  178 QPGDTAAILYTSGTTGPSKGVCCPHAQfywwgrnSAEDLEIGADDVLYTT---------LPLFHTNALNAFFQALLAGAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3494 LFIVPK--------EIVSDGAALCrYYRQHSIDITDGTPAHlklliAAGDLQGVTLqhlliggeALSKTTVNKLKQLFGE 3565
Cdd:PRK06155  249 YVLEPRfsasgfwpAVRRHGATVT-YLLGAMVSILLSQPAR-----ESDRAHRVRV--------ALGPGVPAALHAAFRE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3566 HGAAPGITNvYGPTETcvdaslfNIECSSDAWARSQNYvpigkpLGRNR----MYILDSKKRLQPKGVQGELYIAGD--- 3638
Cdd:PRK06155  315 RFGVDLLDG-YGSTET-------NFVIAVTHGSQRPGS------MGRLApgfeARVVDEHDQELPDGEPGELLLRADepf 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3639 GVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAA 3718
Cdd:PRK06155  381 AFATGYFGMPEKTVEAW-------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAV 453
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 3719 aalkdaddeYYLCGYFAADKTIQISELRKRMA-------RH----LPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK06155  454 ---------FPVPSELGEDEVMAAVVLRDGTAlepvalvRHceprLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
289-747 5.23e-18

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 90.88  E-value: 5.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVqh 368
Cdd:cd05940     4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 hlknslafdgpvidlnDEASYhadcsllspvaghshlayvIYTSGTTGKPKGVMVEHGGIVNSLqwkkAFFKHS----PA 444
Cdd:cd05940    82 ----------------DAALY-------------------IYTSGTTGLPKAAIISHRRAWRGG----AFFAGSggalPS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  445 DRVLVLYP-YVFDAFILNFFGPLISGATLHLlpneenKETFAIQN---AIKQERITHFSTSPRLLKTMIEQMNREDFIHV 520
Cdd:cd05940   123 DVLYTCLPlYHSTALIVGWSACLASGATLVI------RKKFSASNfwdDIRKYQATIFQYIGELCRYLLNQPPKPTERKH 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  521 QHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVST----------FHPVQSA----------DEQItiGSPVAN 580
Cdd:cd05940   197 KVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFInffgkpgaigRNPSLLRkvaplalvkyDLES--GEPIRD 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  581 HQAYILGAhhqiqPIGIPGEL--YVGGAGVARGYLNrPELTEEKFVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQ 658
Cdd:cd05940   275 AEGRCIKV-----PRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDT 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  659 VKIRGYRIEIGEVEAAMFNLENVREAAV--VAREDADGAKQLYAYYVGEP-SLTAAQFREELSRELPNYMIPsRFIPLER 735
Cdd:cd05940   349 FRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQPNeEFDLSALAAHLEKNLPGYARP-LFLRLQP 427
                         490
                  ....*....|....*.
gi 166797876  736 -IPLTSN---GKIDLK 747
Cdd:cd05940   428 eMEITGTfkqQKVDLR 443
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
406-745 5.52e-18

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 92.72  E-value: 5.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  406 AYVIYTSGTTGKPKGVMVEHGGIV-NSLQwKKAFFKHSPADRVLVLYPyVFDAFILN--FFGPLISGATLHLLPNEENKE 482
Cdd:PRK06814  796 AVILFTSGSEGTPKGVVLSHRNLLaNRAQ-VAARIDFSPEDKVFNALP-VFHSFGLTggLVLPLLSGVKVFLYPSPLHYR 873
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  483 TfaIQNAIKQERIT-HFSTSPrLLKTMIEQMNREDFIHVQHVVVGGEQLETDT----VEKLhslqpRIRINNEYGPTENS 557
Cdd:PRK06814  874 I--IPELIYDTNATiLFGTDT-FLNGYARYAHPYDFRSLRYVFAGAEKVKEETrqtwMEKF-----GIRILEGYGVTETA 945
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  558 vvstfhPVqsadeqITIGSPVANHQ---AYIL-GAHHQIQPI-GIP--GELYVGGAGVARGYL--NRPELTEEkfvehlh 628
Cdd:PRK06814  946 ------PV------IALNTPMHNKAgtvGRLLpGIEYRLEPVpGIDegGRLFVRGPNVMLGYLraENPGVLEP------- 1006
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  629 vPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLyAYYVGEPSL 708
Cdd:PRK06814 1007 -PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI-ILLTTASDA 1084
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 166797876  709 TAAQFREELS-RELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:PRK06814 1085 TRAAFLAHAKaAGASELMVPAEIITIDEIPLLGTGKID 1122
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
853-1278 6.68e-18

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 89.67  E-value: 6.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  853 TPIQHWFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIF-EKTPDGYAPRITgtdeseLFHLEVmN 931
Cdd:cd19542     5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVV------LKSLDP-P 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  932 YKGETDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQaerrqtiql 1010
Cdd:cd19542    78 IEEVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAYNG--------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1011 pQKTDSFPFWADQLSkYAAETDMEEEIAYWTE-LSSIKPQPLPKDTISEGSLLRDSEEvtiqwtkEETEQLLKQANRAYN 1089
Cdd:cd19542   149 -QLLPPAPPFSDYIS-YLQSQSQEESLQYWRKyLQGASPCAFPSLSPKRPAERSLSST-------RRSLAKLEAFCASLG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1090 TDINDLLLTSLGLAVHKWTGTEDIVVnleGH---GRepIIPDADISRTIGWFTSQYPVVLRMEAGKNLSQRIKIVKE--- 1163
Cdd:cd19542   220 VTLASLFQAAWALVLARYTGSRDVVF---GYvvsGR--DLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQqyl 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1164 --------GLRRIPDKGMNYsiikyiSGHPEADSLqlkpeisFNYLGQFDQDLKHqalriSPFSTGLSMNENQERTAV-L 1234
Cdd:cd19542   295 rslphqhlSLREIQRALGLW------PSGTLFNTL-------VSYQNFEASPESE-----LSGSSVFELSAAEDPTEYpV 356
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 166797876 1235 DLNGMIAEGTLSLTLSYSSKQYERstmaQFARGLKESLQEVIAH 1278
Cdd:cd19542   357 AVEVEPSGDSLKVSLAYSTSVLSE----EQAEELLEQFDDILEA 396
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
4-249 7.35e-18

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 90.47  E-value: 7.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876     4 FKTQETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKY 83
Cdd:pfam00668  191 YQKDAAYWLEQLEGELPVLQLP----KDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRY 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    84 TDRTSLILGIPTVSKQKAG-QSAVN---NIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEH 159
Cdd:pfam00668  267 TGQDDIVVGTPGSGRPSPDiERMVGmfvNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRLPRDLSR 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   160 MPLIHTVVSLNEIHSLQCKEDTATDTLF------------HFDLE------NNGIHLKLFYNGNLYDERYINQIVSHLDQ 221
Cdd:pfam00668  347 HPLFDPMFSFQNYLGQDSQEEEFQLSELdlsvssvieeeaKYDLSltaserGGGLTIKIDYNTSLFDEETIERFAEHFKE 426
                          250       260
                   ....*....|....*....|....*...
gi 166797876   222 LLSVILFQPQAAIHTAEILPEAQKQKLL 249
Cdd:pfam00668  427 LLEQAIAHPSQPLSELDLLSDAEKQKLL 454
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2370-2782 8.84e-18

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 89.75  E-value: 8.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2370 WFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQneEIAQSGLYRLEVMNLKE-DP 2448
Cdd:cd19539    12 WFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQ--EILPPGPAPLEVRDLSDpDS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2449 DPGRTIEAKADEIQSS-MHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLPQKT 2526
Cdd:cd19539    90 DRERRLEELLRERESRgFDLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPELR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2527 DSFQLWAKRLSEYAQSETIKQEQEYW-TKIEQTEVKPLPKDFHETHTTAKDSETAAVEWTKEETELLLKQANRAYHTEIN 2605
Cdd:cd19539   170 QQYKEYAAWQREALAAPRAAELLDFWrRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARSSLFM 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2606 dLLLTSLGLSISHWSGLEQIPIHLEGHGREQIiqdiDISRTVGWFTSLYPVVLHAQPGKEISDYIKTTKEGLrqiphkgi 2685
Cdd:cd19539   250 -VLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP----RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL-------- 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2686 gygIARYLSGGMP-SKLNPEIsfnylgQFDQDLQRHG-VQLSSYSCGSDSSGHQERPYV---------------LNINGM 2748
Cdd:cd19539   317 ---VDAQRHQELPfQQLVAEL------PVDRDAGRHPlVQIVFQVTNAPAGELELAGGLsytegsdipdgakfdLNLTVT 387
                         410       420       430
                  ....*....|....*....|....*....|....
gi 166797876 2749 ITDGRLKLTISYSSKQYAKETIMRLSETIQSRLR 2782
Cdd:cd19539   388 EEGTGLRGSLGYATSLFDEETIQGFLADYLQVLR 421
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
4359-4818 1.09e-17

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 90.38  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4359 TYRQLNERSNQLARVLQDKGACTDQVVAVL---TDRsaHMIIgILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLawnTHR--HLEL-YYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 ----------------------CAGHAIPPLFEGEVLLLD-DPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQL 4492
Cdd:cd12119   104 drdflplleaiaprlptvehvvVMTDDAAMPEPAGVGVLAyEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4493 EHK-----TMTNLLAyeqDHTQLR-FDRVL----QFAAMSFDVCYqemfSALSSGGILFIIGneAKRDIRQLNDFVRTHG 4562
Cdd:cd12119   184 SHRslvlhAMAALLT---DGLGLSeSDVVLpvvpMFHVNAWGLPY----AAAMVGAKLVLPG--PYLDPASLAELIEREG 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4563 IQ-TAFLPTAFLKLLAS-EKHYFEPFAecVDHII----AAGEQLIatRMLRDMLARhqvTLHNhYGPSETH-VVTMYTVD 4635
Cdd:cd12119   255 VTfAAGVPTVWQGLLDHlEANGRDLSS--LRRVViggsAVPRSLI--EAFEERGVR---VIHA-WGMTETSpLGTVARPP 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4636 PDTDQE--------LQPIGKPISNTEIFILNEAGTLQPV--GIVGELCISGVSLARGYHNRESLTLETFVphpyDSnqrM 4705
Cdd:cd12119   327 SEHSNLsedeqlalRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTE----DG---W 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4706 YKTGDLARYLPEGNIEYAGRRDHQVKIRG---YRVELgevEAALLKH--VQEAVVLakentdGQSD--------LYAYFT 4772
Cdd:cd12119   400 LRTGDVATIDEDGYLTITDRSKDVIKSGGewiSSVEL---ENAIMAHpaVAEAAVI------GVPHpkwgerplAVVVLK 470
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876 4773 AEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd12119   471 EGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
858-1278 1.09e-17

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 89.34  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  858 WFFEQKMPHAHHYNQ--AVMLysaegfkEGPL-----RRTMERIASHHDALRMIFEkTPDGyAP--RItgtDESELFHLE 928
Cdd:cd19531    12 WFLDQLEPGSAAYNIpgALRL-------RGPLdvaalERALNELVARHEALRTTFV-EVDG-EPvqVI---LPPLPLPLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  929 VMNYKG--ETDPAQAIADKAN-EIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAER 1004
Cdd:cd19531    80 VVDLSGlpEAEREAEAQRLAReEARRPFDLARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1005 RQTIQLP----QktdsfpfWADqlskYAA-------ETDMEEEIAYWTE-LSSIKPQ-PLPKD-------TiSEGSLlrd 1064
Cdd:cd19531   160 GRPSPLPplpiQ-------YAD----YAVwqrewlqGEVLERQLAYWREqLAGAPPVlELPTDrprpavqS-FRGAR--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1065 seeVTIQWTKEETEQlLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVnleG---HGRepiiPDADISRTIGWF--T 1139
Cdd:cd19531   225 ---VRFTLPAELTAA-LRALARREGATLFMTLLAAFQVLLHRYSGQDDIVV---GtpvAGR----NRAELEGLIGFFvnT 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1140 sqypVVLRMEAGKNLS-----QRIK----------------IVKEglrripdkgmnysiikyisghpeadslqLKPE--- 1195
Cdd:cd19531   294 ----LVLRTDLSGDPTfrellARVRetaleayahqdlpfekLVEA----------------------------LQPErdl 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1196 -------ISFNYLGQFDQDLKHQALRISPFstglsmnENQERTAVLDLNGMIAE--GTLSLTLSYSSKQYERSTMAQFAR 1266
Cdd:cd19531   342 srsplfqVMFVLQNAPAAALELPGLTVEPL-------EVDSGTAKFDLTLSLTEtdGGLRGSLEYNTDLFDAATIERMAG 414
                         490
                  ....*....|..
gi 166797876 1267 GLKESLQEVIAH 1278
Cdd:cd19531   415 HFQTLLEAIVAD 426
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
3289-3786 1.18e-17

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 91.25  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3289 FEEQAHRTPDntaVVfegkqfTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSP 3368
Cdd:PRK06060   20 YDRPAFYAAD---VV------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3369 SERIRYILNDSSISVLLYCGKLQDDIGfSGTCIDLMEehFYHEKDSSLALSYQ---SSQLAYAIYTSGTTGKPKGTLIEH 3445
Cdd:PRK06060   91 RDDHALAARNTEPALVVTSDALRDRFQ-PSRVAEAAE--LMSEAARVAPGGYEpmgGDALAYATYTSGTTGPPKAAIHRH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3446 RQVIHLIEGLSRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYRQHSidITDGTPA 3525
Cdd:PRK06060  168 ADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPS--VLYGVPN 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3526 HLKLLIAAGDLQGV-TLQHLLIGGEALSKTTVNKLKQLFGehgaapGITNVYGPTETCVDASLfnIECSSDAWARSQnyv 3604
Cdd:PRK06060  246 FFARVIDSCSPDSFrSLRCVVSAGEALELGLAERLMEFFG------GIPILDGIGSTEVGQTF--VSNRVDEWRLGT--- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 pIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPE--LTDEKFVadpfvpedrmyRTGDLARLLPDGNIE 3682
Cdd:PRK06060  315 -LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWL-----------DTRDRVCIDSDGWVT 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3683 YIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYF--AADKTIQISELR---KRMARHLPGYM 3757
Cdd:PRK06060  383 YRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLvaTSGATIDGSVMRdlhRGLLNRLSAFK 462
                         490       500       510
                  ....*....|....*....|....*....|.
gi 166797876 3758 IPAHFVQLDKMPLTPNGKLNRQLLPA--PVK 3786
Cdd:PRK06060  463 VPHRFAVVDRLPRTPNGKLVRGALRKqsPTK 493
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2365-2787 1.18e-17

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 88.90  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2365 TPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRttengceaqnEEIAQSGLYRLeVmnL 2444
Cdd:cd19542     5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFV----------ESSAEGTFLQV-V--L 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2445 KEDPDPGRTIEAKADEIQS------SMHLSDG-PLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQaen 2516
Cdd:cd19542    72 KSLDPPIEEVETDEDSLDAltrdllDDPTLFGqPPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAYNG--- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2517 grviQLPQKTDSFqlwaKRLSEYAQSETIKQEQEYWTKIEQ-TEVKPLPkdfheTHTTAKDSE-TAAVEWTKEETellLK 2594
Cdd:cd19542   149 ----QLLPPAPPF----SDYISYLQSQSQEESLQYWRKYLQgASPCAFP-----SLSPKRPAErSLSSTRRSLAK---LE 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2595 QANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDisRTVGWFTSLYPVVLHAQPGKEISDYIKTTK 2674
Cdd:cd19542   213 AFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGID--DIVGPCINTLPVRVKLDPDWTVLDLLRQLQ 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2675 E-----------GLRQIPHKgigygiarylSGGMPSKLNPEISFNYLGQFDQDLQrhgvQLSSYSCGSDSSGHQERPYVL 2743
Cdd:cd19542   291 QqylrslphqhlSLREIQRA----------LGLWPSGTLFNTLVSYQNFEASPES----ELSGSSVFELSAAEDPTEYPV 356
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 166797876 2744 NINGMITDGRLKLTISYSSKQYAKETIMRLSETIQSRLRTIITH 2787
Cdd:cd19542   357 AVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1780-2198 1.21e-17

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 90.70  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1780 FEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYP 1859
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1860 QDRIRYMLDDSQAGIVLMQRD-------VRKQLAYEGVTVLLDDESSYHQDG-SDLAPISD--------------VSHLA 1917
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEElveafeeARADLARPPRLWVAGGDTLDDPEGyEDLAAAAAgapttnpasrsgvtAKDTA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1918 YVIYTSGSTGRPKGVLIEH----------GGLTNyiwwAKE---VYVkgekaNFPLYSSISFdLTVTSifTPLVTGNAI- 1983
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHmrwlkamggfGGLLR----LTPddvLYC-----CLPLYHNTGG-TVAWS--SVLAAGATLa 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1984 ---------------------IVYDGEDKTALLESivrdprvdiikltPAHlqvlkemniADQTA--VRRMIVGGenlst 2040
Cdd:PRK08279  271 lrrkfsasrfwddvrryrataFQYIGELCRYLLNQ-------------PPK---------PTDRDhrLRLMIGNG----- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2041 rLARSIHEQFEGRI---EICNEYGPTETVVG-CMIYRYDAAKDRresVPiGTAAANTSI---------YVLDEN--MKPA 2105
Cdd:PRK08279  324 -LRPDIWDEFQQRFgipRILEFYAASEGNVGfINVFNFDGTVGR---VP-LWLAHPYAIvkydvdtgePVRDADgrCIKV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2106 PIGVPGEIY--ISGAGVARGYlNRPELTAEKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEI 2183
Cdd:PRK08279  399 KPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEV 477
                         490
                  ....*....|....*
gi 166797876 2184 EAALLQEEVIKEAVV 2198
Cdd:PRK08279  478 ENALSGFPGVEEAVV 492
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
3287-3789 1.63e-17

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 90.11  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3287 ELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAK-GVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDP 3365
Cdd:PRK08974   27 DMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3366 -DSPSErIRYILNDSSI-----------------------SVLLycGKLQDDIGFS-GTCIDLMEEHF------YHEKD- 3413
Cdd:PRK08974  107 lYTPRE-LEHQLNDSGAkaivivsnfahtlekvvfktpvkHVIL--TRMGDQLSTAkGTLVNFVVKYIkrlvpkYHLPDa 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3414 ----SSLALSYQ---------SSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEglsrQVYSAYDAELN----IAMLA-PY 3475
Cdd:PRK08974  184 isfrSALHKGRRmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE----QAKAAYGPLLHpgkeLVVTAlPL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3476 Y--FDASVQQMYASLLSGHTLFIV-PKEIvsdgAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLI---GGE 3549
Cdd:PRK08974  260 YhiFALTVNCLLFIELGGQNLLITnPRDI----PGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLsvgGGM 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3550 ALSKTTVNKLKQLFGEHgaapgITNVYGPTEtC---VDASLFNIECSSDAwarsqnyvpIGKPLGRNRMYILDSKKRLQP 3626
Cdd:PRK08974  336 AVQQAVAERWVKLTGQY-----LLEGYGLTE-CsplVSVNPYDLDYYSGS---------IGLPVPSTEIKLVDDDGNEVP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3627 KGVQGELYIAGDGVGRGYLNLPELTDEkfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESV 3706
Cdd:PRK08974  401 PGEPGELWVKGPQVMLGYWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3707 MLNVPDIQEAAAA-ALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK-LNRQLLPAP 3784
Cdd:PRK08974  474 VMLHPKVLEVAAVgVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKiLRRELRDEA 553

                  ....*
gi 166797876 3785 VKKRD 3789
Cdd:PRK08974  554 RAKVD 558
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1918-2255 1.66e-17

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 87.82  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1918 YVIYTSGSTGRPKGVLIEHG----GLTNYIWWAKEVYVKGEKAN-----------FPLYSSISFDLTVTSIFTPLVTGNA 1982
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEdifrMLMGGADFGTGEFTPSEDAHkaaaaaagtvmFPAPPLMHGTGSWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1983 IIVYDGEDKTALLESIVRDpRVDIIKLT------PAhLQVLKEMNIADQTAVRRMIVGGENLStrlaRSIHEQF---EGR 2053
Cdd:cd05924    87 VLPDDRFDPEEVWRTIEKH-KVTSMTIVgdamarPL-IDALRDAGPYDLSSLFAISSGGALLS----PEVKQGLlelVPN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2054 IEICNEYGPTETvvGCMIYRYDAAKDRrESVPIGTAAANTSiyVLDENMKPAPIGVPGEIYISGAG-VARGYLNRPELTA 2132
Cdd:cd05924   161 ITLVDAFGSSET--GFTGSGHSAGSGP-ETGPFTRANPDTV--VLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2133 EKF--VDdpfepGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHgFKQL 2210
Cdd:cd05924   236 ETFpeVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDER-WGQE 309
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 2211 CAYYVS---GGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGK 2255
Cdd:cd05924   310 VVAVVQlreGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
4337-4818 1.67e-17

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 90.48  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4337 LFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACT-DQVVAVLTDrSAHMIIGILAILKAG-AAFLPiDP 4414
Cdd:PRK06060   10 LAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSgDRVLLCLPD-SPDLVQLLLACLARGvMAFLA-NP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4415 ELPEKRRAFMLKDSGADVLLT----CAGHAIPPLFEGEVLLLD----DPLLYQgrtdnlnlSCSENDLMYVIYTSGTTGQ 4486
Cdd:PRK06060   88 ELHRDDHALAARNTEPALVVTsdalRDRFQPSRVAEAAELMSEaarvAPGGYE--------PMGGDALAYATYTSGTTGP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4487 PKGVQLEHktmTNLLAYEQDHTQlrfdRVLQFAAMSFDVCYQEMFSA----------LSSGGILFI----IGNEAKRDIR 4552
Cdd:PRK06060  160 PKAAIHRH---ADPLTFVDAMCR----KALRLTPEDTGLCSARMYFAyglgnsvwfpLATGGSAVInsapVTPEAAAILS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4553 QLNDFVRTHGIqtaflPTAFLKLL-ASEKHYFEPFaECVdhiIAAGEQL---IATRMLRDMLArhqVTLHNHYGPSET-H 4627
Cdd:PRK06060  233 ARFGPSVLYGV-----PNFFARVIdSCSPDSFRSL-RCV---VSAGEALelgLAERLMEFFGG---IPILDGIGSTEVgQ 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4628 VVTMYTVDpdtDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNResltletfvPHPYDSNQRMYK 4707
Cdd:PRK06060  301 TFVSNRVD---EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWLD 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4708 TGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQ---- 4781
Cdd:PRK06060  369 TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDeaVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmr 448
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 166797876 4782 -LKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK06060  449 dLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
273-749 1.69e-17

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 89.36  E-value: 1.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:cd05929     2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVQHHLKNSLafDGPVIDlnDEASYHADCSLLSPVAGHShlaYVIYTSGTTGKPKGVMVEHGG--IVN 430
Cdd:cd05929    82 CAIIEIKAAALVCGLFTGGGAL--DGLEDY--EAAEGGSPETPIEDEAAGW---KMLYSGGTTGRPKGIKRGLPGgpPDN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  431 SLQWKKAF-FKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFaiqNAIKQERITHFSTSP----RLL 505
Cdd:cd05929   155 DTLMAAALgFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFL---RLIERYRVTFAQFVPtmfvRLL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  506 KTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIrINNEYGPTENSVVStfhpVQSADEQIT----IGSPVANh 581
Cdd:cd05929   232 KLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQGLT----IINGEEWLThpgsVGRAVLG- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  582 QAYILGAHHQIQPIGIPGELYVGGAGvARGYLNRPELTEEKFVEHlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKI 661
Cdd:cd05929   306 KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEG------GWSTLGDVGYLDEDGYLYLTDRRSDMIIS 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  662 RGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAyyVGEP-------SLTAAQFREELSRELPNYMIPSRFIPLE 734
Cdd:cd05929   379 GGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPapgadagTALAEELIAFLRDRLSRYKCPRSIEFVA 456
                         490
                  ....*....|....*
gi 166797876  735 RIPLTSNGKIDLKAL 749
Cdd:cd05929   457 ELPRDDTGKLYRRLL 471
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
4356-4818 2.06e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 89.19  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:PRK08276   10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 CAG------HAIPPLFEG-EVLLLDD---------PLLYQGRTDNLNLSCSENDLMyvIYTSGTTGQPKGV--QLEHK-- 4495
Cdd:PRK08276   90 SAAladtaaELAAELPAGvPLLLVVAgpvpgfrsyEEALAAQPDTPIADETAGADM--LYSSGTTGRPKGIkrPLPGLdp 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4496 -----TMTNLLAYEQD--------------HTQlrfdrVLQFAAMsfdvcyqemfsALSSGGILFIIgneAKRDIRQLND 4556
Cdd:PRK08276  168 deapgMMLALLGFGMYggpdsvylspaplyHTA-----PLRFGMS-----------ALALGGTVVVM---EKFDAEEALA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4557 FVRTHGI-QTAFLPTAFLKLLA------------SEKHYFEPFAECVDHIIAAgeqliatrmlrdMLARHQVTLHNHYGP 4623
Cdd:PRK08276  229 LIERYRVtHSQLVPTMFVRMLKlpeevrarydvsSLRVAIHAAAPCPVEVKRA------------MIDWWGPIIHEYYAS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4624 SETHVVTMYTVD-----PDTdqelqpIGKPISnTEIFILNEAGTLQPVGIVGElcisgVSLARG-----YHNRESLTLET 4693
Cdd:PRK08276  297 SEGGGVTVITSEdwlahPGS------VGKAVL-GEVRILDEDGNELPPGEIGT-----VYFEMDgypfeYHNDPEKTAAA 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4694 FVPHpydsnqRMYKTGDLArYLPEGNIEYAGRRDHQVKIRGyrvelG------EVEAALLKH--VQE------------- 4752
Cdd:PRK08276  365 RNPH------GWVTVGDVG-YLDEDGYLYLTDRKSDMIISG-----GvniypqEIENLLVTHpkVADvavfgvpdeemge 432
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 4753 ---AVVLAKENTDGQSDLYAyftaeqslsisQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK08276  433 rvkAVVQPADGADAGDALAA-----------ELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
270-744 2.16e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 89.45  E-value: 2.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  270 EEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPK 349
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  350 ERLQYLLHDADADVLLVQHHLKNSLA------------------FDGPVIDLNDEASYHADCSLLSPVAGHSHlAYVIYT 411
Cdd:PRK07786  104 PEIAFLVSDCGAHVVVTEAALAPVATavrdivpllstvvvaggsSDDSVLGYEDLLAEAGPAHAPVDIPNDSP-ALIMYT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  412 SGTTGKPKGVMVEHGGIV-NSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETfAIQNAI 490
Cdd:PRK07786  183 SGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPG-QLLDVL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  491 KQERITHFSTSPRLLKTMI-EQMNREDFIHVQhVVVGGEQLETDTV-EKLHSLQPRIRINNEYGPTENSVVSTFHPVQSA 568
Cdd:PRK07786  262 EAEKVTGIFLVPAQWQAVCaEQQARPRDLALR-VLSWGAAPASDTLlRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDA 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  569 DEQI-TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFvehlhvpGQKMYKTGDLARWLPDG 647
Cdd:PRK07786  341 IRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-------AGGWFHSGDLVRQDEEG 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  648 RIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV---GEPSLTAAQFREELSRELPNY 724
Cdd:PRK07786  414 YVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnDDAALTLEDLAEFLTDRLARY 493
                         490       500
                  ....*....|....*....|
gi 166797876  725 MIPSRFIPLERIPLTSNGKI 744
Cdd:PRK07786  494 KHPKALEIVDALPRNPAGKV 513
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1769-2205 2.57e-17

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 89.55  E-value: 2.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1769 APFPQTPVHQLfEEQSQRTPDQAAVIDKD-----RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILA 1843
Cdd:PRK08180   35 GDYPRRLTDRL-VHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1844 VLKSGGAYVPIDPEY---PQD--RIRYMLDDSQAGIVLMQRDVRKQLAYEGVtVLLDDE---SSYHQDGSDLAPISDV-- 1913
Cdd:PRK08180  114 AMYAGVPYAPVSPAYslvSQDfgKLRHVLELLTPGLVFADDGAAFARALAAV-VPADVEvvaVRGAVPGRAATPFAALla 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1914 ----------------SHLAYVIYTSGSTGRPKGVLIEHGGLT--------NYIWWAKE--VYVKGEKANFPLYSSISFD 1967
Cdd:PRK08180  193 tpptaavdaahaavgpDTIAKFLFTSGSTGLPKAVINTHRMLCanqqmlaqTFPFLAEEppVLVDWLPWNHTFGGNHNLG 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1968 LTvtsiftpLVTGNAIIVYDGEDKTALLESIVRDPRvDII------------KLTPAHLQ--VLKEMNIADqtaVRRMIV 2033
Cdd:PRK08180  273 IV-------LYNGGTLYIDDGKPTPGGFDETLRNLR-EISptvyfnvpkgweMLVPALERdaALRRRFFSR---LKLLFY 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2034 GGENLS----TRLARSIHEQFEGRIEICNEYGPTETvvgcmiyrydaakdrresvpigtaaANTSIYVLDENMKPAPIGV 2109
Cdd:PRK08180  342 AGAALSqdvwDRLDRVAEATCGERIRMMTGLGMTET-------------------------APSATFTTGPLSRAGNIGL 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2110 P--G------------EIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWlADGN-----IEYAGRIDEQ 2170
Cdd:PRK08180  397 PapGcevklvpvggklEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF-VDPAdpergLMFDGRIAED 469
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 166797876 2171 VKI-RGYRIELGEIEAALLQE--EVIKEAVVTA--REDVH 2205
Cdd:PRK08180  470 FKLsSGTWVSVGPLRARAVSAgaPLVQDVVITGhdRDEIG 509
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3914-4297 2.71e-17

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 88.08  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3914 LMTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYvldHAAFEAEWYQGE-EDDADLYIRQFIRP--------F 3984
Cdd:cd19534    27 LLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQR---IRGDVEELFRLEvVDLSSLAQAAAIEAlaaeaqssL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3985 HLDEPPLLRVGLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIYE----GETLP-PLRIQYKDYAVWQTGEARLQQI 4059
Cdd:cd19534   104 DLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEqalaGEPIPlPSKTSFQTWAELLAEYAQSPAL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4060 QKQEAYWLELYSGDVPvlHLPADYIRPSARdfaGATMHFTLDKQKSdglKQL------ASQTEstLYMVLLASYTLLLSK 4133
Cdd:cd19534   184 LEELAYWRELPAADYW--GLPKDPEQTYGD---ARTVSFTLDEEET---EALlqeanaAYRTE--INDLLLAALALAFQD 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4134 YSGQEDIIVGSPIAGR----PHADLEPIIGMFvnTlAMrnYP-----EKGKTFSQYLSEVKENaLKAYEHQDYPFEVLid 4204
Cdd:cd19534   254 WTGRAPPAIFLEGHGReeidPGLDLSRTVGWF--T-SM--YPvvldlEASEDLGDTLKRVKEQ-LRRIPNKGIGYGIL-- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4205 qlniaRDLSRnplfDTMFVLQNTEQ-----------EQLEINDVTFKPY---------PNGHTMAKFDLTlTAVEEGAgI 4264
Cdd:cd19534   326 -----RYLTP----EGTKRLAFHPQpeisfnylgqfDQGERDDALFVSAvggggsdigPDTPRFALLDIN-AVVEGGQ-L 394
                         410       420       430
                  ....*....|....*....|....*....|...
gi 166797876 4265 QFTLEYLTALFKPETIERMMGHFEQLVDSIIKQ 4297
Cdd:cd19534   395 VITVSYSRNMYHEETIQQLADSYKEALEALIEH 427
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2363-2817 2.91e-17

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 90.30  E-value: 2.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2363 SLTPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQNEEIAQSGLYRLEVM 2442
Cdd:COG1020    21 SAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2443 NLKEDPDPGRTIEAKADEIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQ 2521
Cdd:COG1020   101 VDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLlLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2522 LPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTKIEQTE--VKPLPKDFHETHTTAKDSETAAVEWTKEETELLLKQAnRA 2599
Cdd:COG1020   181 LPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLppLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALA-RR 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2600 YHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGReqiiQDIDISRTVGWFTSLYPVVLHAQPGKEISDYIKTTKEGLRQ 2679
Cdd:COG1020   260 HGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGR----PRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2680 I-PHKGIGY-------GIARYLSGgmpsklNP--EISFNYLGQFDQDLQRHGVQLSSYSCgsdssGHQERPYVLNINGMI 2749
Cdd:COG1020   336 AyAHQDLPFerlveelQPERDLSR------NPlfQVMFVLQNAPADELELPGLTLEPLEL-----DSGTAKFDLTLTVVE 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 2750 TDGRLKLTISYSSKQYAKETImrlsETIQSRLRTIITHCVHKEQSELTPSDILlkgiSIDELDQLLIQ 2817
Cdd:COG1020   405 TGDGLRLTLEYNTDLFDAATI----ERMAGHLVTLLEALAADPDQPLGDLPLL----TAAERQQLLAE 464
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1779-2279 3.38e-17

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 88.96  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1779 LFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAK-GVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPE 1857
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1858 YPQDRIRYMLDDSQA-GIVLM------------QRDVR--------KQLAYEGVTVL---------------LDDESSYH 1901
Cdd:PRK08974  108 YTPRELEHQLNDSGAkAIVIVsnfahtlekvvfKTPVKhviltrmgDQLSTAKGTLVnfvvkyikrlvpkyhLPDAISFR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1902 ---QDGSDLA---PISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVY-----VKGEKA--NFPLYSSisFDL 1968
Cdd:PRK08974  188 salHKGRRMQyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYgpllhPGKELVvtALPLYHI--FAL 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1969 TVTSIFTPLVTGNAIIVYDGEDKTALLESIVRDPRVDII---KLTPAHLQVlKEMNIADQTAVRRMIVGGenlsTRLARS 2045
Cdd:PRK08974  266 TVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITgvnTLFNALLNN-EEFQELDFSSLKLSVGGG----MAVQQA 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2046 IHEQFEG--RIEICNEYGPTET---VVGCmiyRYDAAKdrrESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGV 2120
Cdd:PRK08974  341 VAERWVKltGQYLLEGYGLTECsplVSVN---PYDLDY---YSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQV 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2121 ARGYLNRPELTAEkfvddpfepgakMYKTGdlakWLADGNIeyaGRIDEQVKIR------------GYRIELGEIEAAL- 2187
Cdd:PRK08974  415 MLGYWQRPEATDE------------VIKDG----WLATGDI---AVMDEEGFLRivdrkkdmilvsGFNVYPNEIEDVVm 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2188 LQEEVIKEAVVTAREDVHGfkQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYfIEL-DEMPLTSNGKINKKglpap 2264
Cdd:PRK08974  476 LHPKVLEVAAVGVPSEVSG--EAVKIFVvkKDPSLTEEELITHCRRHLTGYKVPKL-VEFrDELPKSNVGKILRR----- 547
                         570
                  ....*....|....*
gi 166797876 2265 dfELQDRAEYKAPRT 2279
Cdd:PRK08974  548 --ELRDEARAKVDNK 560
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4470-4816 3.90e-17

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 87.05  E-value: 3.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4470 SENDLmYVIYTSGTTGQPKGVQLEH-------KTMTNLLAYEQDHTQLRFDRVLQFAAMSFDVCYQEM--------FSAL 4534
Cdd:cd05924     2 SADDL-YILYTGGTTGMPKGVMWRQedifrmlMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMhgtgswtaFGGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4535 SSGGILFIIGNeaKRDIRQLNDFVRTHGIQTAFL-PTAFLKLLASEKHYFEPF-AECVDHIIAAGEQLiaTRMLRDMLAR 4612
Cdd:cd05924    81 LGGQTVVLPDD--RFDPEEVWRTIEKHKVTSMTIvGDAMARPLIDALRDAGPYdLSSLFAISSGGALL--SPEVKQGLLE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4613 H--QVTLHNHYGPSETHVvTMYTVDPDTDQELQPIGKPISNTeiFILNEAGTLQPVG--IVGELCISGVsLARGYHNRES 4688
Cdd:cd05924   157 LvpNITLVDAFGSSETGF-TGSGHSAGSGPETGPFTRANPDT--VVLDDDGRVVPPGsgGVGWIARRGH-IPLGYYGDEA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4689 LTLETFvphPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSD 4766
Cdd:cd05924   233 KTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHpaVYDVLVVGRPDERWGQE 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166797876 4767 LYAYFTAEQ--SLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRR 4816
Cdd:cd05924   310 VVAVVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2820-3139 4.15e-17

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 87.92  E-value: 4.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2820 HAGEVenvyPLTPMQKGMLFHSLLDEASSSYFEQASFDLQGELKIDWFKASLERLFETYAVLRTRFYSGWNDtplqiVYK 2899
Cdd:cd19546     1 RPDEV----PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGD-----VHQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2900 tqtpQIHFADLRDIEEHL---REDAIAAYQREDKAKGFDLARDPLMRIAIFRMEDRKYHLIWSFHHIVMDGWCLSLITKE 2976
Cdd:cd19546    72 ----RILDADAARPELPVvpaTEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2977 VFDHYSALQEGREPE--PLsAVPYSDYIEWLDRQDQGAAKR---------YWSGYLEGYKGETTLLHKIAQHEQKEYAYA 3045
Cdd:cd19546   148 LAAAYGARREGRAPEraPL-PLQFADYALWERELLAGEDDRdsligdqiaYWRDALAGAPDELELPTDRPRPVLPSRRAG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3046 NLICRFDHEQTKQLQQIANQHQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSgRPAEIPDVEQMIGLFINTIPVRIRCD 3125
Cdd:cd19546   227 AVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDLS 305
                         330
                  ....*....|....
gi 166797876 3126 EDSTFADTMQMVQQ 3139
Cdd:cd19546   306 GDPTFRELLGRVRE 319
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
4336-4818 4.34e-17

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 88.73  E-value: 4.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4336 QLFEQQAERNPDHEAvmFGNQ--TLTYRQLNERSNQLARVLQDKgacTDQV----VAVLTDRSAHMIIGILAILKAGAAF 4409
Cdd:PRK12492   28 EVFERSCKKFADRPA--FSNLgvTLSYAELERHSAAFAAYLQQH---TDLVpgdrIAVQMPNVLQYPIAVFGALRAGLIV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4410 LPIDPELPEKRRAFMLKDSGADVLL-----------TCAGHAIPPLFE---GEVL----------LLDD----------- 4454
Cdd:PRK12492  103 VNTNPLYTAREMRHQFKDSGARALVylnmfgklvqeVLPDTGIEYLIEakmGDLLpaakgwlvntVVDKvkkmvpayhlp 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4455 ------PLLYQGRTDNLN-LSCSENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLAYEQD------------HTQLRFDRV 4515
Cdd:PRK12492  183 qavpfkQALRQGRGLSLKpVPVGLDDIAVLQYTGGTTGLAKGAMLTHG---NLVANMLQvraclsqlgpdgQPLMKEGQE 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4516 LQFAAMSFDVCYQemFSA-----LSSGGILFIIGNeaKRDIrqlNDFVRTHGIQ--TAF--LPTAFLKLLAsekhyfEPF 4586
Cdd:PRK12492  260 VMIAPLPLYHIYA--FTAncmcmMVSGNHNVLITN--PRDI---PGFIKELGKWrfSALlgLNTLFVALMD------HPG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4587 AECVDHIIAAGEQLIATRMLRDMLARHQ----VTLHNHYGPSETHVVTmyTVDPDTDQ-ELQPIGKPISNTEIFILNEAG 4661
Cdd:PRK12492  327 FKDLDFSALKLTNSGGTALVKATAERWEqltgCTIVEGYGLTETSPVA--STNPYGELaRLGTVGIPVPGTALKVIDDDG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4662 TLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpydSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGE 4741
Cdd:PRK12492  405 NELPLGERGELCIKGPQVMKGYWQQPEATAEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4742 VEAALLKHVQE---AVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK12492  479 IEDVVMAHPKVancAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
408-744 4.82e-17

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 86.16  E-value: 4.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 VIYTSGTTGKPKGVMVEHGGIVNSLQ-WKKAFFKHSPADRVLVLYPYVFD------AFILNFFGPLISG----------- 469
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTFFAVPDiLQKEGLNWVVGDVTYLPLPATHIgglwwiLTCLIHGGLCVTGgenttykslfk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  470 -------ATLHLLPNEENKETFAIQNAIKqerithfsTSPRLlktmieqmnredfihvQHVVVGGEQLETDTVEKLhSLQ 542
Cdd:cd17635    86 ilttnavTTTCLVPTLLSKLVSELKSANA--------TVPSL----------------RLIGYGGSRAIAADVRFI-EAT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  543 PRIRINNEYGPTENSVVsTFHPVQSADEQI-TIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEE 621
Cdd:cd17635   141 GLTNTAQVYGLSETGTA-LCLPTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  622 KFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAY 701
Cdd:cd17635   220 VLID-------GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLA 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876  702 YVGEPSL---TAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:cd17635   293 VVASAELdenAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1909-2261 5.89e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 86.25  E-value: 5.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1909 PISDvsHLAYVIYTSGSTGRPKGVLIEHGGLTNYIWwAKEVYVKGEKA---NFPLYSSISFDLTVTSIF---TPLVtgna 1982
Cdd:PRK07824   32 PIDD--DVALVVATSGTTGTPKGAMLTAAALTASAD-ATHDRLGGPGQwllALPAHHIAGLQVLVRSVIagsEPVE---- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1983 IIVYDGEDKTALLESI--VRDPRVdIIKLTPAhlQVLKEMNIADQTAVRR----MIVGGENLSTRLARSIHEqfeGRIEI 2056
Cdd:PRK07824  105 LDVSAGFDPTALPRAVaeLGGGRR-YTSLVPM--QLAKALDDPAATAALAeldaVLVGGGPAPAPVLDAAAA---AGINV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2057 CNEYGPTETVVGCMiyrYDAakdrresVPIgtaaANTSIYVLDenmkpapigvpGEIYISGAGVARGYLNRPEltaekfv 2136
Cdd:PRK07824  179 VRTYGMSETSGGCV---YDG-------VPL----DGVRVRVED-----------GRIALGGPTLAKGYRNPVD------- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2137 DDPF-EPGakMYKTGDLAKwLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVH-GFKQLCAYY 2214
Cdd:PRK07824  227 PDPFaEPG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVAAVV 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 2215 VSGGQT-TAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK07824  304 GDGGPApTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3278-3781 5.95e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 88.17  E-value: 5.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3278 HYPR-EKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKA 3356
Cdd:PRK06178   27 EYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3357 GGAYLPIDPDSPSERIRYILNDSSISVLLYCGKLQDDI---------------GFSGTC--------------------- 3400
Cdd:PRK06178  107 GAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVeqvraetslrhvivtSLADVLpaeptlplpdslraprlaaag 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3401 -IDLMEehfyHEKDSSLALSYQSSQL---AYAIYTSGTTGKPKGTLIEHRQVI------HLIEGLSRQ--VYSAYDAELN 3468
Cdd:PRK06178  187 aIDLLP----ALRACTAPVPLPPPALdalAALNYTGGTTGMPKGCEHTQRDMVytaaaaYAVAVVGGEdsVFLSFLPEFW 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3469 IA-----MLAPyyfdasvqqmyasLLSGHTLFIVPK-EIVSDGAALCRYYRQHSIDITDG------TPAhlkllIAAGDL 3536
Cdd:PRK06178  263 IAgenfgLLFP-------------LFSGATLVLLARwDAVAFMAAVERYRVTRTVMLVDNavelmdHPR-----FAEYDL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3537 QgvTLQHlliggeALSKTTVNKL--------KQLFG----EhgAAPGITNvygpTETCvdaSLFNIECSSDAWARSQNYV 3604
Cdd:PRK06178  325 S--SLRQ------VRVVSFVKKLnpdyrqrwRALTGsvlaE--AAWGMTE----THTC---DTFTAGFQDDDFDLLSQPV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 PIGKPLGRNRMYILDSKK-RLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpfvpeDRMYRTGDLARLLPDGNIEY 3683
Cdd:PRK06178  388 FVGLPVPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHY 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3684 IGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdaddeyylCGY-----------------FAADKTIQISELR 3746
Cdd:PRK06178  461 LGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG---------------SAVvgrpdpdkgqvpvafvqLKPGADLTAAALQ 525
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 166797876 3747 KRMARHLPGYMIPAHFVqLDKMPLTPNGKLNRQLL 3781
Cdd:PRK06178  526 AWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
PRK08162 PRK08162
acyl-CoA synthetase; Validated
274-744 6.25e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 88.08  E-value: 6.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  274 ERT----PENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPK 349
Cdd:PRK08162   25 ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  350 ERLQYLLHDADADVLLVQHH----LKNSLA-FDGP---VIDLNDEASYHADC-------SLLSpvAGHSHLAYVI----- 409
Cdd:PRK08162  105 ASIAFMLRHGEAKVLIVDTEfaevAREALAlLPGPkplVIDVDDPEYPGGRFigaldyeAFLA--SGDPDFAWTLpadew 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  410 ------YTSGTTGKPKGVMVEHGG-----IVNSLQWkkAFFKHSpadrvlvLYPYVFDAFILNFFG-P---LISGATLHL 474
Cdd:PRK08162  183 daialnYTSGTTGNPKGVVYHHRGaylnaLSNILAW--GMPKHP-------VYLWTLPMFHCNGWCfPwtvAARAGTNVC 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  475 LPNEENKetfAIQNAIKQERITHFSTSPRLLKTMI--EQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQprIRINNEYG 552
Cdd:PRK08162  254 LRKVDPK---LIFDLIREHGVTHYCGAPIVLSALInaPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIG--FDLTHVYG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  553 PTEN---SVVSTFHPVQSA---DEQITIGS--PVANH-QAYILGAHHQ-IQPIgiP------GELYVGGAGVARGYLNRP 616
Cdd:PRK08162  329 LTETygpATVCAWQPEWDAlplDERAQLKArqGVRYPlQEGVTVLDPDtMQPV--PadgetiGEIMFRGNIVMKGYLKNP 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  617 ELTEEKFvehlhvpGQKMYKTGDLARWLPDGRIeylgridhQVKIRGYRIEIG--------EVEAAMFNLENVREAAVVA 688
Cdd:PRK08162  407 KATEEAF-------AGGWFHTGDLAVLHPDGYI--------KIKDRSKDIIISggenissiEVEDVLYRHPAVLVAAVVA 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876  689 REDA-------------DGAkqlyayyvgepSLTAAQFREELSRELPNYMIPSRFIpLERIPLTSNGKI 744
Cdd:PRK08162  472 KPDPkwgevpcafvelkDGA-----------SATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKI 528
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1800-2203 6.39e-17

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 87.66  E-value: 6.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGgayVPIDPEYP---QDRIRYMLDDSQAgivl 1876
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETEC---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 mqrdvrkqlayegVTVLLDDESSyhqdgsDLAPIsdvshlayvIYTSGSTGRPKGVLIEHG-----------GLTNYIWw 1945
Cdd:cd17639    79 -------------SAIFTDGKPD------DLACI---------MYTSGSTGNPKGVMLTHGnlvagiaglgdRVPELLG- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1946 AKEVYVkgekANFPLySSIsFDLTVTSIFtplVTGNAIIVYdGEDKTaLLESIVRDPRVDIIKLTPAHL----------- 2014
Cdd:cd17639   130 PDDRYL----AYLPL-AHI-FELAAENVC---LYRGGTIGY-GSPRT-LTDKSKRGCKGDLTEFKPTLMvgvpaiwdtir 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2015 -QVLKEMN-------------------------------------IADQTA--VRRMIVGGENLStrlaRSIHEQFEgrI 2054
Cdd:cd17639   199 kGVLAKLNpmgglkrtlfwtayqsklkalkegpgtplldelvfkkVRAALGgrLRYMLSGGAPLS----ADTQEFLN--I 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2055 EIC---NEYGPTETVVGCMIYRYDAAKDRRESVPIGTaaanTSIYVLD------ENMKPAPigvPGEIYISGAGVARGYL 2125
Cdd:cd17639   273 VLCpviQGYGLTETCAGGTVQDPGDLETGRVGPPLPC----CEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYY 345
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 2126 NRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIR-GYRIELGEIEAALLQEEVIKEAVVTARED 2203
Cdd:cd17639   346 KNPEKTKEAFDGDGW------FHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPD 418
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
4356-4755 7.25e-17

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 87.41  E-value: 7.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 caghaipplfegevlllddpllyqgrtDNlnlscSENDLMYVIYTSGTTGQPKGVQLEHKT----MTNLLAYEQDHTQLR 4511
Cdd:cd17640    84 ---------------------------EN-----DSDDLATIIYTSGTTGNPKGVMLTHANllhqIRSLSDIVPPQPGDR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4512 FDRVLQFAAMSFDVCyqEMFSALSSGGILFIIGNEAKRDIRQLN-----------DFVRThGIQTAFLP-TAFLKLLAse 4579
Cdd:cd17640   132 FLSILPIWHSYERSA--EYFIFACGCSQAYTSIRTLKDDLKRVKphyivsvprlwESLYS-GIQKQVSKsSPIKQFLF-- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4580 kHYFEPFAECVDHIIAAGEqliatrmlrdmLARHQVT--------LHNHYGPSETH-VVTMYTVDPDTdqeLQPIGKPIS 4650
Cdd:cd17640   207 -LFFLSGGIFKFGISGGGA-----------LPPHVDTffeaigieVLNGYGLTETSpVVSARRLKCNV---RGSVGRPLP 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4651 NTEIFILN-EAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpydSNQRMYKTGDLARYLPEGNIEYAGR-RDH 4728
Cdd:cd17640   272 GTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL------DSDGWFNTGDLGWLTCGGELVLTGRaKDT 345
                         410       420
                  ....*....|....*....|....*....
gi 166797876 4729 QVKIRGYRVELGEVEAALLKH--VQEAVV 4755
Cdd:cd17640   346 IVLSNGENVEPQPIEEALMRSpfIEQIMV 374
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
268-749 8.49e-17

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 87.74  E-value: 8.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  268 LFEEQAErtPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQP-DTLVAILADRSlEMIVSIIAVWKAGgaYVPLDPE 346
Cdd:PRK10946   30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPgDTALVQLGNVA-EFYITFFALLKLG--VAPVNAL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  347 YPKERLQ---Y----------------LLHDAD-ADVLLVQHHLKNSLAF--DGPVIDLNDEASYHADCSLLSPVAGhSH 404
Cdd:PRK10946  105 FSHQRSElnaYasqiepalliadrqhaLFSDDDfLNTLVAEHSSLRVVLLlnDDGEHSLDDAINHPAEDFTATPSPA-DE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  405 LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFdafilNF-------FGPLISGATLHLLPN 477
Cdd:PRK10946  184 VAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAH-----NYpmsspgaLGVFLAGGTVVLAPD 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  478 EENKETFAIqnaIKQERITHFSTSPRLLKTMIEQMNREDFIH----VQHVVVGGEQLEtdtveklHSLQPRI------RI 547
Cdd:PRK10946  259 PSATLCFPL---IEKHQVNVTALVPPAVSLWLQAIAEGGSRAqlasLKLLQVGGARLS-------ETLARRIpaelgcQL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  548 NNEYGPTENSVVSTfhPVQSADEQI--TIGSPVA-NHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFV 624
Cdd:PRK10946  329 QQVFGMAEGLVNYT--RLDDSDERIftTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFD 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  625 EhlhvpgQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVG 704
Cdd:PRK10946  407 A------NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876  705 EPSLTAAQFREELsREL--PNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK10946  481 KEPLKAVQLRRFL-REQgiAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
3276-3778 1.03e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 87.36  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3276 DMHYPrEKTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLK 3355
Cdd:PRK05605   26 DLDYG-DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3356 AGGAYLPIDPDSPSERIRYILNDSSISVLLY-------CGKLQDDIG----FSGTCIDLMEEH----------------- 3407
Cdd:PRK05605  105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVwdkvaptVERLRRTTPletiVSVNMIAAMPLLqrlalrlpipalrkara 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3408 -----------FYHEKDSSLALSYQSSQ--------LAYAIYTSGTTGKPKGTLIEHRQVI-------HLIEGLSRQ--- 3458
Cdd:PRK05605  185 altgpapgtvpWETLVDAAIGGDGSDVShprptpddVALILYTSGTTGKPKGAQLTHRNLFanaaqgkAWVPGLGDGper 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3459 VYS------AYDAELNIAmLAPYYfdasvqqmyasllsGHTLFIVPKeivSDGAALCRYYRQHSIDITDGTPAHLKLLIA 3532
Cdd:PRK05605  265 VLAalpmfhAYGLTLCLT-LAVSI--------------GGELVLLPA---PDIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3533 AGDLQGVTLQHL---LIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTETCVDASlfnieCSSDAWARSQNYVPIGKP 3609
Cdd:PRK05605  327 AAEERGVDLSGVrnaFSGAMALPVSTVELWEKLTGGL-----LVEGYGLTETSPIIV-----GNPMSDDRRPGYVGVPFP 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3610 LGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDH 3689
Cdd:PRK05605  397 DTEVRIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-------LDGWFRTGDVVVMEEDGFIRIVDRIKE 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3690 QVKIQGFRIELGEIESVMLNVPDIQEAAA--AALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPAHFVQLDK 3767
Cdd:PRK05605  470 LIITGGFNVYPAEVEEVLREHPGVEDAAVvgLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDE 549
                         570
                  ....*....|.
gi 166797876 3768 MPLTPNGKLNR 3778
Cdd:PRK05605  550 LPRDQLGKVRR 560
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1776-2276 1.15e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 87.51  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAK-GVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI 1854
Cdd:PRK05677   26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPEYPQDRIRYMLDDSQAGIVL----MQRDVRKQLAYEGVTVLLDDE------------------------SSYH----- 1901
Cdd:PRK05677  106 NPLYTAREMEHQFNDSGAKALVclanMAHLAEKVLPKTGVKHVIVTEvadmlpplkrllinavvkhvkkmvPAYHlpqav 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1902 -----------QDGSDLAPISDvsHLAYVIYTSGSTGRPKGVLIEHGGL-----------TNYIWWAKEVYVkgekANFP 1959
Cdd:PRK05677  186 kfndalakgagQPVTEANPQAD--DVAVLQYTGGTTGVAKGAMLTHRNLvanmlqcralmGSNLNEGCEILI----APLP 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1960 LYSSISFdlTVTSIFTPLVTGNAIIVYDGEDktalLESIVRDPR-------VDIIKLTPAhLQVLKEMNIADQTAVRRMI 2032
Cdd:PRK05677  260 LYHIYAF--TFHCMAMMLIGNHNILISNPRD----LPAMVKELGkwkfsgfVGLNTLFVA-LCNNEAFRKLDFSALKLTL 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2033 VGGENLSTRLARSiHEQFEGrIEICNEYGPTETV-VGCMiyrydaakDRRESVPIGTAA---ANTSIYVLDENMKPAPIG 2108
Cdd:PRK05677  333 SGGMALQLATAER-WKEVTG-CAICEGYGMTETSpVVSV--------NPSQAIQVGTIGipvPSTLCKVIDDDGNELPLG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2109 VPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRI---ELGEIEA 2185
Cdd:PRK05677  403 EVGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVypnELEDVLA 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2186 ALlqEEVIKEAVVTAREDVHGfKQLCAYYVS--GGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKglpa 2263
Cdd:PRK05677  477 AL--PGVLQCAAIGVPDEKSG-EAIKVFVVVkpGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRR---- 549
                         570
                  ....*....|...
gi 166797876 2264 pdfELQDRAEYKA 2276
Cdd:PRK05677  550 ---ELRDEELKKA 559
PRK12316 PRK12316
peptide synthase; Provisional
858-1335 1.27e-16

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 88.86  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  858 WFFEQKMPHAHHYN--QAVMLYSAegFKEGPLRRTMERIASHHDALRMIFEKTPDgyaPRITGTDESELFHLEVMNYKGE 935
Cdd:PRK12316   60 WFLWQLEPQSGAYNlpSAVRLNGP--LDRQALERAFASLVQRHETLRTVFPRGAD---DSLAQVPLDRPLEVEFEDCSGL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  936 TDPAQ--AIADKANEiQSSMVLD--KGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQL 1010
Cdd:PRK12316  135 PEAEQeaRLRDEAQR-ESLQPFDlcEGPLLRVRLLRLGEEEHvLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGL 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1011 P----QKTDsFPFWadQLSKYAAeTDMEEEIAYWT----------ELSSIKPQPlpkdtiSEGSLLRDSEEVTIQwtkEE 1076
Cdd:PRK12316  214 PalpiQYAD-YALW--QRSWLEA-GEQERQLEYWRaqlgeehpvlELPTDHPRP------AVPSYRGSRYEFSID---PA 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1077 TEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREpiipDADISRTIGWFTSQYpvVLRMEagknLSQ 1156
Cdd:PRK12316  281 LAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRN----RAEVEGLIGFFVNTQ--VLRSV----FDG 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1157 RIKiVKEGLRRIPDKGMNYSIIKYISGHPEADSLQLKPEISFNYLGQFDQDLKHQALRISPFST--GLSMN--ENQERTA 1232
Cdd:PRK12316  351 RTR-VATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADIEALDTvaGLEFGqlEWKSRTT 429
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1233 VLDLNGMIAE--GTLSLTLSYSSKQYERSTMAQFARGLKESLQeviAHCVSRQQtsltpsdillkdiSIDELEQL--LEQ 1308
Cdd:PRK12316  430 QFDLTLDTYEkgGRLHAALTYATDLFEARTVERMARHWQNLLR---GMVENPQA-------------RVDELPMLdaEER 493
                         490       500
                  ....*....|....*....|....*..
gi 166797876 1309 TRELGEAENIYPLTPMQKGMlfHSLFD 1335
Cdd:PRK12316  494 GQLVEGWNATAAEYPLQRGV--HRLFE 518
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
288-744 1.42e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 86.50  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  288 HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLV- 366
Cdd:PRK08276   11 VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVs 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  367 --------------QHHLKNSLAFDGPV---IDLNDEASYHADCSLLSPVAGhSHLAyviYTSGTTGKPKGVMVE--HGG 427
Cdd:PRK08276   91 aaladtaaelaaelPAGVPLLLVVAGPVpgfRSYEEALAAQPDTPIADETAG-ADML---YSSGTTGRPKGIKRPlpGLD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  428 I---VNSLQWKKAFFKHSPAD-RVLV---LY---PYVFDAFILNFfgplisGATLHLLPNEENKETFAiqnAIKQERITH 497
Cdd:PRK08276  167 PdeaPGMMLALLGFGMYGGPDsVYLSpapLYhtaPLRFGMSALAL------GGTVVVMEKFDAEEALA---LIERYRVTH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  498 FSTSP----RLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEK-LHSLQPRIrinNE-YGPTENSVVSTFHPVQSADEQ 571
Cdd:PRK08276  238 SQLVPtmfvRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAmIDWWGPII---HEyYASSEGGGVTVITSEDWLAHP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  572 ITIGSPVANhQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVpgqkmyKTGDLArWL-PDGrie 650
Cdd:PRK08276  315 GSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWV------TVGDVG-YLdEDG--- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  651 YL---GRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAyyVGEPSLTAA---QFREEL---SRE- 720
Cdd:PRK08276  384 YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADGADagdALAAELiawLRGr 461
                         490       500
                  ....*....|....*....|....
gi 166797876  721 LPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK08276  462 LAHYKCPRSIDFEDELPRTPTGKL 485
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
4339-4818 1.55e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 86.67  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4339 EQQAERNPDHEAVMFGN--QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPEL 4416
Cdd:PRK13391    4 GIHAQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4417 PEKRRAFMLKDSGADVLLTCAGHA---------IPPLFEGEVLLLDDPLLYQGRTDNLNLSC--------SENDLMyvIY 4479
Cdd:PRK13391   84 TPAEAAYIVDDSGARALITSAAKLdvarallkqCPGVRHRLVLDGDGELEGFVGYAEAVAGLpatpiadeSLGTDM--LY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4480 TSGTTGQPKGV-----QLEHKTMTNLLAYEQDHTQLRFDRV------LQFAAMSFDVcyqemFSALSSGGILFIIGN-EA 4547
Cdd:PRK13391  162 SSGTTGRPKGIkrplpEQPPDTPLPLTAFLQRLWGFRSDMVylspapLYHSAPQRAV-----MLVIRLGGTVIVMEHfDA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4548 KRDIRQLNDFVRTHgiqTAFLPTAFLKLL----ASEKHYFEPFAECVDHIIAAGEQLIAtrmlRDMLARHQVTLHNHYGP 4623
Cdd:PRK13391  237 EQYLALIEEYGVTH---TQLVPTMFSRMLklpeEVRDKYDLSSLEVAIHAAAPCPPQVK----EQMIDWWGPIIHEYYAA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4624 SETHVVTMYtvdpDTDQELQ---PIGKPISNtEIFILNEAGTLQPVGIVGELCISGVSLARgYHNRESLTLETFVPHPyd 4700
Cdd:PRK13391  310 TEGLGFTAC----DSEEWLAhpgTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDG-- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4701 snqRMYKTGDLArYLPEGNIEYAGRRDHQVKIR-GYRVELGEVEAALLKH--VQEAVVLAKENTD-GQS----------- 4765
Cdd:PRK13391  382 ---TWSTVGDIG-YVDEDGYLYLTDRAAFMIISgGVNIYPQEAENLLITHpkVADAAVFGVPNEDlGEEvkavvqpvdgv 457
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876 4766 DLYAYFTAEQslsISQLKEKLAgqipGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK13391  458 DPGPALAAEL---IAFCRQRLS----RQKCPRSIDFEDELPRLPTGKLYKRLL 503
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3430-3778 1.80e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 84.64  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3430 YTSGTTGKPKGTLIEHRQVI---HLIeGLsRQVYSAYDaelNIAMLAPYY--FdASVQQMYASLLSGHTlfIVPKEIVSD 3504
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVnngYFI-GE-RLGLTEQD---RLCIPVPLFhcF-GSVLGVLACLTHGAT--MVFPSPSFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3505 GAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHL---LIGGEALSKTTVNKLKQLFGehgaAPGITNVYGPTET 3581
Cdd:cd05917    81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLrtgIMAGAPCPPELMKRVIEVMN----MKDVTIAYGMTET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3582 C-------VDASLFniecssdawarsQNYVPIGKPLGRNRMYILDSKKRLQPK-GVQGELYIAGDGVGRGYLNLPELTDE 3653
Cdd:cd05917   157 SpvstqtrTDDSIE------------KRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3654 kfVADPfvpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGY 3733
Cdd:cd05917   225 --AIDG----DGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAW 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 3734 --FAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNR 3778
Cdd:cd05917   299 irLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1787-2256 1.87e-16

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 86.94  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1787 TPDQAAVI---DKDRQ-LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEY---- 1858
Cdd:cd05943    82 ADDPAAIYaaeDGERTeVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFgvpg 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 ---------PQ-----DRIRYmlddsqAGIVLMQRD----VRKQLAYEGVTVLLDDESSYHQ-DGSDLAPIS-------- 1911
Cdd:cd05943   162 vldrfgqiePKvlfavDAYTY------NGKRHDVREkvaeLVKGLPSLLAVVVVPYTVAAGQpDLSKIAKALtledflat 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1912 -----------DVSHLAYVIYTSGSTGRPK-------GVLIEHggltnyiwwakevyvkgeKANFPLYSSIS-----FDL 1968
Cdd:cd05943   236 gaagelefeplPFDHPLYILYSSGTTGLPKcivhgagGTLLQH------------------LKEHILHCDLRpgdrlFYY 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1969 TVTS------IFTPLVTGNAIIVYDGED---KTALLESIVRDPRVDIIKLTPAHLQVLKEMNIA-----DQTAVRRMIVG 2034
Cdd:cd05943   298 TTCGwmmwnwLVSGLAVGATIVLYDGSPfypDTNALWDLADEEGITVFGTSAKYLDALEKAGLKpaethDLSSLRTILST 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2035 GENLSTRLARSIHEQFEGRIEICNEYGPTEtVVGCMiyrydAAKDRRESV---PIGTAAANTSIYVLDENMKPApIGVPG 2111
Cdd:cd05943   378 GSPLKPESFDYVYDHIKPDVLLASISGGTD-IISCF-----VGGNPLLPVyrgEIQCRGLGMAVEAFDEEGKPV-WGEKG 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2112 EIYISGAGVAR--GYLNRPEltAEKFVDDPFE--PGakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAAL 2187
Cdd:cd05943   451 ELVCTKPFPSMpvGFWNDPD--GSRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVV 526
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2188 LQEEVIKEAVVTAREDVHGFKQLCAYYV-SGGQTTAARLRKQLSQTLASYM----VPAYFIELDEMPLTSNGKI 2256
Cdd:cd05943   527 EKIPEVEDSLVVGQEWKDGDERVILFVKlREGVELDDELRKRIRSTIRSALsprhVPAKIIAVPDIPRTLSGKK 600
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
3285-3779 1.92e-16

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 86.48  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3285 IHELFEEQAHRTPDNTAVVFEGKQF--TYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLP 3362
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3363 IDPDSPSERIRYILNDSSISVLLycgklqddIGFSGTCIDLMEEHFY--------------------HEKDSSLALSYQS 3422
Cdd:PRK05852   98 LDPALPIAEQRVRSQAAGARVVL--------IDADGPHDRAEPTTRWwpltvnvggdsgpsggtlsvHLDAATEPTPATS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3423 SQL------AYAIYTSGTTGKPKGTLIEHrqviHLIEGLSRQVYSAYDaelniamLAPYyfDASVQQMyaSLLSGHTLFI 3496
Cdd:PRK05852  170 TPEglrpddAMIMFTGGTTGLPKMVPWTH----ANIASSVRAIITGYR-------LSPR--DATVAVM--PLYHGHGLIA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3497 VP-KEIVSDGAALCRYYRQHS-------IDITDGT-----PAHLKLLIAAGDLQGVTLQHLLIG-----GEALSKTTVNK 3558
Cdd:PRK05852  235 ALlATLASGGAVLLPARGRFSahtfwddIKAVGATwytavPTIHQILLERAATEPSGRKPAALRfirscSAPLTAETAQA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3559 LKQLFGehgaAPgITNVYGPTETCVDASLFNIECSsdawARSQNYVPIGKPLGRN---RMYILDSKKRLQPKGVQGELYI 3635
Cdd:PRK05852  315 LQTEFA----AP-VVCAFGMTEATHQVTTTQIEGI----GQTENPVVSTGLVGRStgaQIRIVGSDGLPLPAGAVGEVWL 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3636 AGDGVGRGYLNLPELTDEKFVadpfvpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:PRK05852  386 RGTTVVRGYLGDPTITAANFT-------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVME 458
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 3716 AAAAALKDADDEYYLCGYFAADKTIQIS--ELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQ 3779
Cdd:PRK05852  459 AAVFGVPDQLYGEAVAAVIVPRESAPPTaeELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
289-693 2.05e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 86.11  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAG----GAYVPLDpeypKERLQYLLHDADADVL 364
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNipivTVYATLG----EDALIHSLNETECSAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  365 LvqhhlknslafdgpvidlndeasyhadCSllspvAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSL--QWKKAFFKHS 442
Cdd:cd17639    82 F---------------------------TD-----GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIagLGDRVPELLG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  443 PADRVLVLYPYvfdAFILNFFGPLIS---------GATLHLLPN---------EENKETF-----AIQNAIKQERITHFS 499
Cdd:cd17639   130 PDDRYLAYLPL---AHIFELAAENVClyrggtigyGSPRTLTDKskrgckgdlTEFKPTLmvgvpAIWDTIRKGVLAKLN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  500 TSPRLLKTMIEQ-MNREDFI------------------------HVQHVVVGGEQLETDTVEKLHSLQPRIRINneYGPT 554
Cdd:cd17639   207 PMGGLKRTLFWTaYQSKLKAlkegpgtplldelvfkkvraalggRLRYMLSGGAPLSADTQEFLNIVLCPVIQG--YGLT 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  555 ENSVVSTfhpVQSADEQIT--IGSPVANHQAYIL----GAHHQIQPIgiP-GELYVGGAGVARGYLNRPELTEEKFVehl 627
Cdd:cd17639   285 ETCAGGT---VQDPGDLETgrVGPPLPCCEIKLVdweeGGYSTDKPP--PrGEILIRGPNVFKGYYKNPEKTKEAFD--- 356
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  628 hvpGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIR-GYRIEIGEVEAAMFNLENVREAAVVAREDAD 693
Cdd:cd17639   357 ---GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKS 420
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
3281-3776 2.39e-16

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 86.26  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3281 REKTIHELFEEQAHRTPDNTAVV------FEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVL 3354
Cdd:PRK13295   22 HDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3355 KAGGAYLPIDPDSPSERIRYILNDSSISVLL------------YCGKLQDD---------IGFSGTciDLMEEHF---YH 3410
Cdd:PRK13295  102 RIGAVLNPLMPIFRERELSFMLKHAESKVLVvpktfrgfdhaaMARRLRPElpalrhvvvVGGDGA--DSFEALLitpAW 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3411 EKDSSLALSYQSSQ-----LAYAIYTSGTTGKPKGtliehrqVIHLieglSRQVYSAYDAELNIAMLAPyyfdASVQQMy 3485
Cdd:PRK13295  180 EQEPDAPAILARLRpgpddVTQLIYTSGTTGEPKG-------VMHT----ANTLMANIVPYAERLGLGA----DDVILM- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3486 ASLLSGHTLFI----VPKEI--------VSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGV---TLQHLLIGGEA 3550
Cdd:PRK13295  244 ASPMAHQTGFMyglmMPVMLgatavlqdIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRpvsSLRTFLCAGAP 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3551 LSKTTVNKLKQLFGEHgaapgITNVYGPTETcvdaSLFNIECSSDAWARSQNyvPIGKPLGRNRMYILDSKKRLQPKGVQ 3630
Cdd:PRK13295  324 IPGALVERARAALGAK-----IVSAWGMTEN----GAVTLTKLDDPDERAST--TDGCPLPGVEVRVVDADGAPLPAGQI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3631 GELYIAGDGVGRGYLNLPELTDEKFvadpfvpeDRMYRTGDLARLLPDGNIEYIGRiDHQVKIQGFR-IELGEIESVMLN 3709
Cdd:PRK13295  393 GRLQVRGCSNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYR 463
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 3710 VPDIQEAAAAALKDADDEYYLCGYFA--ADKTIQISEL-----RKRMARHlpgyMIPAHFVQLDKMPLTPNGKL 3776
Cdd:PRK13295  464 HPAIAQVAIVAYPDERLGERACAFVVprPGQSLDFEEMveflkAQKVAKQ----YIPERLVVRDALPRTPSGKI 533
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
887-1163 2.49e-16

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 85.20  E-value: 2.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  887 LRRTMERIASHHDALRMIFEKTPDGYAPrITGTDESELFHLEVMNYKGETDPAQAIADKANEIQSsmvLDKGPLMKLGLF 966
Cdd:cd19532    41 LERAVRAVGQRHEALRTCFFTDPEDGEP-MQGVLASSPLRLEHVQISDEAEVEEEFERLKNHVYD---LESGETMRIVLL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  967 QCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYeqaerrQTIQLPQKTDSFPFWAD-QLSKYAAEtDMEEEIAYW-TEL 1043
Cdd:cd19532   117 SLSPTEHyLIFGYHHIAMDGVSFQIFLRDLERAY------NGQPLLPPPLQYLDFAArQRQDYESG-ALDEDLAYWkSEF 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1044 SSIkPQPLPkdtisegsLLR-------------DSEEVTIQWTKEETEQLLK--QANRA-----YntdindllLTSLGLA 1103
Cdd:cd19532   190 STL-PEPLP--------LLPfakvksrppltryDTHTAERRLDAALAARIKEasRKLRVtpfhfY--------LAALQVL 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1104 VHKWTGTEDIVVNLEGHGRepiiPDADISRTIGWFTSQYPVVLRMEAGKNLSQRIKIVKE 1163
Cdd:cd19532   253 LARLLDVDDICIGIADANR----TDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRD 308
PRK07788 PRK07788
acyl-CoA synthetase; Validated
4337-4819 2.75e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 86.13  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4337 LFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPEL 4416
Cdd:PRK07788   54 LVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4417 PEKRRAFMLKDSGADVLL-----TCAGHAIPPlfegevlLLDDPLLYQGRTDNLNLSCSE----NDLM------------ 4475
Cdd:PRK07788  134 SGPQLAEVAAREGVKALVyddefTDLLSALPP-------DLGRLRAWGGNPDDDEPSGSTdetlDDLIagsstaplpkpp 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4476 ----YVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQFAAmsfdvcyqEMFSA--LSSGGILFIIGNEA-- 4547
Cdd:PRK07788  207 kpggIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPA--------PMFHAtgWAHLTLAMALGSTVvl 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4548 --KRDIRQLNDFVRTHGIQTAFL-PTAFLKLLASEKHYFEPF-AECVDHIIAAGEQLIATRMLRDMLARHQVtLHNHYGP 4623
Cdd:PRK07788  279 rrRFDPEATLEDIAKHKATALVVvPVMLSRILDLGPEVLAKYdTSSLKIIFVSGSALSPELATRALEAFGPV-LYNLYGS 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4624 SETHVVTMYT-----VDPDTdqelqpIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYhnresltleTFVPHP 4698
Cdd:PRK07788  358 TEVAFATIATpedlaEAPGT------VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY---------TDGRDK 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4699 ydsnQR---MYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA 4773
Cdd:PRK07788  423 ----QIidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHpdVVEAAVIGVDDEEFGQRLRAFVVK 498
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166797876 4774 EQSLSISQ------LKEKLAgqipGYMIPSYFIQLEKLPLTGNGKVNRRALP 4819
Cdd:PRK07788  499 APGAALDEdaikdyVRDNLA----RYKVPRDVVFLDELPRNPTGKVLKRELR 546
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
289-649 2.84e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 86.12  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGV--QPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLV 366
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  367 QHHLKnslafdgpVIDLND----EASYHADCSLLSPvaghSHLAYVIYTSGTTGKPKGVMVEHGGIVNSL----QWKKAF 438
Cdd:cd05927    86 DAGVK--------VYSLEEfeklGKKNKVPPPPPKP----EDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEIL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  439 FKHSPADRVLVLYPY--VFDAFILN---FFGPLI---SGATLHLLPNeenketfaiqnaIKQERITHFSTSPRLL----- 505
Cdd:cd05927   154 NKINPTDVYISYLPLahIFERVVEAlflYHGAKIgfySGDIRLLLDD------------IKALKPTVFPGVPRVLnriyd 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  506 --------KTMIEQ------MNRE---------------DFI-----------HVQHVVVGGEQLETDTVEKLHSLqPRI 545
Cdd:cd05927   222 kifnkvqaKGPLKRklfnfaLNYKlaelrsgvvraspfwDKLvfnkikqalggNVRLMLTGSAPLSPEVLEFLRVA-LGC 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  546 RINNEYGPTENSVVSTfhpVQSADEQI--TIGSPVANHQayilgahhqIQPIGIP------------GELYVGGAGVARG 611
Cdd:cd05927   301 PVLEGYGQTECTAGAT---LTLPGDTSvgHVGGPLPCAE---------VKLVDVPemnydakdpnprGEVCIRGPNVFSG 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 166797876  612 YLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRI 649
Cdd:cd05927   369 YYKDPEKTAEALDEDgwLH--------TGDIGEWLPNGTL 400
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
3269-3778 3.58e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 85.59  E-value: 3.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3269 LSRFQSNDMHYPREKTIHELFEEQAHRTPDNTAVVF--EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEM 3346
Cdd:PRK12583    4 PSYYQGGGDKPLLTQTIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEW 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3347 VVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL---------YCGKLQDDIG--FSGTCIDLMEEHFYH----- 3410
Cdd:PRK12583   84 LLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIcadafktsdYHAMLQELLPglAEGQPGALACERLPElrgvv 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3411 --------------------EKDSSLALSYQSSQL----AYAI-YTSGTTGKPKGTLIEHRQVihliegLSRQVYSAYDA 3465
Cdd:PRK12583  164 slapapppgflawhelqargETVSREALAERQASLdrddPINIqYTSGTTGFPKGATLSHHNI------LNNGYFVAESL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3466 ELNIA--MLAP---YYFDASVQQMYASLLSGHTLfIVPKEIVsDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVT 3540
Cdd:PRK12583  238 GLTEHdrLCVPvplYHCFGMVLANLGCMTVGACL-VYPNEAF-DPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3541 LQHLLIGGEALSKTTVNKLKQLFGE-HgaAPGITNVYGPTETcvdASLFNIECSSDAWARSQNYVpiGKPLGRNRMYILD 3619
Cdd:PRK12583  316 LSSLRTGIMAGAPCPIEVMRRVMDEmH--MAEVQIAYGMTET---SPVSLQTTAADDLERRVETV--GRTQPHLEVKVVD 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3620 SKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrMYrTGDLARLLPDGNIEYIGRIDHQVKIQGFRIE 3699
Cdd:PRK12583  389 PDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIY 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3700 LGEIESVMLNVPDIQEaaaAALKDADDEYY---LCGY--FAADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNG 3774
Cdd:PRK12583  463 PREIEEFLFTHPAVAD---VQVFGVPDEKYgeeIVAWvrLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTG 539

                  ....
gi 166797876 3775 KLNR 3778
Cdd:PRK12583  540 KVQK 543
PLN03102 PLN03102
acyl-activating enzyme; Provisional
273-754 4.45e-16

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 85.46  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:PLN03102   24 SECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVQHHL----KNSLAF--------DGPVIDLND----------EASYHADCSLLSPVAGHSHLAYVI- 409
Cdd:PLN03102  104 AAILRHAKPKILFVDRSFeplaREVLHLlssedsnlNLPVIFIHEidfpkrpsseELDYECLIQRGEPTPSLVARMFRIq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  410 ---------YTSGTTGKPKGVMVEHGGIVNS-----LQWKKAFFKhspadrvlvLYPYVFDAFILN----FFGPLISGAT 471
Cdd:PLN03102  184 dehdpislnYTSGTTADPKGVVISHRGAYLStlsaiIGWEMGTCP---------VYLWTLPMFHCNgwtfTWGTAARGGT 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  472 LHLLPNEENKEtfaIQNAIKQERITHFSTSPRLLKTMIEQmNREDFIHVQ---HVVVGGEQLETDTVEKLHSLQprIRIN 548
Cdd:PLN03102  255 SVCMRHVTAPE---IYKNIEMHNVTHMCCVPTVFNILLKG-NSLDLSPRSgpvHVLTGGSPPPAALVKKVQRLG--FQVM 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  549 NEYGPTENSVVSTFHPVQsaDEQitigSPVANHQAYILGAHHQIQPIGIP--------------------GELYVGGAGV 608
Cdd:PLN03102  329 HAYGLTEATGPVLFCEWQ--DEW----NRLPENQQMELKARQGVSILGLAdvdvknketqesvprdgktmGEIVIKGSSI 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  609 ARGYLNRPELTEEKFvEHlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVA 688
Cdd:PLN03102  403 MKGYLKNPKATSEAF-KH------GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  689 REDADGAKQLYAYYVGEPSLTAAQFRE-----------ELSRE-LPNYMIPSRFIPLERIPLTSNGKI------DL-KAL 749
Cdd:PLN03102  476 MPHPTWGETPCAFVVLEKGETTKEDRVdklvtrerdliEYCREnLPHFMCPRKVVFLQELPKNGNGKIlkpklrDIaKGL 555

                  ....*
gi 166797876  750 PAADE 754
Cdd:PLN03102  556 VVEDE 560
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
4332-4816 5.54e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 85.05  E-value: 5.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4332 TTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGA-CTDQVVAVLTDRSAHmIIGILAILKAGAAFL 4410
Cdd:PRK05605   32 TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVrPGDRVAIVLPNCPQH-IVAFYAVLRLGAVVV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4411 PIDPELPEKRRAFMLKDSGADVLL---TCAGHA--------------------------------IPPLFE--------- 4446
Cdd:PRK05605  111 EHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVerlrrttpletivsvnmiaampllqrlalrlpIPALRKaraaltgpa 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4447 -GEV---LLLDDPLLYQGRTDNlNLSCSENDLMYVIYTSGTTGQPKGVQLEHKT-MTNLL---AY-----EQDHTQLRfd 4513
Cdd:PRK05605  191 pGTVpweTLVDAAIGGDGSDVS-HPRPTPDDVALILYTSGTTGKPKGAQLTHRNlFANAAqgkAWvpglgDGPERVLA-- 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4514 rVL-QFAAMSFDVCyqeMFSALSSGGILFIIgneAKRDIRQLNDFVRTHgiQTAFLP---TAFLKLL-ASEKH------- 4581
Cdd:PRK05605  268 -ALpMFHAYGLTLC---LTLAVSIGGELVLL---PAPDIDLILDAMKKH--PPTWLPgvpPLYEKIAeAAEERgvdlsgv 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4582 --YFEPFAECVDHIIAAGEQLIATRMLRDmlarhqvtlhnhYGPSETHVVTMytVDPDTDQElQP--IGKPISNTEIFIL 4657
Cdd:PRK05605  339 rnAFSGAMALPVSTVELWEKLTGGLLVEG------------YGLTETSPIIV--GNPMSDDR-RPgyVGVPFPDTEVRIV 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4658 N--EAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHpydsnqrMYKTGDLARYLPEGNIEYAGRRDHQVKIRGY 4735
Cdd:PRK05605  404 DpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGF 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQ--LKEKLAGQIPGYMIPSYFIQLEKLPLTGNG 4811
Cdd:PRK05605  477 NVYPAEVEEVLREHpgVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556

                  ....*
gi 166797876 4812 KVNRR 4816
Cdd:PRK05605  557 KVRRR 561
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
3306-3715 5.86e-16

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 84.33  E-value: 5.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3306 GKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL 3385
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3386 ycgklqddigfsgtcIDlmeehfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQVI-------HLIEGLSRQ 3458
Cdd:cd05940    81 ---------------VD----------------------AALYIYTSGTTGLPKAAIISHRRAWrggaffaGSGGALPSD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3459 VYsaYDAelniamLAPYYFDASVQQMYASLLSGHTLFIVPK--------EIVSDGAA-------LCRYYRQHSIDITDgt 3523
Cdd:cd05940   124 VL--YTC------LPLYHSTALIVGWSACLASGATLVIRKKfsasnfwdDIRKYQATifqyigeLCRYLLNQPPKPTE-- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3524 PAHlklliaagdlqgvtlQHLLIGGEALSKTTVNKLKQLFGehgaAPGITNVYGPTETcvDASLFNIECSSDAWARSQNY 3603
Cdd:cd05940   194 RKH---------------KVRMIFGNGLRPDIWEEFKERFG----VPRIAEFYAATEG--NSGFINFFGKPGAIGRNPSL 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3604 VPIGKPLGRNRmYILDSKKRLQ---------PKGVQGELYIAGDGVGR--GYLNlPELTDEKFVADPFVPEDRMYRTGDL 3672
Cdd:cd05940   253 LRKVAPLALVK-YDLESGEPIRdaegrcikvPRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVFKKGDAWFNTGDL 330
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 166797876 3673 ARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05940   331 MRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEE 373
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
3297-3713 6.85e-16

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 84.89  E-value: 6.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVV--FEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDpDSPSERirY 3374
Cdd:cd17642    31 PGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN-DIYNER--E 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3375 ILNDSSIS--VLLYCGK--------LQDDIGFSGTCI------DLME-EHFYHEKDSSLALSYQSS-----------QLA 3426
Cdd:cd17642   108 LDHSLNISkpTIVFCSKkglqkvlnVQKKLKIIKTIIildskeDYKGyQCLYTFITQNLPPGFNEYdfkppsfdrdeQVA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3427 YAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVY-SAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKeivSDG 3505
Cdd:cd17642   188 LIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFgNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYK---FEE 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3506 AALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHL---LIGGEALSKTTVNKLKQLFGehgaAPGITNVYGPTETc 3582
Cdd:cd17642   265 ELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLheiASGGAPLSKEVGEAVAKRFK----LPGIRQGYGLTET- 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3583 vdASLFNIECSSDAWARSQNYVpigKPLGRNRMYILDSKKRLQPKGvQGELYIAGDGVGRGYLNLPELTDEkfvadpFVP 3662
Cdd:cd17642   340 --TSAILITPEGDDKPGAVGKV---VPFFYAKVVDLDTGKTLGPNE-RGELCVKGPMIMKGYVNNPEATKA------LID 407
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876 3663 EDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:cd17642   408 KDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKI 458
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
4925-5332 7.30e-16

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 83.84  E-value: 7.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4925 PVSSVQKMvyLTTQIIGGELPYNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVE--FSMER 5002
Cdd:cd19534     3 PLTPIQRW--FFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5003 YEATADEVEECFRAFV----RPFDLSQAPLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLYDGKELA---- 5074
Cdd:cd19534    81 VDLSSLAQAAAIEALAaeaqSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGepip 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5075 -PLRIQYKDFTEWKHQKEQRERIKSQEEYWLGVFHEelPSFELPKDfarPPVRSFDGKRHNFTLDKTVTqgiKQLeeLTG 5153
Cdd:cd19534   161 lPSKTSFQTWAELLAEYAQSPALLEELAYWRELPAA--DYWGLPKD---PEQTYGDARTVSFTLDEEET---EAL--LQE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5154 STAYM------ILFSAYSILLAKYSGQDDIVVGTPIAGR----PHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKE 5223
Cdd:cd19534   231 ANAAYrteindLLLAALALAFQDWTGRAPPAIFLEGHGReeidPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5224 TMLKAFEHqeypfeelveklGVKRDLSRNPLFDTMFVLQNTEQTDI----------EVDSLAVRPYEQTETAAKFD---- 5289
Cdd:cd19534   311 QLRRIPNK------------GIGYGILRYLTPEGTKRLAFHPQPEIsfnylgqfdqGERDDALFVSAVGGGGSDIGpdtp 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 5290 ----LQLNFLIDQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIM 5332
Cdd:cd19534   379 rfalLDINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALI 425
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
4327-4818 7.40e-16

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 85.75  E-value: 7.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4327 EKRIPT--TIHQLFEQQAERNPDHEAVM-FGNQTLTYRQLNERSNQLARVLQDKGAcTDQVVAVLTDRSAHMIIGILAIL 4403
Cdd:PRK08633  608 KSRKEAlpPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALARLLKRELK-DEENVGILLPPSVAGALANLALL 686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4404 KAGA------------------------------AFL------PIDPELPEKRRAFMLKD-----SGADVLLTCAGHAIP 4442
Cdd:PRK08633  687 LAGKvpvnlnytaseaalksaieqaqiktvitsrKFLeklknkGFDLELPENVKVIYLEDlkakiSKVDKLTALLAARLL 766
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4443 PLFegevLLLddpLLYQGRTDNlnlscseNDLMYVIYTSGTTGQPKGVQLEHKtmtNLLA-YEQDHTQLRF---DRVLQ- 4517
Cdd:PRK08633  767 PAR----LLK---RLYGPTFKP-------DDTATIIFSSGSEGEPKGVMLSHH---NILSnIEQISDVFNLrndDVILSs 829
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4518 ---FAAMSFDVcyqEMFSALSSGgiLFIIGNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKL-LASEKHYFEPFAEcVDHI 4593
Cdd:PRK08633  830 lpfFHSFGLTV---TLWLPLLEG--IKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLyLRNKKLHPLMFAS-LRLV 903
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4594 IAAGEQLiATRMLRDMLARHQVTLHNHYGPSETH-VVTMYTvdPDT---DQELQP------IGKPISNTEIFILN-EAGT 4662
Cdd:PRK08633  904 VAGAEKL-KPEVADAFEEKFGIRILEGYGATETSpVASVNL--PDVlaaDFKRQTgskegsVGMPLPGVAVRIVDpETFE 980
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4663 LQPVGIVGELCISGVSLARGYHNRESLTLEtfVPHPYDSnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEV 4742
Cdd:PRK08633  981 ELPPGEDGLILIGGPQVMKGYLGDPEKTAE--VIKDIDG-IGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAV 1057
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4743 EAALLKHV-QEAVVLAKENTD----GQSdlYAYFTAEQSLSISQLKEKLA-GQIPGYMIPSYFIQLEKLPLTGNGKVNRR 4816
Cdd:PRK08633 1058 EEELAKALgGEEVVFAVTAVPdekkGEK--LVVLHTCGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLK 1135

                  ..
gi 166797876 4817 AL 4818
Cdd:PRK08633 1136 GL 1137
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
272-744 7.91e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 84.29  E-value: 7.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  272 QAERTPENAAVKFKN--DHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPK 349
Cdd:PRK13390    6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  350 ERLQYLLHDADADVLLVQHHLKN-----------SLAFDGpviDLNDEASYHADCSLLSP-VAGHSHLAYVIYTSGTTGK 417
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAALDGlaakvgadlplRLSFGG---EIDGFGSFEAALAGAGPrLTEQPCGAVMLYSSGTTGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  418 PKGVMVE-HGGIVNS-----LQWKKAFFKHSPADRVLVLYPyVFDAFILNFFGPLIS-GATLHLLPNEENKETFaiqNAI 490
Cdd:PRK13390  163 PKGIQPDlPGRDVDApgdpiVAIARAFYDISESDIYYSSAP-IYHAAPLRWCSMVHAlGGTVVLAKRFDAQATL---GHV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  491 KQERITHFSTSP----RLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIrINNEYGPTENSVVSTFHPVQ 566
Cdd:PRK13390  239 ERYRITVTQMVPtmfvRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAHGMTFIDSPD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  567 SADEQITIGSPVanhqayiLGAHHQIQ------PIGIPGELYVGGAGVARGYLNRPELTEEkfVEHlhvPGQKMYKT-GD 639
Cdd:PRK13390  318 WLAHPGSVGRSV-------LGDLHICDddgnelPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQH---PAHPFWTTvGD 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  640 LARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYvgepSLTAA-QFREELS 718
Cdd:PRK13390  386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVI----QLVEGiRGSDELA 461
                         490       500       510
                  ....*....|....*....|....*....|....
gi 166797876  719 REL--------PNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK13390  462 RELidytrsriAHYKAPRSVEFVDELPRTPTGKL 495
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4356-4751 8.56e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 84.05  E-value: 8.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRrafmlkdsgadvLLT 4435
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKN------------LKQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 CAGHAIPPLFEGEVLLLDDpllyqgrtdnlnlscsendlMYVIYTSGTTGQPKGVQLEHKTMtnllayeqdHTQL-RFDR 4514
Cdd:cd05910    69 CLQEAEPDAFIGIPKADEP--------------------AAILFTSGSTGTPKGVVYRHGTF---------AAQIdALRQ 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4515 VLQFAAMSFDVCYQEMFSALSSG-GILFIIGN-----EAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLAS--EKHYFePF 4586
Cdd:cd05910   120 LYGIRPGEVDLATFPLFALFGPAlGLTSVIPDmdptrPARADPQKLVGAIRQYGVSIVFGSPALLERVARycAQHGI-TL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4587 AEcVDHIIAAGEQLIATRM--LRDMLArHQVTLHNHYGPSETHVVTMYTvDPDTDQELQP---------IGKPISNTEIF 4655
Cdd:cd05910   199 PS-LRRVLSAGAPVPIALAarLRKMLS-DEAEILTPYGATEALPVSSIG-SRELLATTTAatsggagtcVGRPIPGVRVR 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4656 IL--NEAGTLQ-------PVGIVGELCISGVSLARGYHNRESLTLETFVPHPydSNQRMYKTGDLARYLPEGNIEYAGRR 4726
Cdd:cd05910   276 IIeiDDEPIAEwddtlelPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDEGRLWFCGRK 353
                         410       420
                  ....*....|....*....|....*
gi 166797876 4727 DHQVKIRGYRVELGEVEAALLKHVQ 4751
Cdd:cd05910   354 AHRVITTGGTLYTEPVERVFNTHPG 378
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
255-712 9.26e-16

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 84.26  E-value: 9.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  255 TVRDFsgsrtVYQLFEEQAERTPENAAVKFKNdhLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVW 334
Cdd:PLN02330   29 TLPDF-----VLQDAELYADKVAFVEAVTGKA--VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIM 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  335 KAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH-HLKNSLAFDGPVIDLND-------------EASYHADCSLLSPVA 400
Cdd:PLN02330  102 AAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtNYGKVKGLGLPVIVLGEekiegavnwkellEAADRAGDTSDNEEI 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  401 GHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQwkKAFFKHSPAD----RVLVLYPYvfdafiLNFFGplISGATLHLLP 476
Cdd:PLN02330  182 LQTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGPEMigqvVTLGLIPF------FHIYG--ITGICCATLR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  477 NE------ENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDF----IHVQHVVVGGEQLETDTVEKLHSLQPRIR 546
Cdd:PLN02330  252 NKgkvvvmSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFdlskLKLQAIMTAAAPLAPELLTAFEAKFPGVQ 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  547 INNEYGPTENSVVSTFHPVQSADEQI----TIGSPVANHQA-YILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEE 621
Cdd:PLN02330  332 VQEAYGLTEHSCITLTHGDPEKGHGIakknSVGFILPNLEVkFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDR 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  622 KFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLY 699
Cdd:PLN02330  412 TIDEDgwLH--------TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPA 483
                         490
                  ....*....|...
gi 166797876  700 AYYVGEPSLTAAQ 712
Cdd:PLN02330  484 ACVVINPKAKESE 496
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
4307-4818 9.75e-16

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 84.26  E-value: 9.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4307 MMTKEEERDIQQLFNDTAVAEK-RIPTTIHQLFEQQAERNPDHEAVMfgNQTLTYRQLNERSNQLARVLQDKGACTDQVV 4385
Cdd:PLN02330    6 QKQEDNEHIFRSRYPSVPVPDKlTLPDFVLQDAELYADKVAFVEAVT--GKAVTYGEVVRDTRRFAKALRSLGLRKGQVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4386 AVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTCAGHAipplfeGEVLLLDDPLLYQGRTDNL 4465
Cdd:PLN02330   84 VVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNY------GKVKGLGLPVIVLGEEKIE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4466 NL-----------SCS---------ENDLMYVIYTSGTTGQPKGVQLEHKTM-TNLLAYEQDHTQLRFDRVLQFAAMSF- 4523
Cdd:PLN02330  158 GAvnwkelleaadRAGdtsdneeilQTDLCALPFSSGTTGISKGVMLTHRNLvANLCSSLFSVGPEMIGQVVTLGLIPFf 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4524 ------DVCyqemFSALSSGGILFIIGneaKRDIRQLNDFVRTHGIQTA-FLPTAFLKLLAsekhyfEPFAECVD----- 4591
Cdd:PLN02330  238 hiygitGIC----CATLRNKGKVVVMS---RFELRTFLNALITQEVSFApIVPPIILNLVK------NPIVEEFDlsklk 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4592 --HIIAAGEQLiATRMLRDMLARH-QVTLHNHYGPSETHVVTMYTVDPDTDQEL---QPIGKPISNTEI-FILNEAGTLQ 4664
Cdd:PLN02330  305 lqAIMTAAAPL-APELLTAFEAKFpGVQVQEAYGLTEHSCITLTHGDPEKGHGIakkNSVGFILPNLEVkFIDPDTGRSL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4665 PVGIVGELCISGVSLARGYHNRESLTLETFvphpydSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEA 4744
Cdd:PLN02330  384 PKNTPGELCVRSQCVMQGYYNNKEETDRTI------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4745 ALLKH--VQEA-----------------VVLAKENTDGQSDLYAYFTAeqslSISQLKEKLAGQIpgymipsyfiqLEKL 4805
Cdd:PLN02330  458 ILLTHpsVEDAavvplpdeeageipaacVVINPKAKESEEDILNFVAA----NVAHYKKVRVVQF-----------VDSI 522
                         570
                  ....*....|...
gi 166797876 4806 PLTGNGKVNRRAL 4818
Cdd:PLN02330  523 PKSLSGKIMRRLL 535
PRK05850 PRK05850
acyl-CoA synthetase; Validated
3284-3687 1.10e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 84.22  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVF-------EG--KQFTYEELNRRANQLARTLQAKGVQADQLVgIMTERSLEMVVGILGVL 3354
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFidyeqdpAGvaETLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3355 KAGGAYLPIDPDSPS---ERIRYILNDSSISVLLYCGKLQDDIGFSGTC-----------IDLMEEHfyhEKDSSLALSY 3420
Cdd:PRK05850   81 QAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPqpgqsappvieVDLLDLD---SPRGSDARPR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3421 QSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYD--AELNIAMLA--PYYFDAS-VQQMYASLLSGHtlf 3495
Cdd:PRK05850  158 DLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGgvPPPDTTVVSwlPFYHDMGlVLGVCAPILGGC--- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3496 ivPKEIVSDGAALCRYYR--------QHSID-------------ITDgtpahlklliaaGDLQGVTLQHLLI---GGEAL 3551
Cdd:PRK05850  235 --PAVLTSPVAFLQRPARwmqllasnPHAFSaapnfafelavrkTSD------------DDMAGLDLGGVLGiisGSERV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3552 SKTTVNKLKQLFGEHGAAP-GITNVYG----------------PTETCVDA-SLFN---IECSSDAWARSQNYVPIGKPL 3610
Cdd:PRK05850  301 HPATLKRFADRFAPFNLREtAIRPSYGlaeatvyvatrepgqpPESVRFDYeKLSAghaKRCETGGGTPLVSYGSPRSPT 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3611 GRnrmyILDSKKRLQ-PKGVQGELYIAGDGVGRGYLNLPELTDEKFVA-----DPFVPEDRMYRTGDLArLLPDGNIEYI 3684
Cdd:PRK05850  381 VR----IVDPDTCIEcPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpSPGTPEGPWLRTGDLG-FISEGELFIV 455

                  ...
gi 166797876 3685 GRI 3687
Cdd:PRK05850  456 GRI 458
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
273-692 1.20e-15

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 83.38  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERL 352
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  353 QYLLHDADADVLLVQHHLKNSLAFDgpVIDLNDEASYHADCsllspvAGHSHLAYVIYTSGTTGKPKGVmvehggiVNSL 432
Cdd:PRK09029   93 EELLPSLTLDFALVLEGENTFSALT--SLHLQLVEGAHAVA------WQPQRLATMTLTSGSTGLPKAA-------VHTA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  433 QwkkaffKH-SPADRVLVLYPY-VFDAFILNFfgP-------------LISGATLHLlpNEENKETFAIQNAikqeriTH 497
Cdd:PRK09029  158 Q------AHlASAEGVLSLMPFtAQDSWLLSL--PlfhvsgqgivwrwLYAGATLVV--RDKQPLEQALAGC------TH 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  498 FSTSP----RLLKTMIEQMNredfihVQHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTEnsVVSTFHPVQsADEQIT 573
Cdd:PRK09029  222 ASLVPtqlwRLLDNRSEPLS------LKAVLLGGAAIPVELTEQAEQQG--IRCWCGYGLTE--MASTVCAKR-ADGLAG 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  574 IGSPVANHQAYILGahhqiqpigipGELYVGGAGVARGYLN----RPeLTEEkfvehlhvpgQKMYKTGDLARWLpDGRI 649
Cdd:PRK09029  291 VGSPLPGREVKLVD-----------GEIWLRGASLALGYWRqgqlVP-LVND----------EGWFATRDRGEWQ-NGEL 347
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 166797876  650 EYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDA 692
Cdd:PRK09029  348 TILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADA 390
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
408-745 1.22e-15

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 81.93  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 VIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyVFDAFILNffgplISGATLHLLPNEENKETFAIQ 487
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLP-LFHIAGLN-----LALATFHAGGANVVMEKFDPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  488 NA---IKQERITHFSTSPRLLKTMIEQMNREDF-IHVQHVVVGgeqLET-DTVEKLHSLQPRiRINNEYGPTENSVVSTF 562
Cdd:cd17637    79 EAlelIEEEKVTLMGSFPPILSNLLDAAEKSGVdLSSLRHVLG---LDApETIQRFEETTGA-TFWSLYGQTETSGLVTL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  563 HPvqSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLHvpgqkmyKTGDLAR 642
Cdd:cd17637   155 SP--YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWH-------HTGDLGR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  643 WLPDGRIEYLGRIDHQ--VKIRGYRIEIGEVEAAMFNLENVREAAVVAREDA---DGAKQLYAYYVGEpSLTAAQFREEL 717
Cdd:cd17637   226 FDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPkwgEGIKAVCVLKPGA-TLTADELIEFV 304
                         330       340
                  ....*....|....*....|....*...
gi 166797876  718 SRELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:cd17637   305 GSRIARYKKPRYVVFVEALPKTADGSID 332
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
3283-3787 1.27e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 84.04  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3283 KTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAK-GVQADQLVGIMTERSLEMVVGILGVLKAGGAYL 3361
Cdd:PRK05677   24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3362 PIDPDSPSERIRYILNDSSISVLLYCGKLQD-----------------DIG-----FSGTCIDLMEEHF------YH--- 3410
Cdd:PRK05677  104 NTNPLYTAREMEHQFNDSGAKALVCLANMAHlaekvlpktgvkhvivtEVAdmlppLKRLLINAVVKHVkkmvpaYHlpq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3411 -----------EKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRqviHLIEGLSrQVYSAYDAELN------IAMLA 3473
Cdd:PRK05677  184 avkfndalakgAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHR---NLVANML-QCRALMGSNLNegceilIAPLP 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3474 PYYFDASVQQMYASLLSG-HTLFIV-PKEIvsdgAALCRYYRQHSIDITDGtpahLKLLIAA-------GDLQGVTLQHL 3544
Cdd:PRK05677  260 LYHIYAFTFHCMAMMLIGnHNILISnPRDL----PAMVKELGKWKFSGFVG----LNTLFVAlcnneafRKLDFSALKLT 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3545 LIGGEALSKTTVNKLKQLFGehgaaPGITNVYGPTETCVDASLF---NIECSSdawarsqnyvpIGKPLGRNRMYILDSK 3621
Cdd:PRK05677  332 LSGGMALQLATAERWKEVTG-----CAICEGYGMTETSPVVSVNpsqAIQVGT-----------IGIPVPSTLCKVIDDD 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3622 KRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELG 3701
Cdd:PRK05677  396 GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPN 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3702 EIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAA--DKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK-LNR 3778
Cdd:PRK05677  470 ELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVkpGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKiLRR 549

                  ....*....
gi 166797876 3779 QLLPAPVKK 3787
Cdd:PRK05677  550 ELRDEELKK 558
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
4337-4818 1.41e-15

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 83.95  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4337 LFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQD-----KGactdqvvavltDRSAHMI-------IGILAILK 4404
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNglglkKG-----------DRVALMMpnllqypIALFGILR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4405 AGAAFLPIDPELPEKRRAFMLKDSGA-----------------------DVLLTCAGHAIPplFEGEVLL---------- 4451
Cdd:PRK08974   97 AGMIVVNVNPLYTPRELEHQLNDSGAkaivivsnfahtlekvvfktpvkHVILTRMGDQLS--TAKGTLVnfvvkyikrl 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4452 -----LDDPL-----LYQG-RTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTM-TNLL----AYEqdhTQLRFDRV 4515
Cdd:PRK08974  175 vpkyhLPDAIsfrsaLHKGrRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlANLEqakaAYG---PLLHPGKE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4516 LQFAAMSFdvcYQeMFsALSSGGILFI--------IGNeaKRDI----RQLND--FVRTHGIQTAFlpTAflkLLASEKh 4581
Cdd:PRK08974  252 LVVTALPL---YH-IF-ALTVNCLLFIelggqnllITN--PRDIpgfvKELKKypFTAITGVNTLF--NA---LLNNEE- 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4582 yfepFAEcVD----HIIAAG----EQLIATRMlrdmlarHQVT---LHNHYGPSE-THVVTMYTVDpdTDQELQPIGKPI 4649
Cdd:PRK08974  319 ----FQE-LDfsslKLSVGGgmavQQAVAERW-------VKLTgqyLLEGYGLTEcSPLVSVNPYD--LDYYSGSIGLPV 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4650 SNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQ 4729
Cdd:PRK08974  385 PSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-------KDGWLATGDIAVMDEEGFLRIVDRKKDM 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4730 VKIRGYRVELGEVEAALLKH--VQEAVVLAKENtDGQSDLYAYFTA--EQSLSISQLKEKLAGQIPGYMIPSYFIQLEKL 4805
Cdd:PRK08974  458 ILVSGFNVYPNEIEDVVMLHpkVLEVAAVGVPS-EVSGEAVKIFVVkkDPSLTEEELITHCRRHLTGYKVPKLVEFRDEL 536
                         570
                  ....*....|...
gi 166797876 4806 PLTGNGKVNRRAL 4818
Cdd:PRK08974  537 PKSNVGKILRREL 549
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1784-2261 1.56e-15

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 83.00  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1784 SQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDR- 1862
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLl 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 --------IRYMLDDSQAGIVLMQRDVRKQLAYEGVTVLLDDESsyhqdgsdlapisdvshLAYVIYTSGSTGRPKGVLI 1934
Cdd:PRK09029   93 eellpsltLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQR-----------------LATMTLTSGSTGLPKAAVH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1935 EHGG-LTNyiwwAKEVYvkgEKANF----------PLYSsisfdltvtsiftplVTGNAII-----------VYDGEDkt 1992
Cdd:PRK09029  156 TAQAhLAS----AEGVL---SLMPFtaqdswllslPLFH---------------VSGQGIVwrwlyagatlvVRDKQP-- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1993 alLESIVRDprVDIIKLTPAHLQVLKEMNiADQTAVRRMIVGGENLSTRLArsihEQFEGR-IEICNEYGPTE---TVvg 2068
Cdd:PRK09029  212 --LEQALAG--CTHASLVPTQLWRLLDNR-SEPLSLKAVLLGGAAIPVELT----EQAEQQgIRCWCGYGLTEmasTV-- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2069 CmiyrydaAKdRRESVP-IGTAAANTSIYVLDenmkpapigvpGEIYISGAGVARGYLNRPELTAekFVDDpfepgAKMY 2147
Cdd:PRK09029  281 C-------AK-RADGLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLVP--LVND-----EGWF 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2148 KTGDLAKWlADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHgFKQL-CAYYVSGGQTTAARLR 2226
Cdd:PRK09029  335 ATRDRGEW-QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAE-FGQRpVAVVESDSEAAVVNLA 412
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 166797876 2227 KQLSQTLASYMVP-AYFIeLDEMPLTSNGKINKKGL 2261
Cdd:PRK09029  413 EWLQDKLARFQQPvAYYL-LPPELKNGGIKISRQAL 447
PRK08308 PRK08308
acyl-CoA synthetase; Validated
317-752 1.68e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 82.39  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  317 AILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKE---------RLQYLLHDADADVLLvqhHLKNSLAFDGpvidlndea 387
Cdd:PRK08308   36 AVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEaairmakraGCHGLLYGESDFTKL---EAVNYLAEEP--------- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  388 syhadcSLLSpvaghshlayviYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYP----YvfdAFILNFF 463
Cdd:PRK08308  104 ------SLLQ------------YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPvthsY---GLICGVL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  464 GPLISGATLHLLPNEENKetFAIqNAIKQERITHFSTSPRLLKTMIEQMNREDFIHvqHVVVGGEQLeTDTVekLHSLQP 543
Cdd:PRK08308  163 AALTRGSKPVIITNKNPK--FAL-NILRNTPQHILYAVPLMLHILGRLLPGTFQFH--AVMTSGTPL-PEAW--FYKLRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  544 R-IRINNEYGPTENSVVSTFHPVQSADEqitIGSPVAnhqayilgaHHQIQpigipgelyvggAGVARgylNRPElteEK 622
Cdd:PRK08308  235 RtTYMMQQYGCSEAGCVSICPDMKSHLD---LGNPLP---------HVSVS------------AGSDE---NAPE---EI 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  623 FVEHlhvpGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYY 702
Cdd:PRK08308  285 VVKM----GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKV 360
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 166797876  703 VGEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAA 752
Cdd:PRK08308  361 ISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELG 410
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
4333-4818 1.93e-15

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 83.39  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQD-----KGactdqvvavltDRSAHMI-------IGIL 4400
Cdd:PRK08751   26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGelqlkKG-----------DRVALMMpnclqypIATF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4401 AILKAGAAFLPIDPELPEKRRAFMLKDSGADVLL------TCAGHAIPPLFEGEVL------LLDDP------------- 4455
Cdd:PRK08751   95 GVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVvidnfgTTVQQVIADTPVKQVIttglgdMLGFPkaalvnfvvkyvk 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4456 ----------------LLYQGRTDNL-NLSCSENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLAYEQDHTQ-------LR 4511
Cdd:PRK08751  175 klvpeyringairfreALALGRKHSMpTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQwlagtgkLE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4512 FDRVLQFAAMSFdvcyQEMFsALSSGGILFI-IG--NEAKRDIRQLNDFVRT-HGIQ-TAF--LPTAFLKLLASekhyfe 4584
Cdd:PRK08751  252 EGCEVVITALPL----YHIF-ALTANGLVFMkIGgcNHLISNPRDMPGFVKElKKTRfTAFtgVNTLFNGLLNT------ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4585 PFAECVDHI---IAAGEQLIATRMLRDMLAR-HQVTLHNHYGPSETHVVTmyTVDPDTDQELQ-PIGKPISNTEIFILNE 4659
Cdd:PRK08751  321 PGFDQIDFSslkMTLGGGMAVQRSVAERWKQvTGLTLVEAYGLTETSPAA--CINPLTLKEYNgSIGLPIPSTDACIKDD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4660 AGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpyDSNQRMYkTGDLARYLPEGNIEYAGRRDHQVKIRGYRVEL 4739
Cdd:PRK08751  399 AGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVM-----DADGWLH-TGDIARMDEQGFVYIVDRKKDMILVSGFNVYP 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4740 GEVE--AALLKHVQE-AVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRR 4816
Cdd:PRK08751  473 NEIEdvIAMMPGVLEvAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRR 552

                  ..
gi 166797876 4817 AL 4818
Cdd:PRK08751  553 EL 554
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2364-2675 2.27e-15

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 82.25  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2364 LTPIQHWFFEQTTTDQH---YYNQAVM-LHAPegFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQneEIAQSGLYRL 2439
Cdd:cd19543     4 LSPMQEGMLFHSLLDPGsgaYVEQMVItLEGP--LDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQ--VVLKDRKLPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2440 EVMNLKEDPDPGRT--IEA-KADEIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAE 2515
Cdd:cd19543    80 RELDLSHLSEAEQEaeLEAlAEEDRERGFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKELFAIYAALG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2516 NGRVIQLPQkTDSFQLWAKRLSEYAQSETikqeQEYWTK-----IEQTevkPLPKDFHETHTTAKDSETAAVEWTKEETE 2590
Cdd:cd19543   160 EGQPPSLPP-VRPYRDYIAWLQRQDKEAA----EAYWREylagfEEPT---PLPKELPADADGSYEPGEVSFELSAELTA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2591 LLLKQAnRAYHTEINDLLLTSLGLSISHWSGLEQI---------PIHLEGhgreqiiqdidISRTVGWFTSLYPVVLHAQ 2661
Cdd:cd19543   232 RLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVvfgttvsgrPAELPG-----------IETMVGLFINTLPVRVRLD 299
                         330
                  ....*....|....
gi 166797876 2662 PGKEISDYIKTTKE 2675
Cdd:cd19543   300 PDQTVLELLKDLQA 313
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
286-744 2.32e-15

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 83.31  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  286 NDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDpeypkerLQYLLHDADADVLL 365
Cdd:PLN02860   30 NRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN-------YRWSFEEAKSAMLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  366 VQHHLknsLAFDGPV--------------------IDLNDEASYHADCSLLSP------VAGHSHLAY---------VIY 410
Cdd:PLN02860  103 VRPVM---LVTDETCsswyeelqndrlpslmwqvfLESPSSSVFIFLNSFLTTemlkqrALGTTELDYawapddavlICF 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  411 TSGTTGKPKGVMVEHGG-IVNSLQwKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKETFaiqNA 489
Cdd:PLN02860  180 TSGTTGRPKGVTISHSAlIVQSLA-KIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAAL---QA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  490 IKQERITHFSTSPRLLKTMIE----QMNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVSTFHPV 565
Cdd:PLN02860  256 IKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTL 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  566 QSADEQITIGSPVANHQAYILGAHH-------------QIQpIGIPGELYVG-----GAGVARGYLNRPELTEEKfvehl 627
Cdd:PLN02860  336 HDPTLESPKQTLQTVNQTKSSSVHQpqgvcvgkpaphvELK-IGLDESSRVGriltrGPHVMLGYWGQNSETASV----- 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  628 hVPGQKMYKTGDLArWLPD-GRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDA-------------D 693
Cdd:PLN02860  410 -LSNDGWLDTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSrltemvvacvrlrD 487
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  694 GAKQLYAY---YVGEPSLTAAQFREELSRE-LPNYMIPSRFIPLER-IPLTSNGKI 744
Cdd:PLN02860  488 GWIWSDNEkenAKKNLTLSSETLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKI 543
PLN02479 PLN02479
acetate-CoA ligase
410-744 2.44e-15

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 82.97  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  410 YTSGTTGKPKGVMVEHGG-----IVNSLQWKKaffkhsPADRVlvlYPYVFDAFILN---FFGPL--ISGATLHLlpneE 479
Cdd:PLN02479  202 YTSGTTASPKGVVLHHRGaylmaLSNALIWGM------NEGAV---YLWTLPMFHCNgwcFTWTLaaLCGTNICL----R 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  480 NKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFI---HVQHVVVGGEqleTDTVEKLHSLQPR-IRINNEYGPTE 555
Cdd:PLN02479  269 QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILplpRVVHVMTAGA---APPPSVLFAMSEKgFRVTHTYGLSE 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  556 N---SVVSTFHPvqSADEQitigsPVANhQAYiLGAHHQIQPIG--------------IP------GELYVGGAGVARGY 612
Cdd:PLN02479  346 TygpSTVCAWKP--EWDSL-----PPEE-QAR-LNARQGVRYIGlegldvvdtktmkpVPadgktmGEIVMRGNMVMKGY 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  613 LNRPELTEEKFvehlhvpGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDA 692
Cdd:PLN02479  417 LKNPKANEEAF-------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDE 489
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876  693 DGAKQLYAYYVGEPSLTA---AQFREELSR----ELPNYMIPSR--FIPLeriPLTSNGKI 744
Cdd:PLN02479  490 RWGESPCAFVTLKPGVDKsdeAALAEDIMKfcreRLPAYWVPKSvvFGPL---PKTATGKI 547
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1799-2261 2.59e-15

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 82.91  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1799 QLTYGELNKRANRLARTLRAK-GVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLM 1877
Cdd:PRK05620   38 QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1878 QRDVRKQLA--------YEGVTVLLDDES--------------SYHQ--DGSDLA---PISDVSHLAYVIYTSGSTGRPK 1930
Cdd:PRK05620  118 DPRLAEQLGeilkecpcVRAVVFIGPSDAdsaaahmpegikvySYEAllDGRSTVydwPELDETTAAAICYSTGTTGAPK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1931 GVLIEHGGLtnyiwWAKEVYVKGEKA-------NF----PLYSSISFDLTVTSIFTplvtgNAIIVYDGEDKTA-LLESI 1998
Cdd:PRK05620  198 GVVYSHRSL-----YLQSLSLRTTDSlavthgeSFlccvPIYHVLSWGVPLAAFMS-----GTPLVFPGPDLSApTLAKI 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1999 VRD--PRVdiikltpAH--------LQVLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEgrIEICNEYGPTETVVG 2068
Cdd:PRK05620  268 IATamPRV-------AHgvptlwiqLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYG--VDVVHVWGMTETSPV 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2069 CMIYRYDA-----AKDR-RESVPIGTAAANTSIyVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELT----AEKFVDD 2138
Cdd:PRK05620  339 GTVARPPSgvsgeARWAyRVSQGRFPASLEYRI-VNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaASTFRGE 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2139 PFEPGAKMY------KTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQ-EEVIKEAVVTAREDVHGFKQLC 2211
Cdd:PRK05620  418 DVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAaPEVVECAVIGYPDDKWGERPLA 497
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2212 AYYVSGG----QTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK05620  498 VTVLAPGieptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PRK08315 PRK08315
AMP-binding domain protein; Validated
4333-4813 2.60e-15

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 82.94  E-value: 2.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4333 TIHQLFEQQAERNPDHEAVMFGNQTL--TYRQLNERSNQLARVLQ----DKGactdqvvavltDRsahmiIGI------- 4399
Cdd:PRK08315   17 TIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLalgiEKG-----------DR-----VGIwapnvpe 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4400 -----LAILKAGAAFLPIDP-----ELpekrrAFMLKDSGADVLLTCAGH-----------AIPPLFEGE---------- 4448
Cdd:PRK08315   81 wvltqFATAKIGAILVTINPayrlsEL-----EYALNQSGCKALIAADGFkdsdyvamlyeLAPELATCEpgqlqsarlp 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4449 ----VLLLDDP----------LLYQGRTDNL--------NLSCseNDLMYVIYTSGTTGQPKGVQLEHKtmtNLL--AY- 4503
Cdd:PRK08315  156 elrrVIFLGDEkhpgmlnfdeLLALGRAVDDaelaarqaTLDP--DDPINIQYTSGTTGFPKGATLTHR---NILnnGYf 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4504 --------EQD---------HTqlrFDRVLqfAAMSfdvcyqemfsALSSGGILFIIGNeakrdirqlndfvrthgiqtA 4566
Cdd:PRK08315  231 igeamkltEEDrlcipvplyHC---FGMVL--GNLA----------CVTHGATMVYPGE--------------------G 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4567 FLPTAFLKLLASEK---HYFEP--F-AEcVDHI-------------IAAGeqliAT-------RMLRDMLARhQVTLHnh 4620
Cdd:PRK08315  276 FDPLATLAAVEEERctaLYGVPtmFiAE-LDHPdfarfdlsslrtgIMAG----SPcpievmkRVIDKMHMS-EVTIA-- 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4621 YGPSETH-VVTMYTVDPDTDQELQPIGKPISNTEIFILN-EAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphp 4698
Cdd:PRK08315  348 YGMTETSpVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI---- 423
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4699 yDSNQRMYkTGDLARYLPEGNIEYAGRrdhqVK---IRG----Y-RvelgEVEAALLKH-----VQ----------EAV- 4754
Cdd:PRK08315  424 -DADGWMH-TGDLAVMDEEGYVNIVGR----IKdmiIRGgeniYpR----EIEEFLYTHpkiqdVQvvgvpdekygEEVc 493
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 4755 --VLAKENtdgqsdlyayftaeQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:PRK08315  494 awIILRPG--------------ATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
4331-4495 2.64e-15

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 83.00  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4331 PTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFL 4410
Cdd:PRK08279   36 KRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4411 PIDPELPEKRRAFMLKDSGADVLLT---CAGH--AIPPLFEGEVLL-------LDDPLLYQGRTDNLNLSCSEN------ 4472
Cdd:PRK08279  116 LLNTQQRGAVLAHSLNLVDAKHLIVgeeLVEAfeEARADLARPPRLwvaggdtLDDPEGYEDLAAAAAGAPTTNpasrsg 195
                         170       180
                  ....*....|....*....|....*..
gi 166797876 4473 ----DLMYVIYTSGTTGQPKGVQLEHK 4495
Cdd:PRK08279  196 vtakDTAFYIYTSGTTGLPKAAVMSHM 222
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
3302-3781 2.72e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 82.64  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3302 VVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSI 3381
Cdd:PRK08276    5 MAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3382 SVLLYCGKLQDdigfsgTCIDLMEE------HFYHEK-DSSLALSYQ---SSQLAYAI----------YTSGTTGKPKGT 3441
Cdd:PRK08276   85 KVLIVSAALAD------TAAELAAElpagvpLLLVVAgPVPGFRSYEealAAQPDTPIadetagadmlYSSGTTGRPKGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3442 LIE--HRQVIHLIEGLSRQV-YSAYDAELNIAML-APYY------FDASVQQMyasllsGHTLFIVPKeivSDGAALCRY 3511
Cdd:PRK08276  159 KRPlpGLDPDEAPGMMLALLgFGMYGGPDSVYLSpAPLYhtaplrFGMSALAL------GGTVVVMEK---FDAEEALAL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3512 YRQHSIDITDGTPAHLKLLIAAGDlqgvtlqhlliggEALSKTTVNKLKqlFGEHGAAP-------------G--ITNVY 3576
Cdd:PRK08276  230 IERYRVTHSQLVPTMFVRMLKLPE-------------EVRARYDVSSLR--VAIHAAAPcpvevkramidwwGpiIHEYY 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3577 GPTEtcvdASLFNIeCSSDAWARSQNYVpiGKP-LGRNRmyILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKF 3655
Cdd:PRK08276  295 ASSE----GGGVTV-ITSEDWLAHPGSV--GKAvLGEVR--ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAAR 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3656 VADPFVPedrmyrTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdaddeyylCGYF- 3734
Cdd:PRK08276  366 NPHGWVT------VGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVAD---------------VAVFg 424
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 3735 -------------------AADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK08276  425 vpdeemgervkavvqpadgADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
PLN02246 PLN02246
4-coumarate--CoA ligase
289-752 3.64e-15

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 82.34  E-value: 3.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEY-PKE----------------- 350
Cdd:PLN02246   51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYtPAEiakqakasgakliitqs 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  351 ----RLQYLLHDADADVLLVQHHLKNSLAFdGPVIDLNDEASYHADCSLLSPVAghshlayVIYTSGTTGKPKGVMVEHG 426
Cdd:PLN02246  131 cyvdKLKGLAEDDGVTVVTIDDPPEGCLHF-SELTQADENELPEVEISPDDVVA-------LPYSSGTTGLPKGVMLTHK 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  427 GIVNSLQWK------KAFFKhsPADRVLVLYPyVFDAFILN--FFGPLISGATLHLLPneeNKETFAIQNAIKQERITHF 498
Cdd:PLN02246  203 GLVTSVAQQvdgenpNLYFH--SDDVILCVLP-MFHIYSLNsvLLCGLRVGAAILIMP---KFEIGALLELIQRHKVTIA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  499 STSPRLLKTMIEQ--MNREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSvvstfhPVQS-----ADEQ 571
Cdd:PLN02246  277 PFVPPIVLAIAKSpvVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAG------PVLAmclafAKEP 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  572 ITI-----GSPVANHQAYIL----GAHhqiQPIGIPGELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGDL 640
Cdd:PLN02246  351 FPVksgscGTVVRNAELKIVdpetGAS---LPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDgwLH--------TGDI 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  641 ARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEPS--LTAAQFREELS 718
Cdd:PLN02246  420 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGseITEDEIKQFVA 499
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 166797876  719 RELPNYMIPSRFIPLERIPLTSNGKI---DLKALPAA 752
Cdd:PLN02246  500 KQVVFYKRIHKVFFVDSIPKAPSGKIlrkDLRAKLAA 536
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4833-4907 3.72e-15

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 73.35  E-value: 3.72e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4833 APRTNMEEQLICIWQDVLKVK--EIGVKDNFF-DLGGHSLRGMTLIAKIHKQFSKNISLREVFQCPTVGEMAQAIAEA 4907
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
3310-3714 5.82e-15

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 81.88  E-value: 5.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3310 TYEELNRRANQLARTLQAKGV--QADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLyC 3387
Cdd:cd05927     7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF-C 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3388 gklQDDIGFSgTCIDLME-------EHFYHEKDSslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVY 3460
Cdd:cd05927    86 ---DAGVKVY-SLEEFEKlgkknkvPPPPPKPED----------LATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3461 SAYDAELNIAMLA----PYYFDASVQ-QMYAS-----LLSGHtlfivPKEIVSDGAAL------------CRYY-RQHSI 3517
Cdd:cd05927   152 ILNKINPTDVYISylplAHIFERVVEaLFLYHgakigFYSGD-----IRLLLDDIKALkptvfpgvprvlNRIYdKIFNK 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3518 DITDGTPAHlKLLIAAGDLQgvtLQHLLIGGEALS----KTTVNKLKQLFGEH------GAAPGITNV------------ 3575
Cdd:cd05927   227 VQAKGPLKR-KLFNFALNYK---LAELRSGVVRASpfwdKLVFNKIKQALGGNvrlmltGSAPLSPEVleflrvalgcpv 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3576 ---YGPTETCVDASLfniecsSDAWARSQNYVpiGKPLGRNRMYILD------SKKRLQPKGvqgELYIAGDGVGRGYLN 3646
Cdd:cd05927   303 legYGQTECTAGATL------TLPGDTSVGHV--GGPLPCAEVKLVDvpemnyDAKDPNPRG---EVCIRGPNVFSGYYK 371
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 3647 LPELTDEKFvadpfvPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKI-QGFRIELGEIESVMLNVPDIQ 3714
Cdd:cd05927   372 DPEKTAEAL------DEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVA 434
PRK07867 PRK07867
acyl-CoA synthetase; Validated
260-744 5.96e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 81.65  E-value: 5.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  260 SGSRTVYQLFEEQAErtPENAAVKFKNDHLTYRELNEKASRLARTLRncGVQPDTL---VAILADRSLEMIVSIIAVWKA 336
Cdd:PRK07867    2 SSAPTVAELLLPLAE--DDDRGLYFEDSFTSWREHIRGSAARAAALR--ARLDPTRpphVGVLLDNTPEFSLLLGAAALS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  337 GGAYVPLDPEYPKERLQYLLHDADADVLLV---QHHLKNSLAFDGPVIDLN-----DEASYHADCSLLSPVAGHSHLAYV 408
Cdd:PRK07867   78 GIVPVGLNPTRRGAALARDIAHADCQLVLTesaHAELLDGLDPGVRVINVDspawaDELAAHRDAEPPFRVADPDDLFML 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  409 IYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGP-LISGATLHLlpneenKETFAIQ 487
Cdd:PRK07867  158 IFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIAL------RRKFSAS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  488 NAIKQER---ITHFSTSPRLLKTMIEQMNR-EDFIHVQHVVVGGEQLETDTVEklhsLQPR--IRINNEYGPTENSVVST 561
Cdd:PRK07867  232 GFLPDVRrygATYANYVGKPLSYVLATPERpDDADNPLRIVYGNEGAPGDIAR----FARRfgCVVVDGFGSTEGGVAIT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  562 FHPVQSAD------EQITI-----GSPVANHQAYILGAHHQIQPIGipgELY-VGGAGVARGYLNRPELTEEKFVEhlhv 629
Cdd:PRK07867  308 RTPDTPPGalgplpPGVAIvdpdtGTECPPAEDADGRLLNADEAIG---ELVnTAGPGGFEGYYNDPEADAERMRG---- 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  630 pgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--S 707
Cdd:PRK07867  381 ---GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPgaK 457
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876  708 LTAAQFREELS--RELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK07867  458 FDPDAFAEFLAaqPDLGPKQWPSYVRVCAELPRTATFKV 496
PRK07470 PRK07470
acyl-CoA synthetase; Validated
3293-3788 6.10e-15

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 81.63  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERI 3372
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3373 RYILNDSSISVLLYCGKLQDDI-GFSGTCIDLmeEHFYHEKDSSLALSYQSSQLAYA-----------------IYTSGT 3434
Cdd:PRK07470   97 AYLAEASGARAMICHADFPEHAaAVRAASPDL--THVVAIGGARAGLDYEALVARHLgarvanaavdhddpcwfFFTSGT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3435 TGKPKGTLIEHRQ---VI--H---LIEGLSRQvysayDAELniaMLAPYYFDASVQQMyASLLSGHTLFIVPKEIVsDGA 3506
Cdd:PRK07470  175 TGRPKAAVLTHGQmafVItnHladLMPGTTEQ-----DASL---VVAPLSHGAGIHQL-CQVARGAATVLLPSERF-DPA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3507 ALCRYYRQHSIDITDGTPAHLKLLI---AAGDLQGVTLQHLLIGG---------EALSKTTvNKLKQLFGehgaapgITN 3574
Cdd:PRK07470  245 EVWALVERHRVTNLFTVPTILKMLVehpAVDRYDHSSLRYVIYAGapmyradqkRALAKLG-KVLVQYFG-------LGE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3575 VYGpTETCVDASLFNIECSSDAwarsqnyvPIGkPLGRNR----MYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPEL 3650
Cdd:PRK07470  317 VTG-NITVLPPALHDAEDGPDA--------RIG-TCGFERtgmeVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEA 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3651 TDEKFVadpfvpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDAD-DEYY 3729
Cdd:PRK07470  387 NAKAFR-------DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwGEVG 459
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3730 LCGYFAAD-KTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKKR 3788
Cdd:PRK07470  460 VAVCVARDgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
PLN02479 PLN02479
acetate-CoA ligase
1788-2281 6.87e-15

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 81.81  E-value: 6.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1788 PDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYML 1867
Cdd:PLN02479   34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1868 DDSQAGIVLMQRDVRkQLAYEGVTVLLD-DESSYHQdgSDLAPISDVS----HLAYVI---------------------- 1920
Cdd:PLN02479  114 EHSKSEVVMVDQEFF-TLAEEALKILAEkKKSSFKP--PLLIVIGDPTcdpkSLQYALgkgaieyekfletgdpefawkp 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1921 -----------YTSGSTGRPKGVLIEHGG-----LTNYIWWAKE---VYVkgekANFPL-------YSSISFDLTVTSIF 1974
Cdd:PLN02479  191 padewqsialgYTSGTTASPKGVVLHHRGaylmaLSNALIWGMNegaVYL----WTLPMfhcngwcFTWTLAALCGTNIC 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1975 TPLVTGNAI---IVYDGEDK----TALLESIVRDPRVDIIKLTPAHLQVlkemniadqtavrrMIVGGENLSTRLARSIH 2047
Cdd:PLN02479  267 LRQVTAKAIysaIANYGVTHfcaaPVVLNTIVNAPKSETILPLPRVVHV--------------MTAGAAPPPSVLFAMSE 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2048 EQFEgrieICNEYGPTETVVGCMIYrydAAKDRRESVPIGTAA---ANTSI-YV----LD----ENMKPAPI--GVPGEI 2113
Cdd:PLN02479  333 KGFR----VTHTYGLSETYGPSTVC---AWKPEWDSLPPEEQArlnARQGVrYIglegLDvvdtKTMKPVPAdgKTMGEI 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2114 YISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVI 2193
Cdd:PLN02479  406 VMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2194 KEAVVTAREDVHGFKQLCAYYV-------SGGQTTAARLRKQLSQTLASYMVPAYFIeLDEMPLTSNGKINKKglpapdf 2266
Cdd:PLN02479  479 LEASVVARPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKH------- 550
                         570
                  ....*....|....*
gi 166797876 2267 ELQDRAEYKAPRTKA 2281
Cdd:PLN02479  551 VLRAKAKEMGPVKKS 565
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
4334-4818 7.09e-15

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 81.77  E-value: 7.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4334 IHQLFEQQAERNPDHEAVMFGNQ-----TLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAA 4408
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4409 FLPIDPELPEKRRAFMLKDSGADVLLTCAGHA-----IPPLFEGEVLLLDDP--------------------------LL 4457
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTrrgreVNLKEEADKACAQCPtvekvvvvrhlgndftpakgrdlsydEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4458 YQGRTDNLNLSCSENDLMyVIYTSGTTGQPKGVQleHKTMTNLLAYEQDhTQLRFD-----RVLQFAAMSFDVCYQEMFS 4532
Cdd:cd05968   223 KETAGDGAERTESEDPLM-IIYTSGTTGKPKGTV--HVHAGFPLKAAQD-MYFQFDlkpgdLLTWFTDLGWMMGPWLIFG 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4533 ALSSGGILFII-GNEAKRDIRQLNDFVRTHGIQ----TAFLPTAF---------------LKLLAS--EKHYFEPFAECV 4590
Cdd:cd05968   299 GLILGATMVLYdGAPDHPKADRLWRMVEDHEIThlglSPTLIRALkprgdapvnahdlssLRVLGStgEPWNPEPWNWLF 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4591 DHIIAAGEQLIatrmlrdmlarhqvtlhNHYGPSETH--VVTMYTVDPdtdqeLQPIG--KPISNTEIFILNEAGtlQPV 4666
Cdd:cd05968   379 ETVGKGRNPII-----------------NYSGGTEISggILGNVLIKP-----IKPSSfnGPVPGMKADVLDESG--KPA 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4667 -GIVGELCISG--VSLARGYHNRESLTLETFvphpYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVE 4743
Cdd:cd05968   435 rPEVGELVLLApwPGMTRGFWRDEDRYLETY----WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIE 510
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4744 AALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQ-LKEKLAGQIPGYM----IPSYFIQLEKLPLTGNGKVNRR 4816
Cdd:cd05968   511 SVLNAHpaVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEaLAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRR 590

                  ..
gi 166797876 4817 AL 4818
Cdd:cd05968   591 VI 592
PRK08308 PRK08308
acyl-CoA synthetase; Validated
4352-4823 7.67e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 80.47  E-value: 7.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4352 MF--GNQTLTYRQLNERSNQLARVLQDKgACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSG 4429
Cdd:PRK08308    1 MLivNDEEYSKSDFDLRLQRYEEMEQFQ-EAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4430 ADVLLTcaGHAIPPLFEGEVLLLDDPLLYQgrtdnlnlscsendlmyviYTSGTTGQPK-------GVQLEHKTMTNLLA 4502
Cdd:PRK08308   80 CHGLLY--GESDFTKLEAVNYLAEEPSLLQ-------------------YSSGTTGEPKlirrswtEIDREIEAYNEALN 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4503 YEQDHTQLrfdrVLQFAAMSFD-VCyqEMFSALSSGGILFIIGNEAKRDIRQLNDFVRTHGIQTAflPtAFLKLLASekh 4581
Cdd:PRK08308  139 CEQDETPI----VACPVTHSYGlIC--GVLAALTRGSKPVIITNKNPKFALNILRNTPQHILYAV--P-LMLHILGR--- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4582 yFEPFAECVDHIIAAG----EQLIATrmLRDMLARhqvtLHNHYGPSETHVVTMytvDPDTDQELQpIGKPISNTEIfil 4657
Cdd:PRK08308  207 -LLPGTFQFHAVMTSGtplpEAWFYK--LRERTTY----MMQQYGCSEAGCVSI---CPDMKSHLD-LGNPLPHVSV--- 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4658 nEAGTL--QPVGIVGELcisgvslargyhnresltletfvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGY 4735
Cdd:PRK08308  273 -SAGSDenAPEEIVVKM-----------------------------GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGL 322
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4736 RVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:PRK08308  323 NVYPIEVEDVMLRLpgVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
                         490
                  ....*....|
gi 166797876 4814 NRRALPMPEA 4823
Cdd:PRK08308  403 SRKLLELGEV 412
PRK12467 PRK12467
peptide synthase; Provisional
858-1282 9.19e-15

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 82.52  E-value: 9.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  858 WFFEQKMPHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKTPDGYAPRITGTDESELFHLEVMNYKGETD 937
Cdd:PRK12467   60 WFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDLANEQGRAR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  938 PAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQTIQLP----Q 1012
Cdd:PRK12467  140 ESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHvLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPalpiQ 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1013 KTDsFPFWadQLSKYAAeTDMEEEIAYWTE--------LSSIKPQPLPKDTISEGSLLRdseevtIQWTKEETEQLLKQA 1084
Cdd:PRK12467  220 YAD-YAIW--QRSWLEA-GERERQLAYWQEqlggehtvLELPTDRPRPAVPSYRGARLR------VDLPQALSAGLKALA 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1085 NRaYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIipdaDISRTIGWFTSQYpvVLRMEAGKNLSqrikiVKEG 1164
Cdd:PRK12467  290 QR-EGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV----ETERLIGFFVNTQ--VLKAEVDPQAS-----FLEL 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1165 LRRIPDKGMNYSIIKYISGHPEADSLQLKPEISFNYLGQ--FDQDLKHQALRISPFS--TGLSMNE--NQERTAVLDL-- 1236
Cdd:PRK12467  358 LQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQvmFNHQNTATGGRDREGAqlPGLTVEElsWARHTAQFDLal 437
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876 1237 NGMIAEGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIAHCVSR 1282
Cdd:PRK12467  438 DTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR 483
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3309-3715 9.69e-15

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 80.30  E-value: 9.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3309 FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLP----IDPDSPSERIryilndssisvl 3384
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRV------------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3385 lycgklqdDIGFSGTCIdlmEEHFYHEKDSSLALsyqssqlayaiYTSGTTGKPKgtLIEHRQVIHLIEGLSRQVYSAY- 3463
Cdd:cd05974    69 --------DRGGAVYAA---VDENTHADDPMLLY-----------FTSGTTSKPK--LVEHTHRSYPVGHLSTMYWIGLk 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3464 --DAELNIAmlAPYYFDASVQQMYASLLSGHTLFIVpKEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAgDLQG--V 3539
Cdd:cd05974   125 pgDVHWNIS--SPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ-DLASfdV 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3540 TLQHLLIGGEALSKTTVNKLKQLFGEhgaapGITNVYGPTETCVDASlfNiecssdawARSQNYVP--IGKPLGRNRMYI 3617
Cdd:cd05974   201 KLREVVGAGEPLNPEVIEQVRRAWGL-----TIRDGYGQTETTALVG--N--------SPGQPVKAgsMGRPLPGYRVAL 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3618 LDSKKRlqpKGVQGELYIA-GD----GVGRGYLNLPELTDEkfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVK 3692
Cdd:cd05974   266 LDPDGA---PATEGEVALDlGDtrpvGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
                         410       420
                  ....*....|....*....|...
gi 166797876 3693 IQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05974   336 SSDYRISPFELESVLIEHPAVAE 358
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
2829-3143 1.18e-14

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 79.54  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2829 PLTPMQKGMLFHSLLDEASSSY---FeqaSFDLQGELKIDWFKASLERLFETYAVLRTRFYSGwnDTPLQIVYKTQTPQI 2905
Cdd:cd19537     3 ALSPIEREWWHKYQLSTGTSSFnvsF---ACRLSGDVDRDRLASAWNTVLARHRILRSRYVPR--DGGLRRSYSSSPPRV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2906 HFADLRDIEEHLRedaiaayqREdkakgFDLARDPLMRIAIfrMEDrkyHLIWSFHHIVMDGWCLSLITKEVFDHYSalq 2985
Cdd:cd19537    78 QRVDTLDVWKEIN--------RP-----FDLEREDPIRVFI--SPD---TLLVVMSHIICDLTTLQLLLREVSAAYN--- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2986 eGREPEPlSAVPYSDYIEWLDRQDQGAAKrYWSGYLEGYKGetTLLHKiaQHEQKEYAYANLICRFDHEQTKQLQQIANQ 3065
Cdd:cd19537   137 -GKLLPP-VRREYLDSTAWSRPASPEDLD-FWSEYLSGLPL--LNLPR--RTSSKSYRGTSRVFQLPGSLYRSLLQFSTS 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3066 HQVTLNTLIQTLWGVLLQKYSGSADVVFGSVVSGRPAEipDVEQMIGLFINTIPVRIR--CDEDSTFADTMQMVQ---QN 3140
Cdd:cd19537   210 SGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGLFLEPLPIRIRfpSSSDASAADFLRAVRrssQA 287

                  ...
gi 166797876 3141 ALA 3143
Cdd:cd19537   288 ALA 290
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
4334-4818 1.23e-14

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 80.70  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4334 IHQLFEQQAERNPDHEAVMFGNQ--TLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLP 4411
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4412 IDPELPEKRRAFMLKDSGADVLLTCA----GHAIP--PLFEGEVLLLDD-------PLLYQGRTDNLNLSCS------EN 4472
Cdd:PRK05852   98 LDPALPIAEQRVRSQAAGARVVLIDAdgphDRAEPttRWWPLTVNVGGDsgpsggtLSVHLDAATEPTPATStpeglrPD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 DLMyVIYTSGTTGQPKGVQLEHKTMTN-----LLAYE---QDHTqlrfdrvlqFAAMSFdvcYQ------EMFSALSSGG 4538
Cdd:PRK05852  178 DAM-IMFTGGTTGLPKMVPWTHANIASsvraiITGYRlspRDAT---------VAVMPL---YHghgliaALLATLASGG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4539 ILFIIGnEAKRDIRQLNDFVRTHGIQ--TAfLPTA---FLKLLASEKHYFEPFA-----ECVDHIIAAGEQLIATRMLRD 4608
Cdd:PRK05852  245 AVLLPA-RGRFSAHTFWDDIKAVGATwyTA-VPTIhqiLLERAATEPSGRKPAAlrfirSCSAPLTAETAQALQTEFAAP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4609 ML-------ARHQVTLHNHYGPSETHVVTMYTvdpdtdqelQPIGKPiSNTEIFILNEAGTLQPVGIVGELCISGVSLAR 4681
Cdd:PRK05852  323 VVcafgmteATHQVTTTQIEGIGQTENPVVST---------GLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVR 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4682 GYHNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKE 4759
Cdd:PRK05852  393 GYLGDPTITAANFT-------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHpnVMEAAVFGVP 465
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 4760 NTdgqsdLY-------------AYFTAEQSLSisQLKEKLAGqipgYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK05852  466 DQ-----LYgeavaavivpresAPPTAEELVQ--FCRERLAA----FEIPASFQEASGLPHTAKGSLDRRAV 526
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
4342-4815 1.48e-14

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 80.62  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFGN-----QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPEL 4416
Cdd:cd05970    27 AKEYPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4417 PEKRRAFMLKDSGADVLLTCAGHAIPPLFEG-------------------------EVLLLDDPLLYQGRTDNlNLSCSE 4471
Cdd:cd05970   107 TAKDIVYRIESADIKMIVAIAEDNIPEEIEKaapecpskpklvwvgdpvpegwidfRKLIKNASPDFERPTAN-SYPCGE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4472 nDLMYVIYTSGTTGQPKGVQLEHK-TMTNLLAYEQDHTQLRFDRVLQFAAMSFDVC-YQEMFSALSSGGILFIIGNEaKR 4549
Cdd:cd05970   186 -DILLVYFSSGTTGMPKMVEHDFTyPLGHIVTAKYWQNVREGGLHLTVADTGWGKAvWGKIYGQWIAGAAVFVYDYD-KF 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4550 DIRQLNDFVRTHGIQTAFLPTAFLKLLASEK--HY-FEPFAECVdhiiAAGEQLiATRMLRDMLARHQVTLHNHYGPSET 4626
Cdd:cd05970   264 DPKALLEKLSKYGVTTFCAPPTIYRFLIREDlsRYdLSSLRYCT----TAGEAL-NPEVFNTFKEKTGIKLMEGFGQTET 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4627 hVVTMYTVdPDTDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCIS-----GVSLARGYHNRESLTLETFvphpYDS 4701
Cdd:cd05970   339 -TLTIATF-PWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTAEVW----HDG 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4702 nqrMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVLAKENTDGQS-----DLYAYFTA 4773
Cdd:cd05970   413 ---YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHpavLECAVTGVPDPIRGQVvkatiVLAKGYEP 489
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 166797876 4774 EQSLsISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd05970   490 SEEL-KKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
PRK13382 PRK13382
bile acid CoA ligase;
3288-3784 1.51e-14

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 80.57  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3288 LFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDS 3367
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3368 PSERIRYILNDSSISVLLYCGKLQD--DIGFSGTCIDLMEEHFYHEKDSSLALSYQSSQLAYA-----------IYTSGT 3434
Cdd:PRK13382  128 AGPALAEVVTREGVDTVIYDEEFSAtvDRALADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRpeptgrkgrviLLTSGT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3435 TGKPKGTL-IEHRQVIHLIEGLSRqvySAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDGAALCRYYR 3513
Cdd:PRK13382  208 TGTPKGARrSGPGGIGTLKAILDR---TPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHR 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3514 QHSIDITdgtPAHLKLLIAAGD-----LQGVTLQHLLIGGEALSKTTVNKLKQLFGehgaaPGITNVYGPTEtcvdASLF 3588
Cdd:PRK13382  285 ATGLAVV---PVMFDRIMDLPAevrnrYSGRSLRFAAASGSRMRPDVVIAFMDQFG-----DVIYNNYNATE----AGMI 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3589 NIECSSDAWARSQNyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLpelTDEKFvadpfvpEDRMYR 3668
Cdd:PRK13382  353 ATATPADLRAAPDT---AGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDF-------HDGFMA 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3669 TGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGY--FAADKTIQISELR 3746
Cdd:PRK13382  420 SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFvvLKPGASATPETLK 499
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 166797876 3747 KRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAP 3784
Cdd:PRK13382  500 QHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
269-451 1.96e-14

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 80.30  E-value: 1.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  269 FEEQAERTPENAAVKFKNDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYP 348
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  349 KERLQYLLHDADADVLLVQHHL-------KNSLAFDGPVIDLNDEASYH-------ADCSLLSPVAGHSH--------LA 406
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELveafeeaRADLARPPRLWVAGGDTLDDpegyedlAAAAAGAPTTNPASrsgvtakdTA 202
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876  407 YVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRV---LVLY 451
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLyccLPLY 250
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
3272-3715 2.40e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 79.82  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3272 FQSNDMHYPREKTIHELFEeqahrtPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQA-DQLVGIMTERSlEMVVGI 3350
Cdd:PRK07786   12 YLARRQNWVNQLARHALMQ------PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3351 LGVLKAGGAYLPIDPD-SPSErIRYILNDSSISVLLYCGKLQD----------------DIGFSGTCIDLMEEHFYHEKD 3413
Cdd:PRK07786   85 LAANMLGAIAVPVNFRlTPPE-IAFLVSDCGAHVVVTEAALAPvatavrdivpllstvvVAGGSSDDSVLGYEDLLAEAG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3414 SSLALSYQSSQLAYAI-YTSGTTGKPKGTLIEHR----QVIHLIEGlsrqvySAYDAELNIAMLA-PYYFDASVQQMYAS 3487
Cdd:PRK07786  164 PAHAPVDIPNDSPALImYTSGTTGRPKGAVLTHAnltgQAMTCLRT------NGADINSDVGFVGvPLFHIAGIGSMLPG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3488 LLSGHTLFIVPKEIVSDGAALCRYYRQHSIDITdGTPAHLKLLIAAGDLQG--VTLQHLLIGGEALSKTTVNKLKQLFge 3565
Cdd:PRK07786  238 LLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIF-LVPAQWQAVCAEQQARPrdLALRVLSWGAAPASDTLLRQMAATF-- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3566 hgaaPG--ITNVYGPTE----TCV----DAslfniecssdawARSQNYVpiGKPLGRNRMYILDSKKRLQPKGVQGELYI 3635
Cdd:PRK07786  315 ----PEaqILAAFGQTEmspvTCMllgeDA------------IRKLGSV--GKVIPTVAARVVDENMNDVPVGEVGEIVY 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3636 AGDGVGRGYLNLPELTDEKFVADPFvpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:PRK07786  377 RAPTLMSGYWNNPEATAEAFAGGWF-------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVE 449
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
406-749 3.08e-14

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 77.78  E-value: 3.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  406 AYVIYTSGTTGKPKGVMVEHGGIVNSL-----------QWKKAFFKHSPAD-RVLVLypyvfdafilnffgPLISGAT-L 472
Cdd:PRK07824   38 ALVVATSGTTGTPKGAMLTAAALTASAdathdrlggpgQWLLALPAHHIAGlQVLVR--------------SVIAGSEpV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  473 HL-LPNEENKETFA-IQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLHSLqpRIRINNE 550
Cdd:PRK07824  104 ELdVSAGFDPTALPrAVAELGGGRRYTSLVPMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAA--GINVVRT 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  551 YGPTEnsvvstfhpvqsadeqiTIGSPVANHQAyILGAHHQIqpigIPGELYVGGAGVARGYLNRPEltEEKFVEhlhvP 630
Cdd:PRK07824  182 YGMSE-----------------TSGGCVYDGVP-LDGVRVRV----EDGRIALGGPTLAKGYRNPVD--PDPFAE----P 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  631 GqkMYKTGDLARwLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGE--PSL 708
Cdd:PRK07824  234 G--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDggPAP 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 166797876  709 TAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK07824  311 TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2370-2675 3.13e-14

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 78.65  E-value: 3.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2370 WFFEQTTTDQHYYNQAVMLHApEG-FQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQnEEIAQSGLYRLEVMNLKEDP 2448
Cdd:cd19532    12 WFLQQYLEDPTTFNVTFSYRL-TGpLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPM-QGVLASSPLRLEHVQISDEA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2449 DpgrtIEAKADEIQSsmH---LSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIqlPQ 2524
Cdd:cd19532    90 E----VEEEFERLKN--HvydLESGETMRIVLLSLSPTEHyLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPP--LQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2525 KTDsfqlWAKRLSEYAQSETIKQEQEYWTKIEQTEVKPLP---------------KDFHETHTTaKDSETAAvewtkeet 2589
Cdd:cd19532   162 YLD----FAARQRQDYESGALDEDLAYWKSEFSTLPEPLPllpfakvksrppltrYDTHTAERR-LDAALAA-------- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2590 elLLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREqiiqDIDISRTVGWFTSLYPVVLHAQPGKEISDY 2669
Cdd:cd19532   229 --RIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRT----DEDFMETIGFFLNLLPLRFRRDPSQTFADV 302

                  ....*.
gi 166797876 2670 IKTTKE 2675
Cdd:cd19532   303 LKETRD 308
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
4331-4836 3.28e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 79.30  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4331 PTTIHQLFEQQAERnpDHEAVMFGNQTLTYRQ-LNERSNQ--LARVLQDKGACTDqvVAVLTDRSAHMIIGILAILKAGA 4407
Cdd:PRK13388    2 RDTIAQLLRDRAGD--DTIAVRYGDRTWTWREvLAEAAARaaALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4408 AFLPIDPElpeKRRAFMLKD-SGAD--VLLTCAGHAipPLFEG------EVLLLDDP----LLYQGRTDNLNLSCSENDL 4474
Cdd:PRK13388   78 VLVGLNTT---RRGAALAADiRRADcqLLVTDAEHR--PLLDGldlpgvRVLDVDTPayaeLVAAAGALTPHREVDAMDP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4475 MYVIYTSGTTGQPKGVQLEHKTMTnLLAYEQdhTQlRFDRVLQfaamsfDVCYQEM--FS----------ALSSGGILfi 4542
Cdd:PRK13388  153 FMLIFTSGTTGAPKAVRCSHGRLA-FAGRAL--TE-RFGLTRD------DVCYVSMplFHsnavmagwapAVASGAAV-- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4543 igneAKRDI----RQLNDfVRTHGIqTAFL----PTAFLklLASEKHyfepfAECVDHIIAAGEQLIAT-RMLRDMLARH 4613
Cdd:PRK13388  221 ----ALPAKfsasGFLDD-VRRYGA-TYFNyvgkPLAYI--LATPER-----PDDADNPLRVAFGNEASpRDIAEFSRRF 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4614 QVTLHNHYGPSETHVVTmyTVDPDTDQelQPIGKPISNTEIF-----------ILNEAGTL-QPVGIVGELC-ISGVSLA 4680
Cdd:PRK13388  288 GCQVEDGYGSSEGAVIV--VREPGTPP--GSIGRGAPGVAIYnpetltecavaRFDAHGALlNADEAIGELVnTAGAGFF 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4681 RGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLA- 4757
Cdd:PRK13388  364 EGYYNNPEATAERM-------RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHpaINRVAVYAv 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4758 -KENTDGQSDLYAYFTAEQSLSISQLKEKLAGQ--IPGYMIPSYFIQLEKLPLTGNGKVNRRALpmpeagLQTGTDYVAP 4834
Cdd:PRK13388  437 pDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL------IAQGWATGDP 510

                  ..
gi 166797876 4835 RT 4836
Cdd:PRK13388  511 VT 512
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
4344-4818 4.41e-14

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 78.88  E-value: 4.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4344 RNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAflPIDPELPEKR--- 4420
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRsel 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4421 RAFMLKDSGAdVLLTCAGHAippLFEGE---------------VLLLDDP-------LLYQGRTDNLNLSCSENDLMYVI 4478
Cdd:PRK10946  113 NAYASQIEPA-LLIADRQHA---LFSDDdflntlvaehsslrvVLLLNDDgehslddAINHPAEDFTATPSPADEVAFFQ 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4479 YTSGTTGQPKGVQLEHktmtNLLAYE--------QDHTQLRFDRVLQfAAMSFdvcyqemfsALSSGGIL--FIIGNEA- 4547
Cdd:PRK10946  189 LSGGSTGTPKLIPRTH----NDYYYSvrrsveicGFTPQTRYLCALP-AAHNY---------PMSSPGALgvFLAGGTVv 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4548 -KRDIRQLNDF--VRTHGIQ-TAFLPTAFLKLLAsekhyfepfaecvdHIIAAG--EQLIATRMLR-------DMLARhQ 4614
Cdd:PRK10946  255 lAPDPSATLCFplIEKHQVNvTALVPPAVSLWLQ--------------AIAEGGsrAQLASLKLLQvggarlsETLAR-R 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4615 VT------LHNHYGPSETHVvtMYT-VDPDTDQELQPIGKPIS-NTEIFILNEAGTLQPVGIVGELCISGVSLARGY--- 4683
Cdd:PRK10946  320 IPaelgcqLQQVFGMAEGLV--NYTrLDDSDERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYyks 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4684 --HNRESLTLETFvphpydsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVLAK 4758
Cdd:PRK10946  398 pqHNASAFDANGF-----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHpavIHAALVSME 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 4759 ENTDGQSDlYAYFTAEQSLSISQLKEKLAGQ-IPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK10946  467 DELMGEKS-CAFLVVKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
3298-3715 6.02e-14

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 78.78  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3298 DNTAVVFEGKQ----FTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIR 3373
Cdd:PRK04319   59 DKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3374 YILNDSSISVL-----LYCGKLQD-------------DIGFSGTCIDLMEEHFYHEKDSSLALSyQSSQLAYAIYTSGTT 3435
Cdd:PRK04319  139 DRLEDSEAKVLittpaLLERKPADdlpslkhvllvgeDVEEGPGTLDFNALMEQASDEFDIEWT-DREDGAILHYTSGST 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3436 GKPKGTLIEHRQVI-HLIEGlsRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKEIVSDgaalcRYYR- 3513
Cdd:PRK04319  218 GKPKGVLHVHNAMLqHYQTG--KYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRFSPE-----RWYRi 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3514 --QHSIDITDGTPAHLKLLIAAG-------DLQgvTLQHLLIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTET--- 3581
Cdd:PRK04319  291 leDYKVTVWYTAPTAIRMLMGAGddlvkkyDLS--SLRHILSVGEPLNPEVVRWGMKVFGLP-----IHDNWWMTETggi 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3582 ------CVDaslfnIECSSdawarsqnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGdgvG-----RGYLNLPEL 3650
Cdd:PRK04319  364 mianypAMD-----IKPGS-----------MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKK---GwpsmmRGIWNNPEK 424
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 3651 TDEKFVADpfvpedrMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:PRK04319  425 YESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAE 482
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
3282-3715 6.60e-14

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 78.19  E-value: 6.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3282 EKTIHELFEEQAHRTPDNTAVVFEG-----KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKA 3356
Cdd:PRK08008    6 GQHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3357 GGAYLPIDPDSPSERIRYILNDSSISVL--------LYCGKLQ-DDIGFSGTC-IDLMEEHFYHEKDSSLALSYQSSQLA 3426
Cdd:PRK08008   86 GAIMVPINARLLREESAWILQNSQASLLvtsaqfypMYRQIQQeDATPLRHIClTRVALPADDGVSSFTQLKAQQPATLC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3427 YA-----------IYTSGTTGKPKGTLIEHRQVihLIEGLsrqvYSAYDAELN-----IAMLAPYYFDASVQQMYASLLS 3490
Cdd:PRK08008  166 YApplstddtaeiLFTSGTTSRPKGVVITHYNL--RFAGY----YSAWQCALRdddvyLTVMPAFHIDCQCTAAMAAFSA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3491 GHTLFIVPKEIVSdgaalcRYYRQ---HSIDITDGTPAHLKLLIaagdLQGVT---LQHLL---IGGEALSKTTVNKLKQ 3561
Cdd:PRK08008  240 GATFVLLEKYSAR------AFWGQvckYRATITECIPMMIRTLM----VQPPSandRQHCLrevMFYLNLSDQEKDAFEE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3562 LFGEHgaapgITNVYGPTETCVDAslfniecSSDAWARSQNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYI---AGD 3638
Cdd:PRK08008  310 RFGVR-----LLTSYGMTETIVGI-------IGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGK 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3639 GVGRGYLNLPELTDEKFVADPFVpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:PRK08008  378 TIFKEYYLDPKATAKVLEADGWL------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQD 448
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
4332-4819 7.04e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 78.11  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4332 TTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLP 4411
Cdd:PRK13383   35 TNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4412 IDPELPEKRRAFMLKDSGADVLLTCAGHAIPPLFEGEVLLLDDPLLYQGRTDNLNLSCSENDLMyVIYTSGTTGQPKGVQ 4491
Cdd:PRK13383  115 ISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRI-VLLTSGTTGKPKGVP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4492 LEHKTMTNLLAYEQ--DHTQLRFDRVLQFAAmsfdvcyqEMFSALSSGGILFIIG----------NEAKRDIRQLNdFVR 4559
Cdd:PRK13383  194 RAPQLRSAVGVWVTilDRTRLRTGSRISVAM--------PMFHGLGLGMLMLTIAlggtvlthrhFDAEAALAQAS-LHR 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4560 THGIQTAFLPTAFLKLLASEKHYFEPFAeCVDHIIAAGEQLIATRMLRDMLARHQVtLHNHYGPSETHVVTMYTvDPDTD 4639
Cdd:PRK13383  265 ADAFTAVPVVLARILELPPRVRARNPLP-QLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALAT-PADLR 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4640 QELQPIGKPISNTEIFILNEAGtlQPVG--IVGELCISGVSLARGYHNRESLTLetfvphpYDSnqrMYKTGDLArYLPE 4717
Cdd:PRK13383  342 DAPETVGKPVAGCPVRILDRNN--RPVGprVTGRIFVGGELAGTRYTDGGGKAV-------VDG---MTSTGDMG-YLDN 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4718 -GNIEYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVLAKENTDGQSdLYAYFTAEQSLSI--SQLKEKLAGQIP 4791
Cdd:PRK13383  409 aGRLFIVGREDDMIISGGENVYPRAVENALAAHpavADNAVIGVPDERFGHR-LAAFVVLHPGSGVdaAQLRDYLKDRVS 487
                         490       500
                  ....*....|....*....|....*...
gi 166797876 4792 GYMIPSYFIQLEKLPLTGNGKVNRRALP 4819
Cdd:PRK13383  488 RFEQPRDINIVSSIPRNPTGKVLRKELP 515
PRK07638 PRK07638
acyl-CoA synthetase; Validated
3284-3790 7.97e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 77.90  E-value: 7.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQlVGIMTERSLEMVVGILGVLKAGGAYLPI 3363
Cdd:PRK07638    2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3364 DPD-SPSERIRYILNDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQSSQLA--YAIYTSGTTGKPKG 3440
Cdd:PRK07638   81 DIKwKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQNApfYMGFTSGSTGKPKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3441 TLIEHRQVIHLIEGLSRQVYSAYDAELNIA--MLAPYYFDASVQQMYAsllsGHTLFIVPKEIVSDgaaLCRYYRQHSID 3518
Cdd:PRK07638  161 FLRAQQSWLHSFDCNVHDFHMKREDSVLIAgtLVHSLFLYGAISTLYV----GQTVHLMRKFIPNQ---VLDKLETENIS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3519 ITDGTPAHLKLLIAAgdlQGVTLQHLLI--GGEALSKTTVNKLKQLFgehgaaPGIT--NVYGPTETCVDASLfniecSS 3594
Cdd:PRK07638  234 VMYTVPTMLESLYKE---NRVIENKMKIisSGAKWEAEAKEKIKNIF------PYAKlyEFYGASELSFVTAL-----VD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3595 DAWARSQNYVpiGKPLGRNRMYILDSK-KRLQPkGVQGELYIAGDGVGRGYLNLPELTDEkfvadpfVPEDRMYRTGDLA 3673
Cdd:PRK07638  300 EESERRPNSV--GRPFHNVQVRICNEAgEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE-------LNADGWMTVRDVG 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3674 RLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaAALKDADDEYY---LCGYFAADKTIQisELRKRMA 3750
Cdd:PRK07638  370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDE---IVVIGVPDSYWgekPVAIIKGSATKQ--QLKSFCL 444
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 166797876 3751 RHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAPVKKRDS 3790
Cdd:PRK07638  445 QRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
3319-3695 8.61e-14

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 78.24  E-value: 8.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3319 NQLARTLQAKGVQADQL------VGIMTERSLEMVVGILGVLKAGGAYLPI-DPDSP--SERIRYILNDSSISVLLYCGK 3389
Cdd:PRK12476   72 TQLGVRLRAVGARLQQVagpgdrVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTA 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3390 LQDDI-GFSGTCIDLMEEHFY--HEKDSSLALSYQSSQL-----AYAIYTSGTTGKPKGTLIEHR-------QVIHLIEG 3454
Cdd:PRK12476  152 AAEAVeGFLRNLPRLRRPRVIaiDAIPDSAGESFVPVELdtddvSHLQYTSGSTRPPVGVEITHRavgtnlvQMILSIDL 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3455 LSRQVYSaydaelnIAMLaPYYFDASVQQ-MYASLLSGHTLFIVPKEIVSDGAalcRYYRQHSIDITDG-----TP---- 3524
Cdd:PRK12476  232 LDRNTHG-------VSWL-PLYHDMGLSMiGFPAVYGGHSTLMSPTAFVRRPQ---RWIKALSEGSRTGrvvtaAPnfay 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3525 --AHLKLLIAAG---DLQGVTLqhlLIGGEALSKTTVNKLKQLFGEHGAAPgitNVYGPTETCVDASLFNIECSSDAWA- 3598
Cdd:PRK12476  301 ewAAQRGLPAEGddiDLSNVVL---IIGSEPVSIDAVTTFNKAFAPYGLPR---TAFKPSYGIAEATLFVATIAPDAEPs 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3599 -----RSQ------NYVPIGKP----------LGRNRMYIL---DSKKRLqPKGVQGELYIAGDGVGRGYLNLPELTDEK 3654
Cdd:PRK12476  375 vvyldREQlgagraVRVAADAPnavahvscgqVARSQWAVIvdpDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERT 453
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876 3655 FV------------ADPFVPEDRMYRTGDLARLLpDGNIEYIGRIDHQVKIQG 3695
Cdd:PRK12476  454 FGaklqsrlaegshADGAADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
3285-3791 8.91e-14

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 78.30  E-value: 8.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3285 IHELFEEQAHRTPDNTAVVFEG-----KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGA 3359
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3360 YLPIDPDSPSERIRYILNDSSISVLLycgkLQDdiGFS--GTCIDLMEE------------------------------- 3406
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALI----TAD--GFTrrGREVNLKEEadkacaqcptvekvvvvrhlgndftpakgrd 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3407 HFYHE---KDSSLALSYQSSQLAYAIYTSGTTGKPKGTliehrqvIHLIEGLSrqVYSAYDAELNIA------------- 3470
Cdd:cd05968   217 LSYDEekeTAGDGAERTESEDPLMIIYTSGTTGKPKGT-------VHVHAGFP--LKAAQDMYFQFDlkpgdlltwftdl 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3471 --MLAPYYfdasvqqMYASLLSGHTLFIVpkeivsDGAA-------LCRYYRQHSIDITDGTPAHLKLLIAAGD--LQGV 3539
Cdd:cd05968   288 gwMMGPWL-------IFGGLILGATMVLY------DGAPdhpkadrLWRMVEDHEITHLGLSPTLIRALKPRGDapVNAH 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3540 TLQHL-LIG--GEALSKTTVNKLKQLFGEhGAAPgITNVYGPTEtcVDASLFNiecssdawarsqNYV--PIgKPLGRN- 3613
Cdd:cd05968   355 DLSSLrVLGstGEPWNPEPWNWLFETVGK-GRNP-IINYSGGTE--ISGGILG------------NVLikPI-KPSSFNg 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3614 -----RMYILD-SKKRLQPKgvQGELYIAGDGVG--RGYLNlpelTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIG 3685
Cdd:cd05968   418 pvpgmKADVLDeSGKPARPE--VGELVLLAPWPGmtRGFWR----DEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILG 491
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3686 RIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAA-ALKDADDEYYLCgyFA------ADKTIQISELRKRMARHLPGYMI 3758
Cdd:cd05968   492 RSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIgVPHPVKGEAIVC--FVvlkpgvTPTEALAEELMERVADELGKPLS 569
                         570       580       590
                  ....*....|....*....|....*....|...
gi 166797876 3759 PAHFVQLDKMPLTPNGKLNRQLLPAPVKKRDSG 3791
Cdd:cd05968   570 PERILFVKDLPKTRNAKVMRRVIRAAYLGKELG 602
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4358-4818 1.02e-13

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 77.22  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4358 LTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPEL-PEKRRAFMLKDSGADVLLTC 4436
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLtPDDLRDRVDRGGAVYAAVDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4437 AGHAipplfegevlllDDPLLyqgrtdnlnlscsendlMYviYTSGTTGQPKGVQLEHKTmtnllaYEQDHTQLRFDRVL 4516
Cdd:cd05974    81 NTHA------------DDPML-----------------LY--FTSGTTSKPKLVEHTHRS------YPVGHLSTMYWIGL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4517 QFAAMSFDV--------CYQEMFSALSSGGILFIIgNEAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLASEKhyFEPFAE 4588
Cdd:cd05974   124 KPGDVHWNIsspgwakhAWSCFFAPWNAGATVFLF-NYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD--LASFDV 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4589 CVDHIIAAGEQLiATRMLRDMLARHQVTLHNHYGPSETHVVtmytVDPDTDQELQP--IGKPISNTEIFILNEAGtlQPV 4666
Cdd:cd05974   201 KLREVVGAGEPL-NPEVIEQVRRAWGLTIRDGYGQTETTAL----VGNSPGQPVKAgsMGRPLPGYRVALLDPDG--APA 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4667 GiVGELCIS-----GVSLARGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGE 4741
Cdd:cd05974   274 T-EGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4742 VEAALLKH--VQEAVVLAKENTDGQSDLYAYF--------TAEQSLSISQ-LKEKLAgqiPGYMIPSyfIQLEKLPLTGN 4810
Cdd:cd05974   346 LESVLIEHpaVAEAAVVPSPDPVRLSVPKAFIvlragyepSPETALEIFRfSRERLA---PYKRIRR--LEFAELPKTIS 420

                  ....*...
gi 166797876 4811 GKVNRRAL 4818
Cdd:cd05974   421 GKIRRVEL 428
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
3429-3778 1.03e-13

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 76.15  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3429 IYTSGTTGKPKGTLIEHRQVIHLIEGLSRQV--YSAYDAELniaMLAPYYFDASVQQMYASLLSGhTLFIVPKEIVSDGA 3506
Cdd:cd17635     7 IFTSGTTGEPKAVLLANKTFFAVPDILQKEGlnWVVGDVTY---LPLPATHIGGLWWILTCLIHG-GLCVTGGENTTYKS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3507 AL--CRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLIGGEALskttVNKLKQLFgEHGAAPGITNVYGPTET--- 3581
Cdd:cd17635    83 LFkiLTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRA----IAADVRFI-EATGLTNTAQVYGLSETgta 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3582 -CVDASLFNIECSSdawarsqnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpf 3660
Cdd:cd17635   158 lCLPTDDDSIEINA-----------VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI---- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3661 vpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADD-EYYLCGYFAA--- 3736
Cdd:cd17635   223 ---DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFgELVGLAVVASael 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 166797876 3737 DKTIqISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNR 3778
Cdd:cd17635   300 DENA-IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1798-2203 1.04e-13

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 77.71  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQA-GIVL 1876
Cdd:PLN02330   54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAkLIVT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 MQRDVRKQLAYEGVTVLLDDES-SYHQDGSDLAPISD------------VSHLAYVIYTSGSTGRPKGVLIEHGGLTNYI 1943
Cdd:PLN02330  134 NDTNYGKVKGLGLPVIVLGEEKiEGAVNWKELLEAADragdtsdneeilQTDLCALPFSSGTTGISKGVMLTHRNLVANL 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1944 WWA---------KEVYVKGEKANFPLYSsisfdltVTSI-FTPLVTGNAIIVYDGEDKTALLESIVRD-----PRVDIIK 2008
Cdd:PLN02330  214 CSSlfsvgpemiGQVVTLGLIPFFHIYG-------ITGIcCATLRNKGKVVVMSRFELRTFLNALITQevsfaPIVPPII 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2009 LTPAHLQVLKEMNIAdQTAVRRMIVGGENLSTRLARSIHEQFEGrIEICNEYGPTETvvGCMIYRY-DAAKD----RRES 2083
Cdd:PLN02330  287 LNLVKNPIVEEFDLS-KLKLQAIMTAAAPLAPELLTAFEAKFPG-VQVQEAYGLTEH--SCITLTHgDPEKGhgiaKKNS 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2084 VpiGTAAANTSIYVLD-ENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIE 2162
Cdd:PLN02330  363 V--GFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW------LHTGDIGYIDDDGDIF 434
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 166797876 2163 YAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARED 2203
Cdd:PLN02330  435 IVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPD 475
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
3429-3776 1.06e-13

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 76.00  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3429 IYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYDAelNIAMLAPYYFDASVQQ-MYASLLSGHTlfIVPkEIVSDGAA 3507
Cdd:cd17638     6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD--RYLIINPFFHTFGYKAgIVACLLTGAT--VVP-VAVFDVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3508 LCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLIGGEALSKTTVNKLKQLFGEHGAApGITNVYGPTEtCVDASL 3587
Cdd:cd17638    81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE-TVLTAYGLTE-AGVATM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3588 FNIECSSDAWARSqnyvpIGKPLGRNRMYILDskkrlqpkgvQGELYIAGDGVGRGYLNLPELTDEKFVADPFVpedrmy 3667
Cdd:cd17638   159 CRPGDDAETVATT-----CGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWL------ 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3668 RTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISE--- 3744
Cdd:cd17638   218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEedv 297
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 166797876 3745 ---LRKRMArhlpGYMIPAHFVQLDKMPLTPNGKL 3776
Cdd:cd17638   298 iawCRERLA----NYKVPRFVRFLDELPRNASGKV 328
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1842-2263 1.15e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 77.00  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1842 LAVLKSGGAYVPIDPEYPQDRIRYMLDDSQ-AGIVLMQRDVRKQLAYEGvtvlLDDESSYHQdgsdlapisdvshlayvi 1920
Cdd:PRK08308   50 FFLKEKGASVLPIHPDTPKEAAIRMAKRAGcHGLLYGESDFTKLEAVNY----LAEEPSLLQ------------------ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1921 YTSGSTGRPKgvLIEHGgltnyiwWAK-----EVYVK---GEKANFPLYS---SISFDLtVTSIFTPLVTGNA-IIVYDG 1988
Cdd:PRK08308  108 YSSGTTGEPK--LIRRS-------WTEidreiEAYNEalnCEQDETPIVAcpvTHSYGL-ICGVLAALTRGSKpVIITNK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1989 EDKTALleSIVRDPRVDIIKLTPAHLQVLKEMNIADQTAVRRMIVGgenlsTRLARSIHEQFEGRIEI-CNEYGPTETvv 2067
Cdd:PRK08308  178 NPKFAL--NILRNTPQHILYAVPLMLHILGRLLPGTFQFHAVMTSG-----TPLPEAWFYKLRERTTYmMQQYGCSEA-- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2068 GCMiyryDAAKDRRESVPIGTAAANTSIYV-LDENMkpapigvPGEIYIsgagvargylnrpeltaekfvddpfEPGAKM 2146
Cdd:PRK08308  249 GCV----SICPDMKSHLDLGNPLPHVSVSAgSDENA-------PEEIVV-------------------------KMGDKE 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2147 YKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYVSGGQTTAARLR 2226
Cdd:PRK08308  293 IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLR 372
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 166797876 2227 KQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGLPA 2263
Cdd:PRK08308  373 EWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
273-744 1.29e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 77.42  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKFKNDH--LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKE 350
Cdd:PRK13391    7 AQTTPDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  351 RLQYLLHDADADVLLVQH--------------HLKNSLAFDG----PVIDLNDEASyhADCSLlSPVAGHSHLAYVIYTS 412
Cdd:PRK13391   87 EAAYIVDDSGARALITSAakldvarallkqcpGVRHRLVLDGdgelEGFVGYAEAV--AGLPA-TPIADESLGTDMLYSS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  413 GTTGKPKGVMVE--HGGIVNSLQWkKAFFKH-----------SPAdrvlvlyPyVFDAFILNFFGPLIS-GATLHLLpne 478
Cdd:PRK13391  164 GTTGRPKGIKRPlpEQPPDTPLPL-TAFLQRlwgfrsdmvylSPA-------P-LYHSAPQRAVMLVIRlGGTVIVM--- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  479 enkETFAIQNA---IKQERITHFSTSP----RLLKTMIEQMNREDFIHVQHVVVGGEQLETDTVEKLhslqprIR----- 546
Cdd:PRK13391  232 ---EHFDAEQYlalIEEYGVTHTQLVPtmfsRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQM------IDwwgpi 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  547 INNEYGPTENSVVSTFHPVQSADEQITIGSPVANhQAYILGAHHQIQPIGIPGELYVGGaGVARGYLNRPELTEEKfveh 626
Cdd:PRK13391  303 IHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEA---- 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  627 lHVPGQKMYKTGDLArWLPDGRIEYL-GRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV-- 703
Cdd:PRK13391  377 -RHPDGTWSTVGDIG-YVDEDGYLYLtDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQpv 454
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876  704 --GEPSLTAAQ-----FREELSRelpnYMIPSRFIPLERIPLTSNGKI 744
Cdd:PRK13391  455 dgVDPGPALAAeliafCRQRLSR----QKCPRSIDFEDELPRLPTGKL 498
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
852-1167 1.36e-13

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 76.76  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  852 LTPIQHWFF-----EQKMPH--AHHYNQavmlYSAEGFKEGPLRRTMERIASHHDALRMIFekTPDGYApRItgTDESEL 924
Cdd:cd19535     4 LTDVQYAYWigrqdDQELGGvgCHAYLE----FDGEDLDPDRLERAWNKLIARHPMLRAVF--LDDGTQ-QI--LPEVPW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  925 FHLEVMNYKGEtdPAQAIADKANEIQSSM---VLD--KGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASG 998
Cdd:cd19535    75 YGITVHDLRGL--SEEEAEAALEELRERLshrVLDveRGPLFDIRLSLLPEGRTrLHLSIDLLVADALSLQILLRELAAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  999 YEQAERrqtiQLPQKTDSFPfwaDQLSKYAA--ETDMEEEIAYWTE-LSSIKPQP-LPkdtisegsLLRDSEEVT----- 1069
Cdd:cd19535   153 YEDPGE----PLPPLELSFR---DYLLAEQAlrETAYERARAYWQErLPTLPPAPqLP--------LAKDPEEIKeprft 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1070 --IQWTKEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPdaDISRTIGWFTSQYPVVLR 1147
Cdd:cd19535   218 rrEHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHP--DVNDVVGDFTSLLLLEVD 295
                         330       340
                  ....*....|....*....|
gi 166797876 1148 MEAGKNLSQRIKIVKEGLRR 1167
Cdd:cd19535   296 GSEGQSFLERARRLQQQLWE 315
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
4621-4815 1.44e-13

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 75.38  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4621 YGPSETH-VVTM--YTVDPDTdqelqpIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvph 4697
Cdd:cd17637   143 YGQTETSgLVTLspYRERPGS------AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4698 pydsnqR--MYKTGDLARYLPEGNIEYAGRRDHQ--VKIRGYRVELGEVEAALLKH--VQEAVVLakentdGQSDlyAYF 4771
Cdd:cd17637   214 ------RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHpaIAEVCVI------GVPD--PKW 279
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 4772 T----------AEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd17637   280 GegikavcvlkPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
3304-3793 1.45e-13

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 77.09  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3304 FEGKQFTYEELNRRANQLARTLQ-AKGVQADQLVGIMTERSLEMVVGILGVLKAGGAylpidpdsPSeRIRYILNDSSis 3382
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PA-FINYNLSGDP-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3383 vLLYCGKLqddigfSGtcidlmeehfyhekdsSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVihLIEGLSRQVYSA 3462
Cdd:cd05937    70 -LIHCLKL------SG----------------SRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRT--LVTSNLLSHDLN 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3463 YDAELNIAMLAP-YYFDASVQQMYASLLSGHTLFIVPK--------EIVSDGAA-------LCRYYRQHSIDITDgtPAH 3526
Cdd:cd05937   125 LKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRKfsasqfwkDVRDSGATiiqyvgeLCRYLLSTPPSPYD--RDH 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3527 lKLLIAAGDlqgvtlqhlliggeALSKTTVNKLKQLFGehgaAPGITNVYGPTE-----TCVDASLFNIECSSDA----- 3596
Cdd:cd05937   203 -KVRVAWGN--------------GLRPDIWERFRERFN----VPEIGEFYAATEgvfalTNHNVGDFGAGAIGHHglirr 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3597 WARSQNYVPI------GKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVPEDRMYRTG 3670
Cdd:cd05937   264 WKFENQVVLVkmdpetDDPIRDPKTGFCVRAPVGEPGEMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTG 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3671 DLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKdaddeyyLCGY-----FAADK------- 3738
Cdd:cd05937   344 DLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVK-------VPGHdgragCAAITleessav 416
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 3739 --TIQISELRKRMARHLPGYMIPAhFVQL-DKMPLTPNGKLNRQLLpapvkkRDSGIE 3793
Cdd:cd05937   417 ptEFTKSLLASLARKNLPSYAVPL-FLRLtEEVATTDNHKQQKGVL------RDEGVD 467
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4840-4899 1.62e-13

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 67.97  E-value: 1.62e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876  4840 EQLICIWQDVLKV--KEIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQCPTVGE 4899
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3308-3713 1.75e-13

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 76.73  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3308 QFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLLYC 3387
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3388 GKLQDDigfsgtcidlmeehfyhekdsslalsyqssqlAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLsRQVYSAYDAEL 3467
Cdd:cd05910    82 PKADEP--------------------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDAL-RQLYGIRPGEV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3468 NIAMLAPYyfdasvqQMYASLLsGHTLFIVP----KEIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQH 3543
Cdd:cd05910   129 DLATFPLF-------ALFGPAL-GLTSVIPDmdptRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3544 L---LIGGEALSKTTVNKLKQLFgeHGAAPgITNVYGPTETCVDASlfnIEcSSDAWARSQNY------VPIGKPLGRNR 3614
Cdd:cd05910   201 LrrvLSAGAPVPIALAARLRKML--SDEAE-ILTPYGATEALPVSS---IG-SRELLATTTAAtsggagTCVGRPIPGVR 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3615 MYIL----------DSKKRLqPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPfvPEDRMYRTGDLARLLPDGNIEYI 3684
Cdd:cd05910   274 VRIIeiddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDEGRLWFC 350
                         410       420
                  ....*....|....*....|....*....
gi 166797876 3685 GRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:cd05910   351 GRKAHRVITTGGTLYTEPVERVFNTHPGV 379
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
284-744 2.13e-13

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 76.32  E-value: 2.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  284 FKNDHLTYRELNEKASRLARTLRNC-GVQPDTLVAILADRSLEMIVSIIAVWKAGGAyvpldPEYpkerLQYLLHDadaD 362
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INYNLSG---D 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  363 VLLvqHHLKNSlafdgpvidlndeasyhaDCSLLspVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHS 442
Cdd:cd05937    69 PLI--HCLKLS------------------GSRFV--IVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  443 PADRVLVLYP-YVFDAFILNFFGPLISGATLHLLPNeenketFAIQNAIKQ---ERITHF----STSPRLLKTMIEQMNR 514
Cdd:cd05937   127 NGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRK------FSASQFWKDvrdSGATIIqyvgELCRYLLSTPPSPYDR 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  515 edfihvQHVV--VGGEQLETDTVEKLhslqpRIRINNE-----YGPTENsvVSTFHPVQSADeqITIGSpVANH------ 581
Cdd:cd05937   201 ------DHKVrvAWGNGLRPDIWERF-----RERFNVPeigefYAATEG--VFALTNHNVGD--FGAGA-IGHHglirrw 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  582 ----QAYILGAHHQIQ--------------PIGIPGELYV----GGAGVARGYLNRPELTEEKFVEHLHVPGQKMYKTGD 639
Cdd:cd05937   265 kfenQVVLVKMDPETDdpirdpktgfcvraPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGD 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  640 LARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAV--VAREDADGAKQLYAYYVGEPSLTAAQFR--- 714
Cdd:cd05937   345 LLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSAVPTEFTksl 424
                         490       500       510
                  ....*....|....*....|....*....|...
gi 166797876  715 -EELSR-ELPNYMIPsRFIPL-ERIPLTSNGKI 744
Cdd:cd05937   425 lASLARkNLPSYAVP-LFLRLtEEVATTDNHKQ 456
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1798-2261 2.63e-13

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 75.93  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRANRLARTLR-AKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVl 1876
Cdd:cd05937     4 KTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 mqrdvrkqlayegvtvllddessyhqdgsdlapISDVSHLAYVIYTSGSTGRPKGVLIEHGGLTNYIW-WAKEVYVKGEK 1955
Cdd:cd05937    83 ---------------------------------IVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNlLSHDLNLKNGD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1956 ANF---PLYSSISFDLTVTSI-----------------FTPLV--TGNAIIVYDGEDKTALLEsivrdprvdiiklTPAh 2013
Cdd:cd05937   130 RTYtcmPLYHGTAAFLGACNClmsggtlalsrkfsasqFWKDVrdSGATIIQYVGELCRYLLS-------------TPP- 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2014 lqvlkemNIADQTAVRRMIVGgenlsTRLARSIHEQFEGR--IEICNE-YGPTETVvgcmiyrydAAKDRRESVPIGTAA 2090
Cdd:cd05937   196 -------SPYDRDHKVRVAWG-----NGLRPDIWERFRERfnVPEIGEfYAATEGV---------FALTNHNVGDFGAGA 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2091 ------------ANTSIYV-LDEN-----MKP-------APIGVPGE----IYISGAGVARGYLNRPELTAEKFVDDPFE 2141
Cdd:cd05937   255 ighhglirrwkfENQVVLVkMDPEtddpiRDPktgfcvrAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFR 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2142 PGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTA-----REDVHGFKQLCAYYVS 2216
Cdd:cd05937   335 KGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvpgHDGRAGCAAITLEESS 414
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876 2217 GGQT--TAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05937   415 AVPTefTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
3293-3714 3.82e-13

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 75.68  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERI 3372
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3373 RYILNDSSISVLLYcgkLQDDIGFSGTCIDLMeehfyHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQviHLI 3452
Cdd:PRK09029   93 EELLPSLTLDFALV---LEGENTFSALTSLHL-----QLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA--HLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3453 --EGLSRQV-YSAYDAELniamLAPYYFDASVQQ-MYASLLSGHTLfivpkeIVSDGAALCRyyrqhsiDITDGTPAHL- 3527
Cdd:PRK09029  163 saEGVLSLMpFTAQDSWL----LSLPLFHVSGQGiVWRWLYAGATL------VVRDKQPLEQ-------ALAGCTHASLv 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3528 -----KLLiaAGDLQGVTLQHLLIGGEALSKTTVNKLKQLfgehgaapGITNV--YGPTETcvdASLFnieCSSDAWARS 3600
Cdd:PRK09029  226 ptqlwRLL--DNRSEPLSLKAVLLGGAAIPVELTEQAEQQ--------GIRCWcgYGLTEM---ASTV---CAKRADGLA 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3601 QnyvpIGKPLGrNRMYILdskkrlqpkgVQGELYIAGDGVGRGYLNLPELTdekfvadPFVPEDRMYRTGDLARLLpDGN 3680
Cdd:PRK09029  290 G----VGSPLP-GREVKL----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGE 346
                         410       420       430
                  ....*....|....*....|....*....|....
gi 166797876 3681 IEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQ 3714
Cdd:PRK09029  347 LTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQ 380
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3797-3869 4.51e-13

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 67.57  E-value: 4.51e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 3797 PQTSAEIQLTAIWEDVLGL--EQVGIRDHFF-EIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLARTITK 3869
Cdd:COG0236     2 PREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
PRK07867 PRK07867
acyl-CoA synthetase; Validated
2030-2270 4.66e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 75.49  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2030 RMIVGGENLSTRLARsiheqFEGR--IEICNEYGPTETVVgcmiyrydaAKDRRESVP---IGTAAANTSIY-------- 2096
Cdd:PRK07867  270 RIVYGNEGAPGDIAR-----FARRfgCVVVDGFGSTEGGV---------AITRTPDTPpgaLGPLPPGVAIVdpdtgtec 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2097 ---VLDENMKPAPIGVPGEIY-ISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVK 2172
Cdd:PRK07867  336 ppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMR 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2173 IRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQL-SQT-LASYMVPAYFIELDEM 2248
Cdd:PRK07867  409 VDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVlaPGAKFDPDAFAEFLaAQPdLGPKQWPSYVRVCAEL 488
                         250       260
                  ....*....|....*....|..
gi 166797876 2249 PLTSNGKINKKGLPAPDFELQD 2270
Cdd:PRK07867  489 PRTATFKVLKRQLSAEGVDCAD 510
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
4342-4490 4.97e-13

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 75.29  E-value: 4.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRR 4421
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 4422 AFMLKDSGADVLLTCAGHAIPPLFegevllldDPLLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGV 4490
Cdd:PRK09029   93 EELLPSLTLDFALVLEGENTFSAL--------TSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAA 153
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2363-2678 5.51e-13

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 74.71  E-value: 5.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2363 SLTPIQH--WFFEQTTTDQHYYNQAvmlHAPE--GFQETQ-LRQTLQKLAEHHDALRMTFrTTENGCEAQneEIAQSGLY 2437
Cdd:cd19533     3 PLTSAQRgvWFAEQLDPEGSIYNLA---EYLEitGPVDLAvLERALRQVIAEAETLRLRF-TEEEGEPYQ--WIDPYTPV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2438 RLEVMNLKEDPDPGRTIEA-KADEIQSSMHLSDGPLMKAGLFQCADGDHLLIA-IHHLIIDGISWRILLEDIVSGYKQAE 2515
Cdd:cd19533    77 PIRHIDLSGDPDPEGAAQQwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIYTALL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2516 NGRVIQlPQKTDSFQLWAKRLSEYAQSETIKQEQEYWTkiEQTEVKPLPKDFHE-THTTAKDSETAAVEWTKEETELLLK 2594
Cdd:cd19533   157 KGRPAP-PAPFGSFLDLVEEEQAYRQSERFERDRAFWT--EQFEDLPEPVSLARrAPGRSLAFLRRTAELPPELTRTLLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2595 QAnRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGReqiiqdidISR----TVGWFTSLYPVVLHAQPGKEISDYI 2670
Cdd:cd19533   234 AA-EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR--------LGAaarqTPGMVANTLPLRLTVDPQQTFAELV 304

                  ....*...
gi 166797876 2671 KTTKEGLR 2678
Cdd:cd19533   305 AQVSRELR 312
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
916-1159 5.84e-13

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 74.66  E-value: 5.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  916 ITGTDESELFHLEVMNYkgetdpaqaIADKANEiqsSMVLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLED 994
Cdd:cd20484    78 FQEEDISSLKESEIIAY---------LREKAKE---PFVLENGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHS 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  995 FASGYEQAERRQTIQLPQKTDSFPFWADQLSKYAAETDMEEEIAYWTE-LSSIKPQ-PLPKDtiSEGSLLRDSEEVTiqW 1072
Cdd:cd20484   146 LLDAYQALLQGKQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQqLSGTLPIlELPAD--RPRSSAPSFEGQT--Y 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1073 TKEETEQLLKQAN---RAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGRepiiPDADISRTIGWFTSQYPVVLRME 1149
Cdd:cd20484   222 TRRLPSELSNQIKsfaRSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR----PEERFDSLIGYFINMLPIRSRIL 297
                         250
                  ....*....|
gi 166797876 1150 AGKNLSQRIK 1159
Cdd:cd20484   298 GEETFSDFIR 307
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
4354-4821 6.10e-13

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 75.12  E-value: 6.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4354 GNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVL 4433
Cdd:PRK12406    8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4434 LtcaGHAipPLFEG---------EVLLLDDP--LLYQGRTDNLNLSCSENDLMY--------------------VIYTSG 4482
Cdd:PRK12406   88 I---AHA--DLLHGlasalpagvTVLSVPTPpeIAAAYRISPALLTPPAGAIDWegwlaqqepydgppvpqpqsMIYTSG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4483 TTGQPKGVQLEHKTMTNLLAYEQ----DHTQLRFDRVLQFAAMSFDVCYQEMFSALSSGGILFIignEAKRDIRQLNDFV 4558
Cdd:PRK12406  163 TTGHPKGVRRAAPTPEQAAAAEQmralIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVL---QPRFDPEELLQLI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4559 RTHGIQTAFL-PTAFLKLL------------ASEKHYFEPFAECVDHIiaageqliatrmLRDMLARHQVTLHNHYGPSE 4625
Cdd:PRK12406  240 ERHRITHMHMvPTMFIRLLklpeevrakydvSSLRHVIHAAAPCPADV------------KRAMIEWWGPVIYEYYGSTE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4626 THVVTMYTVD-----PDTdqelqpIGKPISNTEIFILNEAGTLQPVGIVGELcisgVSLARG-----YHN----RESLTL 4691
Cdd:PRK12406  308 SGAVTFATSEdalshPGT------VGKAAPGAELRFVDEDGRPLPQGEIGEI----YSRIAGnpdftYHNkpekRAEIDR 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4692 ETFVphpydsnqrmyKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLK--HVQEAVVLAKENTDGQSDLYA 4769
Cdd:PRK12406  378 GGFI-----------TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAvpGVHDCAVFGIPDAEFGEALMA 446
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 4770 YFT--AEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMP 4821
Cdd:PRK12406  447 VVEpqPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
290-655 6.59e-13

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 75.15  E-value: 6.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  290 TYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ-- 367
Cdd:cd17641    13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEde 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  368 -------------HHLKNSLAFD---------------------GPVIDLNDEASYHADCSLLSPvaghSHLAYVIYTSG 413
Cdd:cd17641    93 eqvdklleiadriPSVRYVIYCDprgmrkyddprlisfedvvalGRALDRRDPGLYEREVAAGKG----EDVAVLCTTSG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  414 TTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYP--YVFDaFILNFFGPLISGATLHLLpneENKETfaIQNAIK 491
Cdd:cd17641   169 TTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPlpWIGE-QMYSVGQALVCGFIVNFP---EEPET--MMEDLR 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  492 QERITHFSTSPRLLKTMIEQM-------------------------------------------------------NRED 516
Cdd:cd17641   243 EIGPTFVLLPPRVWEGIAADVrarmmdatpfkrfmfelgmklglraldrgkrgrpvslwlrlaswladallfrplrDRLG 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  517 FIHVQHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTENSVVSTFHPVQSADEQiTIGSPVANHQAYILGAhhqiqpig 596
Cdd:cd17641   323 FSRLRSAATGGAALGPDTFRFFHAIG--VPLKQLYGQTELAGAYTVHRDGDVDPD-TVGVPFPGTEVRIDEV-------- 391
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876  597 ipGELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGDLARWLPDGRIEYLGRI 655
Cdd:cd17641   392 --GEILVRSPGVFVGYYKNPEATAEDFDE------DGWLHTGDAGYFKENGHLVVIDRA 442
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1784-2258 6.69e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 75.22  E-value: 6.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1784 SQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDpeYpqdri 1863
Cdd:PLN02860   17 ATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN--Y----- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1864 RYMLDDSQAGIVLMQ-----RDVRKQLAYEGVT----------VLLDD--ESSYHQDGSDLAPisdvSHL---------- 1916
Cdd:PLN02860   90 RWSFEEAKSAMLLVRpvmlvTDETCSSWYEELQndrlpslmwqVFLESpsSSVFIFLNSFLTT----EMLkqralgttel 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1917 ---------AYVIYTSGSTGRPKGVLIEHGGLTNYIWwAKEVYVKGEKANFPLYSS-------ISfdltvtSIFTPLVTG 1980
Cdd:PLN02860  166 dyawapddaVLICFTSGTTGRPKGVTISHSALIVQSL-AKIAIVGYGEDDVYLHTAplchiggLS------SALAMLMVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1981 NAIIVYDGEDKTALLESIvRDPRVDIIKLTPAHLQVL-----KEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEgRIE 2055
Cdd:PLN02860  239 ACHVLLPKFDAKAALQAI-KQHNVTSMITVPAMMADLisltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFP-NAK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2056 ICNEYGPTETvvgCMIYRYDAAKDRRESVPIGTAAANTSIYVLDENM-------KPAP-----IGVP-----GEIYISGA 2118
Cdd:PLN02860  317 LFSAYGMTEA---CSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQpqgvcvgKPAPhvelkIGLDessrvGRILTRGP 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2119 GVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVV 2198
Cdd:PLN02860  394 HVMLGYWGQNSETASVLSNDGW------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 2199 TAREDVHGFKQLCA-------YYVSGGQTTAARLRKQLS----------QTLASYMVPAYFIEL-DEMPLTSNGKINK 2258
Cdd:PLN02860  468 VGVPDSRLTEMVVAcvrlrdgWIWSDNEKENAKKNLTLSsetlrhhcreKNLSRFKIPKLFVQWrKPFPLTTTGKIRR 545
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
3430-3778 7.25e-13

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 73.21  E-value: 7.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3430 YTSGTTGKPKGTLIEHRQVIHLIEgLSRQVYsAYDAELNIAMLAPYYFDASVQQMYASLLSGHTlFIVPKEIvsDGAALC 3509
Cdd:cd17633     7 FTSGTTGLPKAYYRSERSWIESFV-CNEDLF-NISGEDAILAPGPLSHSLFLYGAISALYLGGT-FIGQRKF--NPKSWI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3510 RYYRQHSIDITDGTPAHLKLLIAAGDLQgVTLQHLLIGGEALSKTTVNKLKQLFGEhgaaPGITNVYGPTETCVDASLFN 3589
Cdd:cd17633    82 RKINQYNATVIYLVPTMLQALARTLEPE-SKIKSIFSSGQKLFESTKKKLKNIFPK----ANLIEFYGTSELSFITYNFN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3590 IEcssdawARSQNYVpiGKPLGRNRMYILDskkrlQPKGVQGELYIAGDGVGRGYLNLPELTdekfvadpfvpEDRMYRT 3669
Cdd:cd17633   157 QE------SRPPNSV--GRPFPNVEIEIRN-----ADGGEIGKIFVKSEMVFSGYVRGGFSN-----------PDGWMSV 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3670 GDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaAALKDADDEYY-------LCGYFAADKTIQI 3742
Cdd:cd17633   213 GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEE---AIVVGIPDARFgeiavalYSGDKLTYKQLKR 289
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 166797876 3743 SeLRKRMARhlpgYMIPAHFVQLDKMPLTPNGKLNR 3778
Cdd:cd17633   290 F-LKQKLSR----YEIPKKIIFVDSLPYTSSGKIAR 320
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
3283-3784 8.08e-13

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 74.91  E-value: 8.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3283 KTIHELFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTL--QAKGVQADQlVGIMTERSLEMVVGILGVLKAGGAY 3360
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLlgELQLKKGDR-VALMMPNCLQYPIATFGVLRAGLTV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3361 LPIDPDSPSERIRYILNDSSISVLL----YCGKLQ-----------------DDIGF-SGTCIDLMEEHF------YH-- 3410
Cdd:PRK08751  104 VNVNPLYTPRELKHQLIDSGASVLVvidnFGTTVQqviadtpvkqvittglgDMLGFpKAALVNFVVKYVkklvpeYRin 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3411 ------------EKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYD----AELNIAMLAP 3474
Cdd:PRK08751  184 gairfrealalgRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3475 YY-FDASVQQMYASLLSGHTLFIV-PKEIVSDGAALcryYRQHSIDITDGTPAHLKLLIAAG--DLQGVTLQHLLIGGEA 3550
Cdd:PRK08751  264 YHiFALTANGLVFMKIGGCNHLISnPRDMPGFVKEL---KKTRFTAFTGVNTLFNGLLNTPGfdQIDFSSLKMTLGGGMA 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3551 LSKTTVNKLKQLFGehgaaPGITNVYGPTETCVDAslfnieCSSDAWARSQNYvPIGKPLGRNRMYILDSKKRLQPKGVQ 3630
Cdd:PRK08751  341 VQRSVAERWKQVTG-----LTLVEAYGLTETSPAA------CINPLTLKEYNG-SIGLPIPSTDACIKDDAGTVLAIGEI 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3631 GELYIAGDGVGRGYLNLPELTDEKFVADPFVpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNV 3710
Cdd:PRK08751  409 GELCIKGPQVMKGYWKRPEETAKVMDADGWL------HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3711 PDIQEAAAA-ALKDADDEYYLCGYFAADKTIQISELRKRMARHLPGYMIPaHFVQLDK-MPLTPNGK-LNRQLLPAP 3784
Cdd:PRK08751  483 PGVLEVAAVgVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQP-RIIEFRKeLPKTNVGKiLRRELRDAA 558
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1789-2256 8.78e-13

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 75.18  E-value: 8.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1789 DQAAVI------DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI----DPEY 1858
Cdd:PRK00174   82 DKVAIIwegddpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEA 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 PQDRIrymlDDSQAGIVL-----------------------MQRDVRKQLAYE--GVTV------------LLDDESSYH 1901
Cdd:PRK00174  162 LADRI----IDAGAKLVItadegvrggkpiplkanvdealaNCPSVEKVIVVRrtGGDVdwvegrdlwwheLVAGASDEC 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1902 QdgsdlAPISDVSHLAYVIYTSGSTGRPKGVLIEHGGltnYIWWA----KevYVkgekanfplyssisFDLTVTSIF--T 1975
Cdd:PRK00174  238 E-----PEPMDAEDPLFILYTSGSTGKPKGVLHTTGG---YLVYAamtmK--YV--------------FDYKDGDVYwcT 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1976 P---LVTGNAIIVY----DGEdKTALLE------------SIVRDPRVDIIKLTPahlqvlkemniadqTAVRRMIVGGE 2036
Cdd:PRK00174  294 AdvgWVTGHSYIVYgplaNGA-TTLMFEgvpnypdpgrfwEVIDKHKVTIFYTAP--------------TAIRALMKEGD 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2037 ------NLST-RLARSI------------HEQF-EGRIEICNEYGPTETVvGCMIYRYDAAKDrreSVPiGTA------- 2089
Cdd:PRK00174  359 ehpkkyDLSSlRLLGSVgepinpeawewyYKVVgGERCPIVDTWWQTETG-GIMITPLPGATP---LKP-GSAtrplpgi 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2090 -AAntsiyVLDENMKPAPIGVPGEIYI--SGAGVARGYLNRPEltaeKFVDDPFEPGAKMYKTGDLAKWLADGNIEYAGR 2166
Cdd:PRK00174  434 qPA-----VVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWITGR 504
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2167 IDEQVKIRGYRIELGEIEAALLQEEVIKE-AVVTAREDVHGfKQLCAYYV-SGGQTTAARLRKQLSQTLASYM----VPA 2240
Cdd:PRK00174  505 VDDVLNVSGHRLGTAEIESALVAHPKVAEaAVVGRPDDIKG-QGIYAFVTlKGGEEPSDELRKELRNWVRKEIgpiaKPD 583
                         570
                  ....*....|....*.
gi 166797876 2241 YFIELDEMPLTSNGKI 2256
Cdd:PRK00174  584 VIQFAPGLPKTRSGKI 599
PRK07788 PRK07788
acyl-CoA synthetase; Validated
3293-3783 9.83e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 74.58  E-value: 9.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERI 3372
Cdd:PRK07788   59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3373 RYILNDSSISVLLY-------CGKLQDDIG-------------FSGTCIDLMEEHFYHEKDSSLALSYQSSQLayAIYTS 3432
Cdd:PRK07788  139 AEVAAREGVKALVYddeftdlLSALPPDLGrlrawggnpdddePSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILTS 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3433 GTTGKPKGTLIEHRQVIHLIEGLSRQVysAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIV----PKEIVSDGAal 3508
Cdd:PRK07788  217 GTTGTPKGAPRPEPSPLAPLAGLLSRV--PFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRrrfdPEATLEDIA-- 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3509 cryyrQHSIDITDGTPAHLKLLIAAG-------DLQgvTLQHLLIGGEALSKTTVNKLKQLFGehgaaPGITNVYGPTet 3581
Cdd:PRK07788  293 -----KHKATALVVVPVMLSRILDLGpevlakyDTS--SLKIIFVSGSALSPELATRALEAFG-----PVLYNLYGST-- 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3582 cvdaslfniECSSDAWARSQNYV--P--IGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYlnlpeltdekfvA 3657
Cdd:PRK07788  359 ---------EVAFATIATPEDLAeaPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------------T 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3658 DPFVPE--DRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAaaaalkdaddeyYLCG--- 3732
Cdd:PRK07788  418 DGRDKQiiDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA------------AVIGvdd 485
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 3733 --YFA---------ADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPA 3783
Cdd:PRK07788  486 eeFGQrlrafvvkaPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1786-2185 1.07e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 74.78  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1786 RTPDQAAVidkdrQLTYGELNKRanrlartLRAKGVQTDQ------PVAIITRNSIESVVGILAVLKSGGAYVPI-DPEY 1858
Cdd:PRK12476   60 HSAAGCAV-----ELTWTQLGVR-------LRAVGARLQQvagpgdRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPEL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1859 P--QDRIRYMLDDSQAGIVLMQrdvrkQLAYEGVTVLLDDESSYHQD------------GSDLAP----ISDVSHLAYvi 1920
Cdd:PRK12476  128 PghAERLDTALRDAEPTVVLTT-----TAAAEAVEGFLRNLPRLRRPrviaidaipdsaGESFVPveldTDDVSHLQY-- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1921 yTSGSTGRPKGVLIEHGGL-TNYIwwakEVYVKGEKAN--------FPLYSsisfDLTVTSIFTPLVTGNAIIVYdgeDK 1991
Cdd:PRK12476  201 -TSGSTRPPVGVEITHRAVgTNLV----QMILSIDLLDrnthgvswLPLYH----DMGLSMIGFPAVYGGHSTLM---SP 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1992 TALlesiVRDPRVDIIKLTPAHLQ---VLKEMNIADQTAVRR---------------MIVGGENLSTRLARSIHEQFE-- 2051
Cdd:PRK12476  269 TAF----VRRPQRWIKALSEGSRTgrvVTAAPNFAYEWAAQRglpaegddidlsnvvLIIGSEPVSIDAVTTFNKAFApy 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2052 --GRIEICNEYGPTETVVGCMIYRYDAAK-----DRRE-----SVPIGTAAANTSIYV-------------LDENM-KPA 2105
Cdd:PRK12476  345 glPRTAFKPSYGIAEATLFVATIAPDAEPsvvylDREQlgagrAVRVAADAPNAVAHVscgqvarsqwaviVDPDTgAEL 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2106 PIGVPGEIYISGAGVARGYLNRPELTAEKFVD------------DPFEPGAKMYKTGDLAKWLaDGNIEYAGRIDEQVKI 2173
Cdd:PRK12476  425 PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrlaegshaDGAADDGTWLRTGDLGVYL-DGELYITGRIADLIVI 503
                         490
                  ....*....|..
gi 166797876 2174 RGYRIELGEIEA 2185
Cdd:PRK12476  504 DGRNHYPQDIEA 515
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
3291-3715 1.19e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 74.36  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3291 EQAHRTPDNTAVV---FEGK--QFTYEELNRRANQLARTLQAKGVQADQLVGIMT---ERSLEMVVGILGVlkagGAYL- 3361
Cdd:PRK07008   17 AHAARHAGDTEIVsrrVEGDihRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSGS----GAVCh 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3362 PIDPDSPSERIRYILNDSSISVLLYcgklqdDIGF-------SGTCID-----LMEEHFYHEKDSSLALSYQS------- 3422
Cdd:PRK07008   93 TINPRLFPEQIAYIVNHAEDRYVLF------DLTFlplvdalAPQCPNvkgwvAMTDAAHLPAGSTPLLCYETlvgaqdg 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3423 ---------SQLAYAIYTSGTTGKPKGTLIEHRQ-VIHlieglsrqvysAYDAELNIAM----------LAPYYFDASVQ 3482
Cdd:PRK07008  167 dydwprfdeNQASSLCYTSGTTGNPKGALYSHRStVLH-----------AYGAALPDAMglsardavlpVVPMFHVNAWG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3483 QMYASLLSGHTLFIVPKEIvsDGAALCRYYRQHSIDITDGTPA-HLKLL--IAAGDLQGVTLQHLLIGGEALSKTTVNKL 3559
Cdd:PRK07008  236 LPYSAPLTGAKLVLPGPDL--DGKSLYELIEAERVTFSAGVPTvWLGLLnhMREAGLRFSTLRRTVIGGSACPPAMIRTF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3560 KQLFG-EHGAAPGITNVyGPTETCvdASLFNIECSSDAWARSQNYVPIGKPLGRNRMYILDSKKRLQP-KGV-QGELYIA 3636
Cdd:PRK07008  314 EDEYGvEVIHAWGMTEM-SPLGTL--CKLKWKHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPwDGKaFGDLQVR 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 3637 GDGVGRGYLnlpeltdeKFVADPFVpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:PRK07008  391 GPWVIDRYF--------RGDASPLV--DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAE 459
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
3257-3781 1.59e-12

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 73.86  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3257 LELLTQQEKEYLL-SRFQSndMHYPREKTIHELFEEQAHRTPDNTAVV--FEGKQFTYEELNRRANQLARTLQAKGVQAD 3333
Cdd:PLN02330    3 MEIQKQEDNEHIFrSRYPS--VPVPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3334 QLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVL----LYCGKLQD----DIGFSGTCI---- 3401
Cdd:PLN02330   81 QVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIvtndTNYGKVKGlglpVIVLGEEKIegav 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3402 ---DLMEEHfYHEKDSSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRqviHLIEGLSRQVYSAYD---AELNIAMLAPY 3475
Cdd:PLN02330  161 nwkELLEAA-DRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHR---NLVANLCSSLFSVGPemiGQVVTLGLIPF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3476 YFDASVQQMYASLL--SGHTLFIVPKEIVSDGAALCryyrQHSIDITDGTPAHLKLLIAAG-----DLQGVTLQHLLIGG 3548
Cdd:PLN02330  237 FHIYGITGICCATLrnKGKVVVMSRFELRTFLNALI----TQEVSFAPIVPPIILNLVKNPiveefDLSKLKLQAIMTAA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3549 EALSKTTVNKLKQLFgehgaaPGIT--NVYGPTE-TCVdaSLFNIECSSDAWARSQNYVPIGKPLGRNRMYILDSKKRLq 3625
Cdd:PLN02330  313 APLAPELLTAFEAKF------PGVQvqEAYGLTEhSCI--TLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSL- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3626 PKGVQGELYIAGDGVGRGYLNLPELTDEKfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIES 3705
Cdd:PLN02330  384 PKNTPGELCVRSQCVMQGYYNNKEETDRT------IDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3706 VMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISE--LRKRMARHLPGY--MIPAHFVqlDKMPLTPNGKLNRQLL 3781
Cdd:PLN02330  458 ILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEedILNFVAANVAHYkkVRVVQFV--DSIPKSLSGKIMRRLL 535
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1320-1742 1.74e-12

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 73.05  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKgmLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYR---GWKdqplQII--FKTKKI 1394
Cdd:cd19534     3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRRedgGWQ----QRIrgDVEELF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1395 GFQFNDLREMKESQK-EAMIQKYARedkmrGFDLEKGALMRLFILRTDEKTYRFIWSFHHILMDG--WclPLITKEIFEN 1471
Cdd:cd19534    77 RLEVVDLSSLAQAAAiEALAAEAQS-----SLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW--RILLEDLEAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1472 YFALLQQKQPEQSSITPYSQYIEWL----GRQDAKEAAAYWDQYLEGYEEqtGLPKDH-HAAEDGRYVPEKVTCDISSDL 1546
Cdd:cd19534   150 YEQALAGEPIPLPSKTSFQTWAELLaeyaQSPALLEELAYWRELPAADYW--GLPKDPeQTYGDARTVSFTLDEEETEAL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1547 tskMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDVvfgsVVS----GRPAGIPNVETM--IGLFINTIPVRFRCEAGTT 1620
Cdd:cd19534   228 ---LQEANAAYRTEINDLLLAALALAFQDWTGRAPP----AIFleghGREEIDPGLDLSrtVGWFTSMYPVVLDLEASED 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1621 FAELMKEAQE--RAV----------------ASQKFETHPLYDIQA----RTTQKQDlithlmifenypVDQYMESIGRQ 1678
Cdd:cd19534   301 LGDTLKRVKEqlRRIpnkgigygilryltpeGTKRLAFHPQPEISFnylgQFDQGER------------DDALFVSAVGG 368
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 1679 NGTSItisNVQMEEQTNYDFNlTVIPGDEMNISFEYNANVYERASIERVREHFMQILHQVVTDA 1742
Cdd:cd19534   369 GGSDI---GPDTPRFALLDIN-AVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
3293-3783 2.21e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 73.49  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERI 3372
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3373 RYILNDSSISVLLYCGKLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQSSQlAYAIYTSGTTGKPKG------------ 3440
Cdd:PRK13383  125 AAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGvprapqlrsavg 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3441 ---TLIEHRQV---------IHLIEGLSRQVYSaydaeLNIAM----LAPYYFDASVQQMYASLLSGHTLFIVPkeivsd 3504
Cdd:PRK13383  204 vwvTILDRTRLrtgsrisvaMPMFHGLGLGMLM-----LTIALggtvLTHRHFDAEAALAQASLHRADAFTAVP------ 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3505 gAALCRYyrqhsIDITDGTPAH-----LKLLIAAGDlqgvtlqhlliggeALSKTTVNKLKQLFGEHgaapgITNVYGPT 3579
Cdd:PRK13383  273 -VVLARI-----LELPPRVRARnplpqLRVVMSSGD--------------RLDPTLGQRFMDTYGDI-----LYNGYGST 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3580 ETCVDASLFNIECSSdaWARSqnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNlpelTDEKFVADP 3659
Cdd:PRK13383  328 EVGIGALATPADLRD--APET-----VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3660 fvpedrMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADK- 3738
Cdd:PRK13383  397 ------MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPg 470
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876 3739 -TIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPA 3783
Cdd:PRK13383  471 sGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1783-2258 2.28e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 73.50  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1783 QSQRTPDQAAVI--DKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQ 1860
Cdd:PRK13390    6 HAQIAPDRPAVIvaETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1861 DRIRYMLDDSQAGIVLMQR-----------DVRKQLAYEG-VTVLLDDESSYHQDGsdlAPISDVSHLAYVIYTSGSTGR 1928
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAaldglaakvgaDLPLRLSFGGeIDGFGSFEAALAGAG---PRLTEQPCGAVMLYSSGTTGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1929 PKGVLIEHGGltnyiwwaKEVYVKGEkanfPLYSSIS--FDLTVTSIF---------TPL-------VTGNAIIVYDGED 1990
Cdd:PRK13390  163 PKGIQPDLPG--------RDVDAPGD----PIVAIARafYDISESDIYyssapiyhaAPLrwcsmvhALGGTVVLAKRFD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1991 KTALLESIVRdPRVDIIKLTPAHLQVLKEMNIA-----DQTAVRRMIVGGENLSTRLArsiHEQFEGRIEICNEYGPTET 2065
Cdd:PRK13390  231 AQATLGHVER-YRITVTQMVPTMFVRLLKLDADvrtryDVSSLRAVIHAAAPCPVDVK---HAMIDWLGPIVYEYYSSTE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2066 VVGCMIyrYDAAKDRRESVPIGTAAANTsIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEkfVDDPFEPgak 2145
Cdd:PRK13390  307 AHGMTF--IDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP--- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2146 MYKT-GDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYY-----VSGGQ 2219
Cdd:PRK13390  379 FWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIqlvegIRGSD 458
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876 2220 TTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINK 2258
Cdd:PRK13390  459 ELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVK 497
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1776-2261 2.53e-12

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 73.32  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAkgvQTD-QP---VAIITRNSIESVVGILAVLKSGGAY 1851
Cdd:PRK12492   26 VVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQ---HTDlVPgdrIAVQMPNVLQYPIAVFGALRAGLIV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1852 VPIDPEYPQDRIRYMLDDSQAGIV----LMQRDVRKQLAYEGVTVLLDDE------------------------SSYH-- 1901
Cdd:PRK12492  103 VNTNPLYTAREMRHQFKDSGARALvylnMFGKLVQEVLPDTGIEYLIEAKmgdllpaakgwlvntvvdkvkkmvPAYHlp 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1902 ---------QDGSDLA--PIS-DVSHLAYVIYTSGSTGRPKGVLIEHGGLT------------------NYIWWAKEVYV 1951
Cdd:PRK12492  183 qavpfkqalRQGRGLSlkPVPvGLDDIAVLQYTGGTTGLAKGAMLTHGNLVanmlqvraclsqlgpdgqPLMKEGQEVMI 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1952 kgekANFPLYSSISFDLTVTSIftpLVTGN-AIIVYDGEDKTALLESIVRDPRVDIIKLTPAHLQVLK--EMNIADQTAV 2028
Cdd:PRK12492  263 ----APLPLYHIYAFTANCMCM---MVSGNhNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDhpGFKDLDFSAL 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2029 RRMIVGGenlsTRLARSIHEQFEGRI--EICNEYGPTET--VVGCMIYrydAAKDRRESVpiGTAAANTSIYVLDENMKP 2104
Cdd:PRK12492  336 KLTNSGG----TALVKATAERWEQLTgcTIVEGYGLTETspVASTNPY---GELARLGTV--GIPVPGTALKVIDDDGNE 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2105 APIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIE 2184
Cdd:PRK12492  407 LPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2185 ------------AAL-LQEEVIKEAV---VTAREDVHGFKQLCAYyvsggqttaarlrkqLSQTLASYMVPAYFIELDEM 2248
Cdd:PRK12492  481 dvvmahpkvancAAIgVPDERSGEAVklfVVARDPGLSVEELKAY---------------CKENFTGYKVPKHIVLRDSL 545
                         570
                  ....*....|...
gi 166797876 2249 PLTSNGKINKKGL 2261
Cdd:PRK12492  546 PMTPVGKILRREL 558
PRK08308 PRK08308
acyl-CoA synthetase; Validated
3664-3783 2.77e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 72.38  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3664 DRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS 3743
Cdd:PRK08308  290 DKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPV 369
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 166797876 3744 ELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPA 3783
Cdd:PRK08308  370 QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
4359-4818 2.87e-12

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 72.94  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4359 TYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLP-----IDPELPE-----KRRAFMLKDS 4428
Cdd:cd17642    46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPtndiyNERELDHslnisKPTIVFCSKK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4429 GADVLLTCAGHAipPLFEGeVLLLDDPLLYQG---------RTDNLNLSCS---------ENDLMYVIYTSGTTGQPKGV 4490
Cdd:cd17642   126 GLQKVLNVQKKL--KIIKT-IIILDSKEDYKGyqclytfitQNLPPGFNEYdfkppsfdrDEQVALIMNSSGSTGLPKGV 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4491 QLEHKTMTNLLAYEQDHTQLrfDRVLQFAAMSFDVCYQEMFSALSSGG-------ILFIIGNEAKRDIRQLNDFvrthGI 4563
Cdd:cd17642   203 QLTHKNIVARFSHARDPIFG--NQIIPDTAILTVIPFHHGFGMFTTLGylicgfrVVLMYKFEEELFLRSLQDY----KV 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4564 QTAFL-PTAFLkllasekhyFEPFAECVD-------HIIAAGEQLIAtRMLRDMLAR--HQVTLHNHYGPSETHVVTMYT 4633
Cdd:cd17642   277 QSALLvPTLFA---------FFAKSTLVDkydlsnlHEIASGGAPLS-KEVGEAVAKrfKLPGIRQGYGLTETTSAILIT 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4634 vdPDTDQELQPIGK--PISNTEIFILNEAGTLQPvGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDL 4711
Cdd:cd17642   347 --PEGDDKPGAVGKvvPFFYAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKALIDKDGW------LHSGDI 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4712 ARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGqSDLYAYFTAEQS---LSISQLKEKL 4786
Cdd:cd17642   418 AYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHpkIFDAGVAGIPDEDA-GELPAAVVVLEAgktMTEKEVMDYV 496
                         490       500       510
                  ....*....|....*....|....*....|...
gi 166797876 4787 AGQI-PGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd17642   497 ASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
287-700 3.35e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 73.11  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  287 DHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDA------- 359
Cdd:PRK07768   28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTlrvigmi 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  360 DADVLLVQH---HLKNSLAFDG----PVIDLNDEASyhadcslLSPV-AGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNS 431
Cdd:PRK07768  108 GAKAVVVGEpflAAAPVLEEKGirvlTVADLLAADP-------IDPVeTGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  432 LQWKKAFFKHSPADRVLVLY-PYVFDAFILNFFG-PLISGATL-HLLPNEenketFAIQNAIKQERITH----------- 497
Cdd:PRK07768  181 AEAMFVAAEFDVETDVMVSWlPLFHDMGMVGFLTvPMYFGAELvKVTPMD-----FLRDPLLWAELISKyrgtmtaapnf 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  498 -FSTSPRLLKTMIEQmNREDFIHVQHVVVGGEQLETDTVEKL------HSLQPRIrINNEYGPTENSVVSTFHPVQ---- 566
Cdd:PRK07768  256 aYALLARRLRRQAKP-GAFDLSSLRFALNGAEPIDPADVEDLldagarFGLRPEA-ILPAYGMAEATLAVSFSPCGaglv 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  567 ----SADE-----------------QITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYlnrpeLTEEKFVE 625
Cdd:PRK07768  334 vdevDADLlaalrravpatkgntrrLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIP 408
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  626 hlHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVA-REDADGAKQLYA 700
Cdd:PRK07768  409 --AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAvRLDAGHSREGFA 482
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
3292-3781 3.43e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 72.73  E-value: 3.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3292 QAHRTPDNTAVVFE--GKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPS 3369
Cdd:PRK13390    6 HAQIAPDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3370 ERIRYILNDSSISVLLYCGKLQDDIGFSGTCIDLM-----EEHFYHEKDSSLA-----LSYQSSQlAYAIYTSGTTGKPK 3439
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAALDGLAAKVGADLPLRlsfggEIDGFGSFEAALAgagprLTEQPCG-AVMLYSSGTTGFPK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3440 GTL--IEHRQVIH---LIEGLSRQVYSAYDAELNIAMlAPYYFDASVQ--QMYASLlsGHTLFIVPKeivSDGAALCRYY 3512
Cdd:PRK13390  165 GIQpdLPGRDVDApgdPIVAIARAFYDISESDIYYSS-APIYHAAPLRwcSMVHAL--GGTVVLAKR---FDAQATLGHV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3513 RQHSIDITDGTPAHLKLLIAAGDlqgvtlqhlliggEALSKTTVNKLKQLFgeHGAAPGITNV---------------YG 3577
Cdd:PRK13390  239 ERYRITVTQMVPTMFVRLLKLDA-------------DVRTRYDVSSLRAVI--HAAAPCPVDVkhamidwlgpivyeyYS 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3578 PTE----TCVDaslfniecsSDAWARSQNYVpigkplGRN---RMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPEL 3650
Cdd:PRK13390  304 STEahgmTFID---------SPDWLAHPGSV------GRSvlgDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEK 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3651 TDE-KFVADPFvpedrMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVM-----------LNVPDIQEAAA 3718
Cdd:PRK13390  369 TAAaQHPAHPF-----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALtmhpavhdvavIGVPDPEMGEQ 443
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 3719 AALKDADDEyylcGYFAADKTIQ--ISELRKRMARhlpgYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK13390  444 VKAVIQLVE----GIRGSDELARelIDYTRSRIAH----YKAPRSVEFVDELPRTPTGKLVKGLL 500
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1919-2261 3.73e-12

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 72.88  E-value: 3.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKgvLIEHggltnyiwwAKEVYVKGEKANFPLY-----SSISFDLTVT--------SIFTPLVTGNAIIV 1985
Cdd:cd05928   179 IYFTSGTTGSPK--MAEH---------SHSSLGLGLKVNGRYWldltaSDIMWNTSDTgwiksawsSLFEPWIQGACVFV 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1986 YDGE--DKTALLESIVRDPrVDIIKLTPAHLQVLKEMNIADQT--AVRRMIVGGENLSTRlarsIHEQFEGR--IEICNE 2059
Cdd:cd05928   248 HHLPrfDPLVILKTLSSYP-ITTFCGAPTVYRMLVQQDLSSYKfpSLQHCVTGGEPLNPE----VLEKWKAQtgLDIYEG 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2060 YGPTETVVGCMIYRYDAAKdrreSVPIGTAAANTSIYVLDENMKPAPIGVPGEIYIS-----GAGVARGYLNRPELTAEK 2134
Cdd:cd05928   323 YGQTETGLICANFKGMKIK----PGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAAT 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2135 FVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQE-EVIKEAVVTAREDVHG-----FK 2208
Cdd:cd05928   399 IRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHpAVVESAVVSSPDPIRGevvkaFV 471
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2209 QLCAYYVSGGQTTAAR-LRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05928   472 VLAPQFLSHDPEQLTKeLQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
PRK09274 PRK09274
peptide synthase; Provisional
4340-4731 4.18e-12

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 72.62  E-value: 4.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4340 QQAERNPDHEAV----------MFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAF 4409
Cdd:PRK09274   14 RAAQERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4410 LPIDPELPEKRRAFMLKDSGADVLLTCA-GHAIPPLF---EGEVLLL---DDPLLYQGRT--------DNLNLSC---SE 4471
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAQPDAFIGIPkAHLARRLFgwgKPSVRRLvtvGGRLLWGGTTlatllrdgAAAPFPMadlAP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4472 NDLMYVIYTSGTTGQPKGVQLEHKTmtnllaYEQDHTQLRFDRVLQ--------FAAMS-FDVCYqemfsalssgGILFI 4542
Cdd:PRK09274  174 DDMAAILFTSGSTGTPKGVVYTHGM------FEAQIEALREDYGIEpgeidlptFPLFAlFGPAL----------GMTSV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4543 IGN-----EAKRDIRQLNDFVRTHGIQTAFLPTAFLKLLAsekhyfepfAECVDH---------IIAAGE----QLIAtr 4604
Cdd:PRK09274  238 IPDmdptrPATVDPAKLFAAIERYGVTNLFGSPALLERLG---------RYGEANgiklpslrrVISAGApvpiAVIE-- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4605 MLRDMLArHQVTLHNHYGPSET---HVVTMYTVDPDTDQELQP-----IGKPISNTEIFILN---------EAGTLQPVG 4667
Cdd:PRK09274  307 RFRAMLP-PDAEILTPYGATEAlpiSSIESREILFATRAATDNgagicVGRPVDGVEVRIIAisdapipewDDALRLATG 385
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 4668 IVGELCISGVSLARGYHNRESLTLETFVPHPyDSN--QRMyktGDLARYLPEGNIEYAGRRDHQVK 4731
Cdd:PRK09274  386 EIGEIVVAGPMVTRSYYNRPEATRLAKIPDG-QGDvwHRM---GDLGYLDAQGRLWFCGRKAHRVE 447
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
764-835 5.16e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 64.49  E-value: 5.16e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  764 APRNTIEELLASIWQEVLG--AERIGILDNFF-DFGGDSIKSIQVSSRLYQA-GYKVDMKHLFKHPSIAELSQFVA 835
Cdd:COG0236     1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLE 76
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3804-3862 5.76e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 63.74  E-value: 5.76e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876  3804 QLTAIWEDVLGL--EQVGIRDHFFEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQ 3862
Cdd:pfam00550    2 RLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1779-2175 6.70e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 71.90  E-value: 6.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1779 LFEEQSQRTPDQAAV--IDKDRQ-------LTYGELNKRANRLARTLRAKGVQTDQpVAIITRNSIESVVGILAVLKSGG 1849
Cdd:PRK05850    6 LLRERASLQPDDAAFtfIDYEQDpagvaetLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1850 AYVPIDPeyPQ-----DRIRYMLDDSQAGIVL----MQRDVRKQL-AYEGVTV-------LLDDESSyhqDGSDLAPiSD 1912
Cdd:PRK05850   85 IAVPLSV--PQggahdERVSAVLRDTSPSVVLttsaVVDDVTEYVaPQPGQSAppvievdLLDLDSP---RGSDARP-RD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1913 VSHLAYVIYTSGSTGRPKGVLIEHGGLT-NYIWWAKEVYvkGEKANFPlyssiSFDLTVTS-------------IFTPLV 1978
Cdd:PRK05850  159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIaNFEQLMSDYF--GDTGGVP-----PPDTTVVSwlpfyhdmglvlgVCAPIL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 TGnaiivydgedKTALLESIV----RdprvdiikltPAH-LQVLKEM--------NIADQTAVRR--------------- 2030
Cdd:PRK05850  232 GG----------CPAVLTSPVaflqR----------PARwMQLLASNphafsaapNFAFELAVRKtsdddmagldlggvl 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2031 -MIVGGENLSTRLARSIHEQFeGRIEICNE-----YGPTETVV---------GCMIYRYDAAK------DRRES------ 2083
Cdd:PRK05850  292 gIISGSERVHPATLKRFADRF-APFNLRETairpsYGLAEATVyvatrepgqPPESVRFDYEKlsaghaKRCETgggtpl 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2084 VPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKF---VDDPFE--PGAKMYKTGDLAkWLAD 2158
Cdd:PRK05850  371 VSYGSPRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtPEGPWLRTGDLG-FISE 449
                         490
                  ....*....|....*..
gi 166797876 2159 GNIEYAGRIDEQVKIRG 2175
Cdd:PRK05850  450 GELFIVGRIKDLLIVDG 466
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
404-744 6.81e-12

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 71.75  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 HLAYVIYTSGTTGKPKGVMVEHG-------GIVNSLQWKKaffkhspADRVLVLYPYVFDAFILNF-FGPLISGATLHLL 475
Cdd:cd05908   107 ELAFIQFSSGSTGDPKGVMLTHEnlvhnmfAILNSTEWKT-------KDRILSWMPLTHDMGLIAFhLAPLIAGMNQYLM 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  476 PNEE--NKETFAIQNAIKQeRITHFSTSPRLLKTMIEQMNRE-----DFIHVQHVVVGGEQLETDTVEKL------HSLQ 542
Cdd:cd05908   180 PTRLfiRRPILWLKKASEH-KATIVSSPNFGYKYFLKTLKPEkandwDLSSIRMILNGAEPIDYELCHEFldhmskYGLK 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  543 pRIRINNEYGPTENSVVSTFHPVQSADEQITI---------------------------GSPVANHQAYILGAHHQIQPI 595
Cdd:cd05908   259 -RNAILPVYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKILPD 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  596 GIPGELYVGGAGVARGYLNRPELTEEKFVEHLHVpgqkmyKTGDLArWLPDGRIEYLGRIDHQVKIRGYR---------- 665
Cdd:cd05908   338 GYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNvyphdieria 410
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  666 -----IEIGEVEAAMFNLENVREAAVVA-REDADGAKQLYAYyvgepsltAAQFREELSrELPNYMIpSRFIPLERIPLT 739
Cdd:cd05908   411 eelegVELGRVVACGVNNSNTRNEEIFCfIEHRKSEDDFYPL--------GKKIKKHLN-KRGGWQI-NEVLPIRRIPKT 480

                  ....*
gi 166797876  740 SNGKI 744
Cdd:cd05908   481 TSGKV 485
PRK05857 PRK05857
fatty acid--CoA ligase;
264-759 7.11e-12

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 71.96  E-value: 7.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  264 TVYQLFEEQAERTPENAAVKFKN--DHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYV 341
Cdd:PRK05857   15 TVLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  342 PLDPEYPKERLQYLLHDADADVLLVQHHLK---NSL-----AFDGPVIDLNDEASYHAdCSL------LSPVAGHSHLAY 407
Cdd:PRK05857   95 MADGNLPIAAIERFCQITDPAAALVAPGSKmasSAVpealhSIPVIAVDIAAVTRESE-HSLdaaslaGNADQGSEDPLA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 VIYTSGTTGKPKGVMV-------------EHGgiVNSLQWKKAFFKHSP--ADRVLVLYpyvfdaFILNFF---GPLISG 469
Cdd:PRK05857  174 MIFTSGTTGEPKAVLLanrtffavpdilqKEG--LNWVTWVVGETTYSPlpATHIGGLW------WILTCLmhgGLCVTG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  470 AtlhllpneenKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFI--HVQHVVVGGEQLETDTVEKLHSLQprIRI 547
Cdd:PRK05857  246 G----------ENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGSRAIAADVRFIEATG--VRT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  548 NNEYGPTENSVVSTFHPVQSAD----EQITIGSPVANHQAYIL--GAHHQIQPIGIP----GELYVGGAGVARGYLNRPE 617
Cdd:PRK05857  314 AQVYGLSETGCTALCLPTDDGSivkiEAGAVGRPYPGVDVYLAatDGIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  618 LTEEKFVEhlhvpgqKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREA------------- 684
Cdd:PRK05857  394 RTAEVLID-------GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAacyeipdeefgal 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  685 ---AVVAREDADGAkqlyayyvGEPSLT---AAQFReelsRELPNYMIPSRFIPLERIPLTSNGKIDLKALPAADENTRA 758
Cdd:PRK05857  467 vglAVVASAELDES--------AARALKhtiAARFR----RESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKA 534

                  .
gi 166797876  759 E 759
Cdd:PRK05857  535 R 535
PLN03102 PLN03102
acyl-activating enzyme; Provisional
4321-4818 7.17e-12

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 71.97  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4321 NDTAVAE-KRIPTTIHQLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGI 4399
Cdd:PLN03102    2 DNLALCEaNNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4400 LAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLTcaGHAIPPLFEgEVLLL---DD-----PLLYQGRTD-------- 4463
Cdd:PLN03102   82 FAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV--DRSFEPLAR-EVLHLlssEDsnlnlPVIFIHEIDfpkrpsse 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4464 NLNLSC-------------------SENDLMYVIYTSGTTGQPKGVQLEHK-----TMTNLLAYEQDhtqlRFDRVLQFA 4519
Cdd:PLN03102  159 ELDYECliqrgeptpslvarmfriqDEHDPISLNYTSGTTADPKGVVISHRgaylsTLSAIIGWEMG----TCPVYLWTL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4520 AMSFDVCYQEMFSALSSGGILFIIGNEAKRDIRQlndFVRTHGI-QTAFLPTAFLKLLASEKHYFEPFAECVdHIIAAGE 4598
Cdd:PLN03102  235 PMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYK---NIEMHNVtHMCCVPTVFNILLKGNSLDLSPRSGPV-HVLTGGS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4599 QLIATRMLRDMLARHQVtLHNhYGPSETHVVTMY-------TVDPDTDQ-ELQPiGKPISN---TEIFILNEAgTLQPV- 4666
Cdd:PLN03102  311 PPPAALVKKVQRLGFQV-MHA-YGLTEATGPVLFcewqdewNRLPENQQmELKA-RQGVSIlglADVDVKNKE-TQESVp 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4667 ---GIVGELCISGVSLARGYHNRESLTLETFvPHPYdsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVE 4743
Cdd:PLN03102  387 rdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGW------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4744 AALLKH--VQEA-----------------VVLAKENTDGQSDLYAYFTAEQSLsISQLKEKLagqiPGYMIPSYFIQLEK 4804
Cdd:PLN03102  460 NVLYKYpkVLETavvamphptwgetpcafVVLEKGETTKEDRVDKLVTRERDL-IEYCRENL----PHFMCPRKVVFLQE 534
                         570
                  ....*....|....
gi 166797876 4805 LPLTGNGKVNRRAL 4818
Cdd:PLN03102  535 LPKNGNGKILKPKL 548
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
406-673 7.44e-12

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 71.77  E-value: 7.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  406 AYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyVFDAFILNFFG--PLISGATLHLLPNEENKET 483
Cdd:PRK06334  186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLP-PFHAYGFNSCTlfPLLSGVPVVFAYNPLYPKK 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  484 faIQNAIKQERITHFSTSPRLLKTMIEQMNRED--FIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTENSVVST 561
Cdd:PRK06334  265 --IVEMIDEAKVTFLGSTPVFFDYILKTAKKQEscLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVIT 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  562 FHPVQSADEQITIGSPVANHQAYILGAHHQIQ-PIGIPGELYVGGAGVARGYLNRPEltEEKFVehlHVPGQKMYKTGDL 640
Cdd:PRK06334  343 INTVNSPKHESCVGMPIRGMDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLGEDF--GQGFV---ELGGETWYVTGDL 417
                         250       260       270
                  ....*....|....*....|....*....|...
gi 166797876  641 ARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEA 673
Cdd:PRK06334  418 GYVDRHGELFLKGRLSRFVKIGAEMVSLEALES 450
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
1797-2261 7.71e-12

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 71.30  E-value: 7.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1797 DRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAgivl 1876
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKA---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 mqrdvrKQLAYEGVTvLLDDESSYHQDGSDLAPISDVshLAYvIYTSGSTGRPKGVLIEHgglTNYIWWAKEVYvKGEKA 1956
Cdd:cd05939    77 ------KALIFNLLD-PLLTQSSTEPPSQDDVNFRDK--LFY-IYTSGTTGLPKAAVIVH---SRYYRIAAGAY-YAFGM 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1957 N--------FPLY----------SSISFDLTV--------TSIFTPLVTGNAIIV-YDGEDKTALLESIVRDprvdiikl 2009
Cdd:cd05939   143 RpedvvydcLPLYhsaggimgvgQALLHGSTVvirkkfsaSNFWDDCVKYNCTIVqYIGEICRYLLAQPPSE-------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2010 tpahlqvlkemniADQTAVRRMIVGgenlsTRLARSIHEQFEGRI---EICNEYGPTETvvGCMIYRYDAAkdrresvpI 2086
Cdd:cd05939   215 -------------EEQKHNVRLAVG-----NGLRPQIWEQFVRRFgipQIGEFYGATEG--NSSLVNIDNH--------V 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2087 GTAAANT----SIY------VLDENMKP--APIGV-----PGEiyiSGAGVAR-----------GYLNRPElTAEKFVDD 2138
Cdd:cd05939   267 GACGFNSrilpSVYpirlikVDEDTGELirDSDGLcipcqPGE---PGLLVGKiiqndplrrfdGYVNEGA-TNKKIARD 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2139 PFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTARE--DVHGFKQLCAYYVS 2216
Cdd:cd05939   343 VFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvpGVEGRAGMAAIVDP 422
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 166797876 2217 GGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:cd05939   423 ERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3422-3775 8.19e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 70.59  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3422 SSQLAYAIYTSGTTGKPKgtLIEHRQvihlieglSRQVYSAYDAELNI------AMLAP---YYFDASVQQMYASLLSG- 3491
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPK--LAQHTH--------SNEVYNAWMLALNSlfdpddVLLCGlplFHVNGSVVTLLTPLASGa 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3492 HTLFIVP-----KEIVSDGAALCRYYRQHSIDitdGTPAHLKLLIAA-GDLQGVTLQHLLIGGEALSKTTVNKlkqlFGE 3565
Cdd:cd05944    71 HVVLAGPagyrnPGLFDNFWKLVERYRITSLS---TVPTVYAALLQVpVNADISSLRFAMSGAAPLPVELRAR----FED 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3566 HGAAPgITNVYGPTE-TCVDAslfnieCSSDAWARSQNYVPIGKPLGRNRMYILDSKKRLQ-PKGVQ--GELYIAGDGVG 3641
Cdd:cd05944   144 ATGLP-VVEGYGLTEaTCLVA------VNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLrDCAPDevGEICVAGPGVF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3642 RGYLNlPELTDEKFVADPFVpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAAL 3721
Cdd:cd05944   217 GGYLY-TEGNKNAFVADGWL------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQ 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3722 KDADDEYYLCGY--FAADKTIQISELRKRMARHLPGY-MIPAHFVQLDKMPLTPNGK 3775
Cdd:cd05944   290 PDAHAGELPVAYvqLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGK 346
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
288-655 9.14e-12

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 71.62  E-value: 9.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  288 HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ 367
Cdd:cd05933     8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  368 H---------------HLKNSLAFDGPV-------------IDLNDEASYHADCSLLSPVAGhSHLAYVIYTSGTTGKPK 419
Cdd:cd05933    88 NqkqlqkilqiqdklpHLKAIIQYKEPLkekepnlyswdefMELGRSIPDEQLDAIISSQKP-NQCCTLIYTSGTTGMPK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  420 GVMVEH-------GGIVNSLQWKKAFFKHspadRVLVLY-PYVFDAF-ILNFFGPLISGATLHL---------LPN---- 477
Cdd:cd05933   167 GVMLSHdnitwtaKAASQHMDLRPATVGQ----ESVVSYlPLSHIAAqILDIWLPIKVGGQVYFaqpdalkgtLVKtlre 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  478 -----------------EENKETFAI------------------QNAIKQERITHFSTSPRLLKTMIEQMNRED--FIHV 520
Cdd:cd05933   243 vrptafmgvprvwekiqEKMKAVGAKsgtlkrkiaswakgvgleTNLKLMGGESPSPLFYRLAKKLVFKKVRKAlgLDRC 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  521 QHVVVGGEQLETDTVEKLHSLQprIRINNEYGPTENSVVSTFHpVQSADEQITIGSPVANHQAYIlgahHQIQPIGIpGE 600
Cdd:cd05933   323 QKFFTGAAPISRETLEFFLSLN--IPIMELYGMSETSGPHTIS-NPQAYRLLSCGKALPGCKTKI----HNPDADGI-GE 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  601 LYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGRI 655
Cdd:cd05933   395 ICFWGRHVFMGYLNMEDKTEEAIDEDgwLH--------SGDLGKLDEDGFLYITGRI 443
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
403-744 2.04e-11

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 70.54  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  403 SHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYV-FDAFILNFFGPLISGATLHL----LPN 477
Cdd:PTZ00237  254 SHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIgWVSFHGFLYGSLSLGNTFVMfeggIIK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  478 EENKETFaIQNAIKQERITHFSTSPRLLKTMI------EQMNRE-DFIHVQHVVVGGEQLETDTVEKLHSlQPRIRINNE 550
Cdd:PTZ00237  334 NKHIEDD-LWNTIEKHKVTHTLTLPKTIRYLIktdpeaTIIRSKyDLSNLKEIWCGGEVIEESIPEYIEN-KLKIKSSRG 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  551 YGPTENSVVSTFHPVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVG---GAGVARGYLNRPELTEEKFVEHl 627
Cdd:PTZ00237  412 YGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKF- 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  628 hvPGqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV---- 703
Cdd:PTZ00237  491 --PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVlkqd 566
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876  704 -GEPSLTAAQFREE----LSRELPNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PTZ00237  567 qSNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKI 612
PRK07514 PRK07514
malonyl-CoA synthase; Validated
4337-4818 2.50e-11

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 69.90  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4337 LFEQQAERNPDHEAVMF---GNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPID 4413
Cdd:PRK07514    5 LFDALRAAFADRDAPFIetpDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4414 -----PELpekrrAFMLKDSGADVLLtCAGH---AIPPLFE----GEVLLLDD----PLLYQGR---TDNLNLSCSENDL 4474
Cdd:PRK07514   85 taytlAEL-----DYFIGDAEPALVV-CDPAnfaWLSKIAAaagaPHVETLDAdgtgSLLEAAAaapDDFETVPRGADDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4475 MYVIYTSGTTGQPKGVQLEHKtmtNLLAYEQ---DHTQLRFDRVLQFAAMSFDVcyQEMFSA-----LSSGGILFIIGNE 4546
Cdd:PRK07514  159 AAILYTSGTTGRSKGAMLSHG---NLLSNALtlvDYWRFTPDDVLIHALPIFHT--HGLFVAtnvalLAGASMIFLPKFD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4547 AKRDIRQLNDfvrthgiQTAFL--PTAFLKLLASEKhyFEPfaECVDHI---IAAGEQLIA-TRmlRDMLARHQVTLHNH 4620
Cdd:PRK07514  234 PDAVLALMPR-------ATVMMgvPTFYTRLLQEPR--LTR--EAAAHMrlfISGSAPLLAeTH--REFQERTGHAILER 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4621 YGPSEThvvTMYTVDP-DTDQELQPIGKPISNTEIFILN-EAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHP 4698
Cdd:PRK07514  301 YGMTET---NMNTSNPyDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4699 YdsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAAL--LKHVQE----------------AVVLAKEN 4760
Cdd:PRK07514  378 F------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIdeLPGVVEsavigvphpdfgegvtAVVVPKPG 451
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4761 tdgqsdlyayftaeQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK07514  452 --------------AALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
256-742 3.43e-11

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 69.79  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  256 VRDFSGSRTVYQLFEEQaertpenaavkfknDHLTYRELNEKASRLARTLR-NCGVQPDTLVAILADRSLEMIVSIIAVW 334
Cdd:cd17632    49 VTDPATGRTTLRLLPRF--------------ETITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALT 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  335 KAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH-HLKNSLA-------------FDG---------------------- 378
Cdd:cd17632   115 RLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAeHLDLAVEavleggtpprlvvFDHrpevdahraalesarerlaavg 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  379 -PVIDLNDEASYHADCSLLSPVAGHSH---LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLY-PY 453
Cdd:cd17632   195 iPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFmPM 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  454 VFDAFILNFFGPLISGATLHLLPNEENKETFaiqNAIKQERITHFSTSPRLLKTMIEQMNREdfihVQHVVVGGEQLETD 533
Cdd:cd17632   275 SHIAGRISLYGTLARGGTAYFAAASDMSTLF---DDLALVRPTELFLVPRVCDMLFQRYQAE----LDRRSVAGADAETL 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  534 TVEKLHSLQPR-----------------------------IRINNEYGPTENSVVSTFHPVQSAdeqitigsPVANHQAy 584
Cdd:cd17632   348 AERVKAELRERvlggrllaavcgsaplsaemkafmeslldLDLHDGYGSTEAGAVILDGVIVRP--------PVLDYKL- 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  585 ilgahhqiqpIGIP-------------GELYVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGD-LARWLPDgRIE 650
Cdd:cd17632   419 ----------VDVPelgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDE------DGFYRTGDvMAELGPD-RLV 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  651 YLGRIDHQVKI-RGYRIEIGEVEAAMFNLENVRE-------------AAVVAREDADGAkqlyayyvGEPSLTAAQFREE 716
Cdd:cd17632   482 YVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQifvygnserayllAVVVPTQDALAG--------EDTARLRAALAES 553
                         570       580       590
                  ....*....|....*....|....*....|..
gi 166797876  717 LSR-----ELPNYMIPSRFIpLERIPLT-SNG 742
Cdd:cd17632   554 LQRiareaGLQSYEIPRDFL-IETEPFTiANG 584
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1919-2254 4.39e-11

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 68.10  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKGVLIEHGGL----TNYIW----WAKEVYVkgekANFPLY--SSISFDLTV-----TSIFTPLVtgnai 1983
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALlaqaLVLAVlqaiDEGTVFL----NSGPLFhiGTLMFTLATfhaggTNVFVRRV----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1984 ivydgeDKTALLESIVRDpRVDIIKLTPAHLQVLKEMNIAdqtavrrmivGGENLSTRLARSIHEQFEGRIEICNE---- 2059
Cdd:cd17636    76 ------DAEEVLELIEAE-RCTHAFLLPPTIDQIVELNAD----------GLYDLSSLRSSPAAPEWNDMATVDTSpwgr 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2060 ----YGPTEtVVGCMIYrydAAKDRRESVPIGTAAANTSIYVLDENMKPAPIGVPGEIYISGAGVARGYLNRPELTAEKF 2135
Cdd:cd17636   139 kpggYGQTE-VMGLATF---AALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2136 VDdpfepgaKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV 2215
Cdd:cd17636   215 RG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVV 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 166797876 2216 --SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNG 2254
Cdd:cd17636   288 lkPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
PRK07514 PRK07514
malonyl-CoA synthase; Validated
3288-3706 7.68e-11

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 68.36  E-value: 7.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3288 LFEEQAHRTPDNTAVVFE---GKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPID 3364
Cdd:PRK07514    5 LFDALRAAFADRDAPFIEtpdGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3365 PDSPSERIRYILNDSSISVLLYCGKLQDDIG-----------------FSGTCIDLMEehfyHEKDSSLALSYQSSQLAY 3427
Cdd:PRK07514   85 TAYTLAELDYFIGDAEPALVVCDPANFAWLSkiaaaagaphvetldadGTGSLLEAAA----AAPDDFETVPRGADDLAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3428 AIYTSGTTGKPKGTLIEHRQVihliegLSrqvysaydaelNIAMLAPYY--------------------FDASvqqmYAS 3487
Cdd:PRK07514  161 ILYTSGTTGRSKGAMLSHGNL------LS-----------NALTLVDYWrftpddvlihalpifhthglFVAT----NVA 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3488 LLSGHTLFIVPKeivSDGAALcryyrqhsiditdgtpahLKLLIAAGDLQGV-TLQHLLIGGEALSKTTVNKLKqLFGEh 3566
Cdd:PRK07514  220 LLAGASMIFLPK---FDPDAV------------------LALMPRATVMMGVpTFYTRLLQEPRLTREAAAHMR-LFIS- 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3567 GAAP---------------GITNVYGPTETCVDASlfNiECSSDAWARSqnyvpIGKPLGRNRMYILDSK--KRLqPKGV 3629
Cdd:PRK07514  277 GSAPllaethrefqertghAILERYGMTETNMNTS--N-PYDGERRAGT-----VGFPLPGVSLRVTDPEtgAEL-PPGE 347
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3630 QGELYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESV 3706
Cdd:PRK07514  348 IGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGE 418
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
670-743 7.90e-11

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 61.02  E-value: 7.90e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876   670 EVEAAMFNLENVREAAVVAREDADGAKQLYAYYV--GEPSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGK 743
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
2182-2255 8.72e-11

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 60.64  E-value: 8.72e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  2182 EIEAALLQEEVIKEAVVTAREDVHGFKQLCAYYV--SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGK 2255
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
5111-5344 1.01e-10

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 68.94  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  5111 LPSFELPKDFARPPVRSFDGKRHNFTLDKtvtqgiKQLEELTGSTAYMILFSAYSILLAKYSGQDDIVVGTpiagRPHAD 5190
Cdd:TIGR03443    9 PTLSVLPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT----SSNKS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  5191 LEPIIgmfvntlaIRTAPMAEKTFLDYITETKETMLKAFEHQEYPFEELVEKLGVKRDLSRNP-LFDTMFVlqntEQTDI 5269
Cdd:TIGR03443   79 GRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAFQ----DAPDN 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  5270 EVDSLAvrpyeqteTAAKFDLQLNFLIDQDEIQGSFDYCTKLFKKKTIAVLAKDYVMILSAIMRNPSIPLKDIQL 5344
Cdd:TIGR03443  147 QQTTYS--------TGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSL 213
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
4471-4818 1.04e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 68.30  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4471 ENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLAYEQdhTQLRF------DRVLQFA----AMSFDVCyqEMFSALSSGGIL 4540
Cdd:PRK06334  182 PEDVAVILFTSGTEKLPKGVPLTHA---NLLANQR--ACLKFfspkedDVMMSFLppfhAYGFNSC--TLFPLLSGVPVV 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4541 FIIGNEAKRDIRQLNDfvRTHGIQTAFLPTAFLKLLASEKHYfEPFAECVDHIIAAGEQLIATrmLRDMLARH--QVTLH 4618
Cdd:PRK06334  255 FAYNPLYPKKIVEMID--EAKVTFLGSTPVFFDYILKTAKKQ-ESCLPSLRFVVIGGDAFKDS--LYQEALKTfpHIQLR 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4619 NHYGPSE-THVVTMYTVDPDTDQELqpIGKPISNTEIFILNEAgTLQPV--GIVGELCISGVSLARGY------HNRESL 4689
Cdd:PRK06334  330 QGYGTTEcSPVITINTVNSPKHESC--VGMPIRGMDVLIVSEE-TKVPVssGETGLVLTRGTSLFSGYlgedfgQGFVEL 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4690 TLETFvphpydsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKHV-----QEAVVLAKENTDGQ 4764
Cdd:PRK06334  407 GGETW-----------YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFgqnaaDHAGPLVVCGLPGE 475
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 4765 SDLYAYFTAeQSLSISQLKEKLAG-QIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK06334  476 KVRLCLFTT-FPTSISEVNDILKNsKTSSILKISYHHQVESIPMLGTGKPDYCSL 529
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
3426-3781 1.21e-10

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 66.99  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3426 AYAIYTSGTTGKPKGTLiehrqvihLIEGLSRQVYSAYDAELN------IAMlaPYYFDASVQQMYASLLSGhtlfIVPK 3499
Cdd:PRK07824   38 ALVVATSGTTGTPKGAM--------LTAAALTASADATHDRLGgpgqwlLAL--PAHHIAGLQVLVRSVIAG----SEPV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3500 EI-VSDG---AALCRYYRQHSID--ITDGTPAhlKLLIAAGDLQGV----TLQHLLIGGEALSKTTVNKLKQLfgehgaa 3569
Cdd:PRK07824  104 ELdVSAGfdpTALPRAVAELGGGrrYTSLVPM--QLAKALDDPAATaalaELDAVLVGGGPAPAPVLDAAAAA------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3570 pGITNV--YGPTETCVDaslfnieCSSDawarsqnyvpiGKPLGRNRMYILDskkrlqpkgvqGELYIAGDGVGRGYLNL 3647
Cdd:PRK07824  175 -GINVVrtYGMSETSGG-------CVYD-----------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNP 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3648 PEltdekfvADPFVpEDRMYRTGDLArLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEaaaaalkdadde 3727
Cdd:PRK07824  225 VD-------PDPFA-EPGWFRTDDLG-ALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVAD------------ 283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 3728 yylCGYF-----------------AADKTIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:PRK07824  284 ---CAVFglpddrlgqrvvaavvgDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
284-731 1.27e-10

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 67.70  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  284 FKNDHLTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADAD 362
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  363 VLLVQHHLKNSLAFDGP--------------------VIDLNDEASYHAD----CSLLSPVAGHSHLAYvIYTSGTTGKP 418
Cdd:cd05938    81 VLVVAPELQEAVEEVLPalradgvsvwylshtsntegVISLLDKVDAASDepvpASLRAHVTIKSPALY-IYTSGTTGLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  419 KGVMVEHGGIvnslqWKKAFFKHS---PADRV--LVLYPYVFDAFILNFFGPLISGATLHLlpneenKETF-AIQ--NAI 490
Cdd:cd05938   160 KAARISHLRV-----LQCSGFLSLcgvTADDViyITLPLYHSSGFLLGIGGCIELGATCVL------KPKFsASQfwDDC 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  491 KQERITHFSTSPRLLKTMIEQMNR-EDFIHVQHVVVgGEQLETDTVEKLHSLQPRIRINNEYGPTENSV----------- 558
Cdd:cd05938   229 RKHNVTVIQYIGELLRYLCNQPQSpNDRDHKVRLAI-GNGLRADVWREFLRRFGPIRIREFYGSTEGNIgffnytgkiga 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  559 ---VSTFHPVQSADEQI----TIGSPVANHQAYILGAhhqiqPIGIPGELyvggagVAR--------GYLNRPELTEEKF 623
Cdd:cd05938   308 vgrVSYLYKLLFPFELIkfdvEKEEPVRDAQGFCIPV-----AKGEPGLL------VAKitqqspflGYAGDKEQTEKKL 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  624 VEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVRE-----------------AAV 686
Cdd:cd05938   377 LRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEvnvygvtvpghegrigmAAV 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876  687 VAREDA--DGaKQLYAYyvgepsltaaqfreeLSRELPNYMIPsRFI 731
Cdd:cd05938   457 KLKPGHefDG-KKLYQH---------------VREYLPAYARP-RFL 486
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
2370-2567 1.52e-10

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 67.29  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2370 WFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFrTTENGCEAQNEEIAQSGLYRLEVMNLKEDPD 2449
Cdd:cd19538    12 WFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVF-PEEDGVPYQLILEEDEATPKLEIKEVDEEEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2450 PGRTIEAkadeIQSSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVI---QLPQK 2525
Cdd:cd19538    91 ESEINEA----VRYPFDLSEEPPFRATLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPelaPLPVQ 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876 2526 TDSFQLWAKRLSEYA--QSETIKQEQEYWTKI-----EQTEvkpLPKDF 2567
Cdd:cd19538   167 YADYALWQQELLGDEsdPDSLIARQLAYWKKQlaglpDEIE---LPTDY 212
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1320-1631 1.60e-10

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 67.13  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKgmlfhslfdpnsgAYF-----QQTM----------FDLHgDLEIDSFSKSLDGLSQKYDIFRTNFYrgwKDQP 1384
Cdd:cd19535     3 PLTDVQY-------------AYWigrqdDQELggvgchayleFDGE-DLDPDRLERAWNKLIARHPMLRAVFL---DDGT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1385 LQIIFKTKKIGFQFNDLREMKESQKEAMIQKYaREdKM--RGFDLEKGAL--MRLFILrtDEKTYRFIWSFHHILMDGWC 1460
Cdd:cd19535    66 QQILPEVPWYGITVHDLRGLSEEEAEAALEEL-RE-RLshRVLDVERGPLfdIRLSLL--PEGRTRLHLSIDLLVADALS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1461 LPLITKEIFENYfaLLQQKQPEQSSITpYSQYIEWLGRQDA---KEAAAYWDQYLEGYEEQTGLPkdhhAAEDgryvPEK 1537
Cdd:cd19535   142 LQILLRELAALY--EDPGEPLPPLELS-FRDYLLAEQALREtayERARAYWQERLPTLPPAPQLP----LAKD----PEE 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1538 VT--------CDISSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDV-----VFGsvvsgRPAGIPNVETMIGL 1604
Cdd:cd19535   211 IKeprftrreHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFllnltLFN-----RLPLHPDVNDVVGD 285
                         330       340
                  ....*....|....*....|....*..
gi 166797876 1605 FINTIPVRFRCEAGTTFAELMKEAQER 1631
Cdd:cd19535   286 FTSLLLLEVDGSEGQSFLERARRLQQQ 312
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
4473-4813 1.63e-10

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 66.37  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 DLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRF-DRVLQFAAMSFDVCYQEMF-SALSSGGILFiigNEAKRD 4550
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEdDRYLIINPFFHTFGYKAGIvACLLTGATVV---PVAVFD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4551 IRQLNDFVRTHGIqtAFLP---TAFLKLLAsekhyfEPFAECVDHII-------AAGEQLIATRMLRDMLARHQVTlhNH 4620
Cdd:cd17638    78 VDAILEAIERERI--TVLPgppTLFQSLLD------HPGRKKFDLSSlraavtgAATVPVELVRRMRSELGFETVL--TA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4621 YGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILNEagtlqpvgivGELCISGVSLARGYHNRESLTLETFvphpyD 4700
Cdd:cd17638   148 YGLTEAGVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI-----D 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4701 SNQRMYkTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVLAKENTDGQSDlYAYFTAEQSL 4777
Cdd:cd17638   213 ADGWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHpgvAQVAVIGVPDERMGEVG-KAFVVARPGV 290
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 166797876 4778 SISQ------LKEKLAgqipGYMIPSYFIQLEKLPLTGNGKV 4813
Cdd:cd17638   291 TLTEedviawCRERLA----NYKVPRFVRFLDELPRNASGKV 328
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
4356-4812 1.77e-10

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 66.99  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:cd05940     2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 caghaipplfegevllldDPLLYqgrtdnlnlscsendlmyvIYTSGTTGQPKGVQLEHKtmtnllayeqdhtqlRFDRV 4515
Cdd:cd05940    82 ------------------DAALY-------------------IYTSGTTGLPKAAIISHR---------------RAWRG 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4516 LQFAAMSF-----DVCYQEM------------FSALSSGGILfIIGNE--AK---RDIRQLNdfvrthgiqtaflPTAF- 4572
Cdd:cd05940   110 GAFFAGSGgalpsDVLYTCLplyhstalivgwSACLASGATL-VIRKKfsASnfwDDIRKYQ-------------ATIFq 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4573 -----LKLLASEKHYFEPFAECVDHIIAAGeqliatrmLR-----DMLARHQV-TLHNHYGPSEThVVTMYTVDPDT--- 4638
Cdd:cd05940   176 yigelCRYLLNQPPKPTERKHKVRMIFGNG--------LRpdiweEFKERFGVpRIAEFYAATEG-NSGFINFFGKPgai 246
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4639 --DQELQPIGKPIS------NTEIFILNEAGTLQPV--GIVGELC--ISGVSLARGYHNrESLTLETFVPHPYDSNQRMY 4706
Cdd:cd05940   247 grNPSLLRKVAPLAlvkydlESGEPIRDAEGRCIKVprGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWF 325
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4707 KTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKE--NTDGQSDLYAYFT-AEQSLSISQ 4781
Cdd:cd05940   326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFpgVEEANVYGVQvpGTDGRAGMAAIVLqPNEEFDLSA 405
                         490       500       510
                  ....*....|....*....|....*....|..
gi 166797876 4782 LKEKLAGQIPGYMIPsYFIQLEK-LPLTGNGK 4812
Cdd:cd05940   406 LAAHLEKNLPGYARP-LFLRLQPeMEITGTFK 436
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
266-681 1.91e-10

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 67.56  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  266 YQLFEEQAERTPENAAV--KFKNDH-------LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKA 336
Cdd:PLN02861   46 WQFFSDAVKKYPNNQMLgrRQVTDSkvgpyvwLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQ 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  337 GGAYVPLDPEYPKERLQYLLHDADADVLLVQH---------------HLKNSLAFDGPVIDLNDEA--------SYHADC 393
Cdd:PLN02861  126 GITYVPLYDTLGANAVEFIINHAEVSIAFVQEskissilsclpkcssNLKTIVSFGDVSSEQKEEAeelgvscfSWEEFS 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  394 SLLS-----PVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIV--------------NSLQWKKAFFKHSPA----DRVLVL 450
Cdd:PLN02861  206 LMGSldcelPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIaevlstdhllkvtdRVATEEDSYFSYLPLahvyDQVIET 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  451 Y---------------------------------PYVFDAFILNFFGPLISGATL--HLLPNEENKETFAIQNAIKQERi 495
Cdd:PLN02861  286 YciskgasigfwqgdirylmedvqalkptifcgvPRVYDRIYTGIMQKISSGGMLrkKLFDFAYNYKLGNLRKGLKQEE- 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  496 thfsTSPRLLKTMIEQMnREDFIHVQHVVVGGEQLETDTVEKLHSLQPRIRINNEYGPTEN------SVVSTFHPVQsad 569
Cdd:PLN02861  365 ----ASPRLDRLVFDKI-KEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEScggcftSIANVFSMVG--- 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  570 eqiTIGSPVANHQAYIlgahHQIQPIG------IP-GELYVGGAGVARGYLNRPELTEEKFVEhlhvpgqKMYKTGDLAR 642
Cdd:PLN02861  437 ---TVGVPMTTIEARL----ESVPEMGydalsdVPrGEICLRGNTLFSGYHKRQDLTEEVLID-------GWFHTGDIGE 502
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 166797876  643 WLPDGRIEYlgrIDHQVKIrgYRIEIGEVeAAMFNLENV 681
Cdd:PLN02861  503 WQPNGAMKI---IDRKKNI--FKLSQGEY-VAVENLENT 535
PRK05850 PRK05850
acyl-CoA synthetase; Validated
4330-4505 1.93e-10

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 67.27  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4330 IPTTIHQLFEQQaernPDHEAVMFGN---------QTLTYRQLNERSNQLARVLQDKGACTDQVVaVLTDRSAHMIIGIL 4400
Cdd:PRK05850    3 VPSLLRERASLQ----PDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4401 AILKAGAAFLPIDPELP---EKRRAFMLKDSGADVLLTCA--------------GHAIPPLFEGEVLLLDDPLLYQGRTD 4463
Cdd:PRK05850   78 GALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSavvddvteyvapqpGQSAPPVIEVDLLDLDSPRGSDARPR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 166797876 4464 NLNlscsenDLMYVIYTSGTTGQPKGVQLEHKtmtNLLA-YEQ 4505
Cdd:PRK05850  158 DLP------STAYLQYTSGSTRTPAGVMVSHR---NVIAnFEQ 191
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
1798-2198 1.95e-10

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 67.45  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLM 1877
Cdd:cd17641    10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1878 Q--------------------------RDVRK----------QLAYEGVTVLLDDESSYHQDGSDLAPiSDVSHLAYviy 1921
Cdd:cd17641    90 EdeeqvdklleiadripsvryviycdpRGMRKyddprlisfeDVVALGRALDRRDPGLYEREVAAGKG-EDVAVLCT--- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1922 TSGSTGRPKGVLIEHGGLTNYIWWAKEVYVKGEKANF----PLYSSISFDLTVTSiftPLVTGNaiIVYDGEDKTALL-- 1995
Cdd:cd17641   166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYvsvlPLPWIGEQMYSVGQ---ALVCGF--IVNFPEEPETMMed 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1996 ----------------ESIVRDPRVDIIKLTPAHLQVLKE-MNIADQTAVRRMIVGGENLSTRLARSIHEQFEGR----- 2053
Cdd:cd17641   241 lreigptfvllpprvwEGIAADVRARMMDATPFKRFMFELgMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRplrdr 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2054 ----------------------------IEICNEYGPTETVVGCMIYRydAAKDRRESVpiGTAAANTSIYVlDENmkpa 2105
Cdd:cd17641   321 lgfsrlrsaatggaalgpdtfrffhaigVPLKQLYGQTELAGAYTVHR--DGDVDPDTV--GVPFPGTEVRI-DEV---- 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2106 pigvpGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKI-RGYRIELGEIE 2184
Cdd:cd17641   392 -----GEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIE 460
                         490
                  ....*....|....
gi 166797876 2185 AALLQEEVIKEAVV 2198
Cdd:cd17641   461 NKLKFSPYIAEAVV 474
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
273-642 2.19e-10

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 67.07  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  273 AERTPENAAVKfkndhLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYP---- 348
Cdd:cd05921    15 AEREGNGGWRR-----VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsq 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  349 -KERLQYLL----------HDADAdvllVQHHLKNSLAFDGPVI----DLNDEASYHADCSLLSPV----------AGHS 403
Cdd:cd05921    90 dLAKLKHLFellkpglvfaQDAAP----FARALAAIFPLGTPLVvsrnAVAGRGAISFAELAATPPtaavdaafaaVGPD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 HLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHsPADRVLVL-----YPYVFDAFIlNFFGPLISGATLHLLPNE 478
Cdd:cd05921   166 TVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPF-FGEEPPVLvdwlpWNHTFGGNH-NFNLVLYNGGTLYIDDGK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  479 ENKETFA--IQNaIKQERITHFSTSPRLLKTMIEQMNRED------FIHVQHVVVGGEQLETDTVEKLHSLQ-----PRI 545
Cdd:cd05921   244 PMPGGFEetLRN-LREISPTVYFNVPAGWEMLVAALEKDEalrrrfFKRLKLMFYAGAGLSQDVWDRLQALAvatvgERI 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  546 RINNEYGPTENSVVSTFhPVQSADEQITIGSPVAnhqayilGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVE 625
Cdd:cd05921   323 PMMAGLGATETAPTATF-THWPTERSGLIGLPAP-------GTELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDE 394
                         410
                  ....*....|....*..
gi 166797876  626 hlhvpgQKMYKTGDLAR 642
Cdd:cd05921   395 ------EGFYCLGDAAK 405
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
1912-2270 2.32e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 67.07  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1912 DVSHLAYVIYTSGSTGRPKGVLIEHGGLT---NYIWWAkeVYVKGEKANFPLYSSISFDLTVTSIFTPLVTGNAIIVYDG 1988
Cdd:PTZ00237  252 ESSHPLYILYTSGTTGNSKAVVRSNGPHLvglKYYWRS--IIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEG 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1989 ------EDKTALLESIVRDpRVDIIKLTPAHLQVLKEM-----NIA---DQTAVRRMIVGGENLStrlaRSIHEQFEGRI 2054
Cdd:PTZ00237  330 giiknkHIEDDLWNTIEKH-KVTHTLTLPKTIRYLIKTdpeatIIRskyDLSNLKEIWCGGEVIE----ESIPEYIENKL 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2055 EIC--NEYGPTETvvGCM-IYRYDAAKDRRESVPIGTAAANTSIyvLDENMKPAPIGVPGEIYISgagvargyLNRPELT 2131
Cdd:PTZ00237  405 KIKssRGYGQTEI--GITyLYCYGHINIPYNATGVPSIFIKPSI--LSEDGKELNVNEIGEVAFK--------LPMPPSF 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2132 AEKFV--DDPFE------PGakMYKTGDLAkwLADGNIEYA--GRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAR 2201
Cdd:PTZ00237  473 ATTFYknDEKFKqlfskfPG--YYNSGDLG--FKDENGYYTivSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2202 EDVHGFKQLCAYYV-----SGGQTTAARLRKQ----LSQTLASYMVPAYFIELDEMPLTSNGKINK----KGLPAPDFEL 2268
Cdd:PTZ00237  549 YDPDCYNVPIGLLVlkqdqSNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRqiisKFLNDSNYQL 628

                  ..
gi 166797876 2269 QD 2270
Cdd:PTZ00237  629 PD 630
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
858-1114 2.42e-10

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 67.76  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  858 WFFEQKMPHAHHYN--QAVMLysaegfkEGPLR-----RTMERIASHHDALRMIFEKTPDGYAPRItgtDESELF-HLEV 929
Cdd:PRK10252   18 WMAEKLSPLPSAWSvaHYVEL-------TGELDapllaRAVVAGLAEADTLRMRFTEDNGEVWQWV---DPALTFpLPEI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  930 MNYKGETDP-AQAIADKANEIQSSMVLDKG-PLMKLGLFQCPDGDHLL-IAIHHLLIDGVSWRILLEDFASGYEQAERRQ 1006
Cdd:PRK10252   88 IDLRTQPDPhAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWyQRYHHLLVDGFSFPAITRRIAAIYCAWLRGE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1007 tiqlPQKTDSFPFWADQLSKYAAETDME---EEIAYWTEL-------SSIKPQPLPKDTISEgSLLRDseevTIQWTKEE 1076
Cdd:PRK10252  168 ----PTPASPFTPFADVVEEYQRYRASEawqRDAAFWAEQrrqlpppASLSPAPLPGRSASA-DILRL----KLEFTDGA 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 166797876 1077 TEQLLKQA--NRAYntdinDLLLTSLGLAVHKWTGTEDIV 1114
Cdd:PRK10252  239 FRQLAAQAsgVQRP-----DLALALVALWLGRLCGRMDYA 273
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
406-749 2.80e-10

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 67.04  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  406 AYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPyVFDAFILN--FFGPLISGATLHLLPNEENket 483
Cdd:PRK08043  368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALP-LFHSFGLTvgLFTPLLTGAEVFLYPSPLH--- 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  484 FAIQNAIKQER--ITHFSTSPrLLKTMIEQMNREDFIHVQHVVVGGEQLEtDTVEKLHSLQPRIRINNEYGPTENS-VVS 560
Cdd:PRK08043  444 YRIVPELVYDRncTVLFGTST-FLGNYARFANPYDFARLRYVVAGAEKLQ-ESTKQLWQDKFGLRILEGYGVTECApVVS 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  561 TFHPVqsADEQITIGSPVANHQAYILgahhQIQPIGIPGELYVGGAGVARGYL--NRPELTEEKFVEHLHvpGQK---MY 635
Cdd:PRK08043  522 INVPM--AAKPGTVGRILPGMDARLL----SVPGIEQGGRLQLKGPNIMNGYLrvEKPGVLEVPTAENAR--GEMergWY 593
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  636 KTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLyAYYVGEPSLTaaqfRE 715
Cdd:PRK08043  594 DTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEAL-VLFTTDSELT----RE 668
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 166797876  716 ELSRELPNYMIPSRFIP-----LERIPLTSNGKIDLKAL 749
Cdd:PRK08043  669 KLQQYAREHGVPELAVPrdiryLKQLPLLGSGKPDFVTL 707
PLN02614 PLN02614
long-chain acyl-CoA synthetase
290-681 2.91e-10

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 66.97  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  290 TYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQH- 368
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEk 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  369 --------------HLKNSLAFDGPVIDLNDEAS-----YHADCSLLS---------PVAGHSHLAYVIYTSGTTGKPKG 420
Cdd:PLN02614  161 kiselfktcpnsteYMKTVVSFGGVSREQKEEAEtfglvIYAWDEFLKlgegkqydlPIKKKSDICTIMYTSGTTGDPKG 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  421 VMVEHGGIVN--------------SLQWKKAFFKHSPA----DRVL--------------------------VLYPYVFD 456
Cdd:PLN02614  241 VMISNESIVTliagvirllksanaALTVKDVYLSYLPLahifDRVIeecfiqhgaaigfwrgdvklliedlgELKPTIFC 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  457 AfILNFFGPLISGATLHL-----LPNEENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNREDFIHVQHVVVGGEQLE 531
Cdd:PLN02614  321 A-VPRVLDRVYSGLQKKLsdggfLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLA 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  532 TDtVEKLHSLQPRIRINNEYGPTEnSVVSTFHPVQSADEQI-TIGSPVANHQAYILGA-HHQIQPIGIP--GELYVGGAG 607
Cdd:PLN02614  400 SH-VESFLRVVACCHVLQGYGLTE-SCAGTFVSLPDELDMLgTVGPPVPNVDIRLESVpEMEYDALASTprGEICIRGKT 477
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  608 VARGYLNRPELTEEKFVEH-LHvpgqkmykTGDLARWLPDGRIEYLGRidhqvKIRGYRIEIGEVeAAMFNLENV 681
Cdd:PLN02614  478 LFSGYYKREDLTKEVLIDGwLH--------TGDVGEWQPNGSMKIIDR-----KKNIFKLSQGEY-VAVENIENI 538
PLN03102 PLN03102
acyl-activating enzyme; Provisional
1772-2261 3.16e-10

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 66.58  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1772 PQTPVhQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAY 1851
Cdd:PLN03102   13 PLTPI-TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1852 VPIDPEYPQDRIRYMLDDSQAGIVLMQRDVrKQLAYEGVTVLLDDESS-------YHQDGSDLAPISDVSHLAYVI---- 1920
Cdd:PLN03102   92 NPINTRLDATSIAAILRHAKPKILFVDRSF-EPLAREVLHLLSSEDSNlnlpvifIHEIDFPKRPSSEELDYECLIqrge 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1921 ----------------------YTSGSTGRPKGVLIEHGG-----LTNYIWWakevyvkgEKANFPLY---------SSI 1964
Cdd:PLN03102  171 ptpslvarmfriqdehdpislnYTSGTTADPKGVVISHRGaylstLSAIIGW--------EMGTCPVYlwtlpmfhcNGW 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1965 SFDLTV-----TSIFTPLVTGNAIIvydgedKTALLESIVRdprvdiIKLTPAHLQVLKEMNIADQTAVR---RMIVGGE 2036
Cdd:PLN03102  243 TFTWGTaarggTSVCMRHVTAPEIY------KNIEMHNVTH------MCCVPTVFNILLKGNSLDLSPRSgpvHVLTGGS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2037 NLSTRLARSIhEQFEgrIEICNEYGPTETVVGCMIYRYDAAKDR-----------RESVPIGTAAAntsiyvLDENMKPA 2105
Cdd:PLN03102  311 PPPAALVKKV-QRLG--FQVMHAYGLTEATGPVLFCEWQDEWNRlpenqqmelkaRQGVSILGLAD------VDVKNKET 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2106 PIGVP------GEIYISGAGVARGYLNRPELTAEKFvddpfepGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIE 2179
Cdd:PLN03102  382 QESVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENIS 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2180 LGEIEAAL-LQEEVIKEAVVTAREDVHGfKQLCAYYV-SGGQTTAARLRKQL-----------SQTLASYMVPAYFIELD 2246
Cdd:PLN03102  455 SVEVENVLyKYPKVLETAVVAMPHPTWG-ETPCAFVVlEKGETTKEDRVDKLvtrerdlieycRENLPHFMCPRKVVFLQ 533
                         570
                  ....*....|....*
gi 166797876 2247 EMPLTSNGKINKKGL 2261
Cdd:PLN03102  534 ELPKNGNGKILKPKL 548
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1785-2263 3.69e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 66.20  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1785 QRTPDQA-AVIDKDRQLTYGE-LNKRANR--LARTLRAkgvqTDQP--VAIITRNSIESVVGILAVLKSGGAYVPIDP-- 1856
Cdd:PRK13388   11 DRAGDDTiAVRYGDRTWTWREvLAEAAARaaALIALAD----PDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTtr 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1857 ---EYPQDrIRYMldDSQagIVLMQRDVRKQLA---YEGVTVLLDDESSYHQ---DGSDLAPISDV--SHLAYVIYTSGS 1925
Cdd:PRK13388   87 rgaALAAD-IRRA--DCQ--LLVTDAEHRPLLDgldLPGVRVLDVDTPAYAElvaAAGALTPHREVdaMDPFMLIFTSGT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1926 TGRPKGVLIEHGGLtnyiwwAKEVYVKGEKanfplyssisFDLTVTSIF---TPLVTGNAI------IVYDGEdktalle 1996
Cdd:PRK13388  162 TGAPKAVRCSHGRL------AFAGRALTER----------FGLTRDDVCyvsMPLFHSNAVmagwapAVASGA------- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1997 SIVRDPRV-------DI-----------------IKLTPAH-------LQVL--KEMNIADQTAVRRmivggenlstrla 2043
Cdd:PRK13388  219 AVALPAKFsasgfldDVrrygatyfnyvgkplayILATPERpddadnpLRVAfgNEASPRDIAEFSR------------- 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2044 RSIHEQFEGrieicneYGPTETvvGCMIYRYDAAkdrresvP---IGTAAANTSIY-----------VLDENMKPA-PIG 2108
Cdd:PRK13388  286 RFGCQVEDG-------YGSSEG--AVIVVREPGT-------PpgsIGRGAPGVAIYnpetltecavaRFDAHGALLnADE 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2109 VPGEIY-ISGAGVARGYLNRPELTAEKFVDDpfepgakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAAL 2187
Cdd:PRK13388  350 AIGELVnTAGAGFFEGYYNNPEATAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERIL 422
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2188 LQEEVIKEAVVTAREDVHGFKQ-LCAYYVSGGQTT-----AARLRKQlsQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK13388  423 LRHPAINRVAVYAVPDERVGDQvMAALVLRDGATFdpdafAAFLAAQ--PDLGTKAWPRYVRIAADLPSTATNKVLKREL 500

                  ..
gi 166797876 2262 PA 2263
Cdd:PRK13388  501 IA 502
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
3424-3777 4.13e-10

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 66.87  E-value: 4.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3424 QLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSrQVYSAydaELNIAMLA--PYY--FDASVQQMYAsLLSGHTLFIVPK 3499
Cdd:PRK08633  783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQIS-DVFNL---RNDDVILSslPFFhsFGLTVTLWLP-LLEGIKVVYHPD 857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3500 EIvsDGAALCRYYRQHSIDITDGTPAHLKLLI---AAGDLQGVTLQHLLIGGEALSKTTVNKLKQLFGEHgaapgITNVY 3576
Cdd:PRK08633  858 PT--DALGIAKLVAKHRATILLGTPTFLRLYLrnkKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIR-----ILEGY 930
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3577 GPTETC--VDASLFNIECSSDAWARSQNYVPIGKPLGRNRMYILD--SKKRLQPkGVQGELYIAGDGVGRGYLNLPELTD 3652
Cdd:PRK08633  931 GATETSpvASVNLPDVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpeTFEELPP-GEDGLILIGGPQVMKGYLGDPEKTA 1009
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3653 EkFVADpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIES-------------VMLNVPDIQEAAAA 3719
Cdd:PRK08633 1010 E-VIKD--IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEelakalggeevvfAVTAVPDEKKGEKL 1086
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 3720 ALKDADDEyylcgyfaadktIQISELRKRMAR-HLPGYMIPAHFVQLDKMPLTPNGKLN 3777
Cdd:PRK08633 1087 VVLHTCGA------------EDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLD 1133
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
4356-4836 5.26e-10

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 66.18  E-value: 5.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGA-------AFLPidPELpekrrAFMLKDS 4428
Cdd:cd05967    81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAihsvvfgGFAA--KEL-----ASRIDDA 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4429 GADVLLTCA-----GHAIP--PLFEG----------EVLLLDDPLLYQGRTDNLN----------------LSCSENDLM 4475
Cdd:cd05967   154 KPKLIVTAScgiepGKVVPykPLLDKalelsghkphHVLVLNRPQVPADLTKPGRdldwsellakaepvdcVPVAATDPL 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4476 YVIYTSGTTGQPKGVQLE--------HKTMTNLLAYEQDHTqlrfdrvlqFAAMSfDV---------CYQEMFSALSSgg 4538
Cdd:cd05967   234 YILYTSGTTGKPKGVVRDngghavalNWSMRNIYGIKPGDV---------WWAAS-DVgwvvghsyiVYGPLLHGATT-- 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4539 ILFiignEAKR----DIRQLNDFVRTHGIQTAF-LPTAFLKLlasekHYFEPFAE--------CVDHIIAAGEQL----- 4600
Cdd:cd05967   302 VLY----EGKPvgtpDPGAFWRVIEKYQVNALFtAPTAIRAI-----RKEDPDGKyikkydlsSLRTLFLAGERLdpptl 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4601 -IATRMLRdmlarhqVTLHNHYGPSETH--VVTMYTvdpdtDQELQPI-----GKPISNTEIFILNEAGTLQPVGIVGEL 4672
Cdd:cd05967   373 eWAENTLG-------VPVIDHWWQTETGwpITANPV-----GLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNI 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4673 CISGvSLARG-----YHNRE---SLTLETFVPHpydsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEA 4744
Cdd:cd05967   441 VIKL-PLPPGclltlWKNDErfkKLYLSKFPGY--------YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4745 ALLKH---VQEAVVLAKENTDGQSDLyAYFTAEQSLSI---SQLKEKLA---GQIPGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:cd05967   512 SVLSHpavAECAVVGVRDELKGQVPL-GLVVLKEGVKItaeELEKELVAlvrEQIGPVAAFRLVIFVKRLPKTRSGKILR 590
                         570       580
                  ....*....|....*....|.
gi 166797876 4816 RALpmpeAGLQTGTDYVAPRT 4836
Cdd:cd05967   591 RTL----RKIADGEDYTIPST 607
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
3-230 5.52e-10

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 65.45  E-value: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    3 VFKTQETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYK 82
Cdd:cd19531   187 VLERQLAYWREQLAGAPPVLELP----TDRPRPAVQSFRGARVRFTLPAELTAALRALARREGATLFMTLLAAFQVLLHR 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   83 YTDRTSLILGIPTvskqkAGQSA----------VNNIVLlKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKM----- 147
Cdd:cd19531   263 YSGQDDIVVGTPV-----AGRNRaelegligffVNTLVL-RTDLSGDPTFRELLARVRETALEAYAHQDLPFEKLvealq 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  148 -ARHLSvqyndeHMPLIHTVVSLN------------EIHSLQCKEDTAtdtlfHFDL------ENNGIHLKLFYNGNLYD 208
Cdd:cd19531   337 pERDLS------RSPLFQVMFVLQnapaaalelpglTVEPLEVDSGTA-----KFDLtlslteTDGGLRGSLEYNTDLFD 405
                         250       260
                  ....*....|....*....|..
gi 166797876  209 ERYINQIVSHLDQLLSVILFQP 230
Cdd:cd19531   406 AATIERMAGHFQTLLEAIVADP 427
PRK07529 PRK07529
AMP-binding domain protein; Validated
3284-3775 5.85e-10

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 65.75  E-value: 5.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3284 TIHELFEEQAHRTPDNTAVVF--------EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLK 3355
Cdd:PRK07529   26 STYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3356 AGGAYlPIDPDSPSERIRYILNDSSISVLLYCGklqddiGFSGT--------------------CIDLME---------- 3405
Cdd:PRK07529  106 AGIAN-PINPLLEPEQIAELLRAAGAKVLVTLG------PFPGTdiwqkvaevlaalpelrtvvEVDLARylpgpkrlav 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3406 -------EHFYHEKDSSLALSY----------QSSQLAYAIYTSGTTGKPKgtLIEHRQvihlieglSRQVYSAYDAELN 3468
Cdd:PRK07529  179 plirrkaHARILDFDAELARQPgdrlfsgrpiGPDDVAAYFHTGGTTGMPK--LAQHTH--------GNEVANAWLGALL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3469 IA------MLAP---YYFDASVQQMYASLLSG-HTLFIVP-----KEIVSDGAALCRYYRqhsIDITDGTP----AHLKL 3529
Cdd:PRK07529  249 LGlgpgdtVFCGlplFHVNALLVTGLAPLARGaHVVLATPqgyrgPGVIANFWKIVERYR---INFLSGVPtvyaALLQV 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3530 LIAAGDLQgvTLQHLLIGGEALSkttVNkLKQLFGEHGAAPgITNVYGPTE-TCVDaslfniecssdawarSQNYV---- 3604
Cdd:PRK07529  326 PVDGHDIS--SLRYALCGAAPLP---VE-VFRRFEAATGVR-IVEGYGLTEaTCVS---------------SVNPPdger 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3605 ---PIGKPLGRNRMYI--LDSKKRLQ---PKGVQGELYIAGDGVGRGYLNlpeltDEKfVADPFVpEDRMYRTGDLARLL 3676
Cdd:PRK07529  384 rigSVGLRLPYQRVRVviLDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLE-----AAH-NKGLWL-EDGWLNTGDLGRID 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3677 PDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLCGY--FAADKTIQISELRKRMARHLP 3754
Cdd:PRK07529  457 ADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELLAFARDHIA 536
                         570       580
                  ....*....|....*....|..
gi 166797876 3755 G-YMIPAHFVQLDKMPLTPNGK 3775
Cdd:PRK07529  537 ErAAVPKHVRILDALPKTAVGK 558
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
264-751 6.03e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 65.82  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  264 TVYQLFEEQAERTpeNAAVKFKNDHLTYRE-LNEKASR--LARTLRNCGVQPDtlVAILADRSLEMIVSIIAVWKAGGAY 340
Cdd:PRK13388    4 TIAQLLRDRAGDD--TIAVRYGDRTWTWREvLAEAAARaaALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGYVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  341 VPLDPEYPKERLQYLLHDADADVLLV--QH-HLKNSLAFDG-PVIDLNDEA-----SYHADCSLLSPVaGHSHLAYVIYT 411
Cdd:PRK13388   80 VGLNTTRRGAALAADIRRADCQLLVTdaEHrPLLDGLDLPGvRVLDVDTPAyaelvAAAGALTPHREV-DAMDPFMLIFT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  412 SGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGP-LISGATLHLLPneenkeTFAIQN-- 488
Cdd:PRK13388  159 SGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALPA------KFSASGfl 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  489 -AIKQERITHFSTSPRLLKTMIEQMNR-EDFIHVQHVVVGGEQLETDTVEklHSLQPRIRINNEYGPTENSVVSTFHPVQ 566
Cdd:PRK13388  233 dDVRRYGATYFNYVGKPLAYILATPERpDDADNPLRVAFGNEASPRDIAE--FSRRFGCQVEDGYGSSEGAVIVVREPGT 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  567 SADeqiTIGSPVANHQAY-----------ILGAH-HQIQPIGIPGELY-VGGAGVARGYLNRPELTEEKfVEHlhvpgqK 633
Cdd:PRK13388  311 PPG---SIGRGAPGVAIYnpetltecavaRFDAHgALLNADEAIGELVnTAGAGFFEGYYNNPEATAER-MRH------G 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  634 MYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGEP--SLTAA 711
Cdd:PRK13388  381 MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDgaTFDPD 460
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 166797876  712 QFREELS--RELPNYMIPsRFIPL-ERIPLTSNGKIDLKALPA 751
Cdd:PRK13388  461 AFAAFLAaqPDLGTKAWP-RYVRIaADLPSTATNKVLKRELIA 502
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1776-2261 6.81e-10

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 65.67  E-value: 6.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1776 VHQLFEEQSQRTPDQAAVIDKDRQLTYGELNKRANRLARTLRAK-GVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPI 1854
Cdd:PRK08751   27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1855 DPEYPQDRIRYMLDDSQAGIVLMQRDVR------------KQLAYEGVTVLLDDESS----------------YHQDGS- 1905
Cdd:PRK08751  107 NPLYTPRELKHQLIDSGASVLVVIDNFGttvqqviadtpvKQVITTGLGDMLGFPKAalvnfvvkyvkklvpeYRINGAi 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1906 ----DLA-------PISDVSH--LAYVIYTSGSTGRPKGVLIEHGGL-------------TNYIWWAKEVYVKGekanFP 1959
Cdd:PRK08751  187 rfreALAlgrkhsmPTLQIEPddIAFLQYTGGTTGVAKGAMLTHRNLvanmqqahqwlagTGKLEEGCEVVITA----LP 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1960 LYSSisFDLTVTSIFTPLVTGNAIIVYDGEDKTALLESIVRDPRVDIIKL---------TPAHLQVlkemniaDQTAVRR 2030
Cdd:PRK08751  263 LYHI--FALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVntlfngllnTPGFDQI-------DFSSLKM 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2031 MIVGGenlsTRLARSIHEQFE--GRIEICNEYGPTETVVGCMIYRYDAaKDRRESvpIGTAAANTSIYVLDENMKPAPIG 2108
Cdd:PRK08751  334 TLGGG----MAVQRSVAERWKqvTGLTLVEAYGLTETSPAACINPLTL-KEYNGS--IGLPIPSTDACIKDDAGTVLAIG 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2109 VPGEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALL 2188
Cdd:PRK08751  407 EIGELCIKGPQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIA 480
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2189 QEEVIKEAVVTAREDVHGFKQLCAYYVSGGQT-TAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PRK08751  481 MMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPAlTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
274-748 7.18e-10

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 65.53  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  274 ERTPENAAVKfkndhLTYRELNEKASRLARTLRNCgVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPL-DPEYP--KE 350
Cdd:PRK12476   59 SHSAAGCAVE-----LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  351 RLQYLLHDADADVLL--------VQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVM 422
Cdd:PRK12476  133 RLDTALRDAEPTVVLtttaaaeaVEGFLRNLPRLRRPRVIAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  423 VEHGGI-VNSLQWKKAFFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLL--------PNEENKetfAIQNAIKQE 493
Cdd:PRK12476  213 ITHRAVgTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMsptafvrrPQRWIK---ALSEGSRTG 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  494 RIthFSTSPRLLKTMIEQMN---REDFIHVQHVV--VGGEQLETDTVEKLHSL-----QPRIRINNEYGPTENSV-VSTF 562
Cdd:PRK12476  290 RV--VTAAPNFAYEWAAQRGlpaEGDDIDLSNVVliIGSEPVSIDAVTTFNKAfapygLPRTAFKPSYGIAEATLfVATI 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  563 HPVQSAD------EQITIGSPV---ANHQAYILG------AHHQI-----------QPIGIPGELYVGGAGVARGYLNRP 616
Cdd:PRK12476  368 APDAEPSvvyldrEQLGAGRAVrvaADAPNAVAHvscgqvARSQWavivdpdtgaeLPDGEVGEIWLHGDNIGRGYWGRP 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  617 ELTEEKFVEHLHV------------PGQKMYKTGDLARWLpDGRIEYLGRIDHQVKIRGYR-----IEIGEVEA------ 673
Cdd:PRK12476  448 EETERTFGAKLQSrlaegshadgaaDDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNhypqdIEATVAEAspmvrr 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  674 ---AMFNLE-NVREAAVVAREDADGAKQlyayyvGEPSLTAAQFREELSRElpnYMIPS---RFIPLERIPLTSNGKIDL 746
Cdd:PRK12476  527 gyvTAFTVPaEDNERLVIVAERAAGTSR------ADPAPAIDAIRAAVSRR---HGLAVadvRLVPAGAIPRTTSGKLAR 597

                  ..
gi 166797876  747 KA 748
Cdd:PRK12476  598 RA 599
PRK08315 PRK08315
AMP-binding domain protein; Validated
3281-3446 8.68e-10

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 65.22  E-value: 8.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3281 REKTIHELFEEQAHRTPDNTAVVF--EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGG 3358
Cdd:PRK08315   14 LEQTIGQLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3359 AYLPIDPDSPSERIRYILNDSSISVLL---------YCGKLQDDIGFSGTCI--DLMEEHFYHEK--------------- 3412
Cdd:PRK08315   94 ILVTINPAYRLSELEYALNQSGCKALIaadgfkdsdYVAMLYELAPELATCEpgQLQSARLPELRrviflgdekhpgmln 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876 3413 -DSSLALSYQSSQLAYAI--------------YTSGTTGKPKGTLIEHR 3446
Cdd:PRK08315  174 fDELLALGRAVDDAELAArqatldpddpiniqYTSGTTGFPKGATLTHR 222
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
1800-2254 8.76e-10

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 65.17  E-value: 8.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKG-VQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGI---- 1874
Cdd:cd17632    68 ITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLlavs 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1875 ----------------------------VLMQRDV----RKQLAYEGVTVLLDDESSYHQDGSDLAPI----SDVSHLAY 1918
Cdd:cd17632   148 aehldlaveavleggtpprlvvfdhrpeVDAHRAAlesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLfrpePDDDPLAL 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1919 VIYTSGSTGRPKGVLIEHGGLTNYiwWAKevyVKGEKANFPLYSS------ISFDLTVTSIFTPLVTGNAIIVYDGEDKT 1992
Cdd:cd17632   228 LIYTSGSTGTPKGAMYTERLVATF--WLK---VSSIQDIRPPASItlnfmpMSHIAGRISLYGTLARGGTAYFAAASDMS 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1993 ALLE--SIVRD------PRV-DIIkltpaHLQVLKEMN---------IADQTAVR---RMIVGGENLSTRLARS--IHEQ 2049
Cdd:cd17632   303 TLFDdlALVRPtelflvPRVcDML-----FQRYQAELDrrsvagadaETLAERVKaelRERVLGGRLLAAVCGSapLSAE 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2050 FEGRIEIC------NEYGPTET---VVGCMIYRYDAAKDRRESVP-IGtaaantsiYVLDEnmKPAPigvPGEIYISGAG 2119
Cdd:cd17632   378 MKAFMESLldldlhDGYGSTEAgavILDGVIVRPPVLDYKLVDVPeLG--------YFRTD--RPHP---RGELLVKTDT 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2120 VARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVKI-RGYRIELGEIEAALLQEEVIKE--- 2195
Cdd:cd17632   445 LFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQifv 518
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 2196 ----------AVVTAREDVhgfkqLCAYyvsGGQTTAARLRKQLSQT-----LASYMVPAYFIeLDEMPLT-SNG 2254
Cdd:cd17632   519 ygnserayllAVVVPTQDA-----LAGE---DTARLRAALAESLQRIareagLQSYEIPRDFL-IETEPFTiANG 584
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1798-2175 8.80e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 65.14  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRAnrlaRTLRAKGVQTDQP---VAIITRNSIESVVGILAVLKSGGAYVPI-DPEYP--QDRIRYMLDDSQ 1871
Cdd:PRK07769   54 RDLTWSQFGARN----RAVGARLQQVTKPgdrVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCT 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1872 AGIVLMQRDvrkqlAYEGVTVLLDDESSYHQD------------GSDLAPIS-DVSHLAYVIYTSGSTGRPKGVLIEHGG 1938
Cdd:PRK07769  130 PSAILTTTD-----SAEGVRKFFRARPAKERPrviavdavpdevGATWVPPEaNEDTIAYLQYTSGSTRIPAGVQITHLN 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1939 L-TNYIwwakEVY--VKGEKAN-----FPLYSsisfDLTVTSIFTPLVTGNAIIVYDGEdktalleSIVRDPRVDIIKLT 2010
Cdd:PRK07769  205 LpTNVL----QVIdaLEGQEGDrgvswLPFFH----DMGLITVLLPALLGHYITFMSPA-------AFVRRPGRWIRELA 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2011 PAHLQVLKEMNIA---------------------DQTAVRRMIVGGENLSTRLARSIHEQFE----GRIEICNEYGPTE- 2064
Cdd:PRK07769  270 RKPGGTGGTFSAApnfafehaaarglpkdgepplDLSNVKGLLNGSEPVSPASMRKFNEAFApyglPPTAIKPSYGMAEa 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2065 TVVGCMIYRYDAAK----DRRE-----SVPIGTAAANT--------------SIYVLDENMKPAPIGVPGEIYISGAGVA 2121
Cdd:PRK07769  350 TLFVSTTPMDEEPTviyvDRDElnagrFVEVPADAPNAvaqvsagkvgvsewAVIVDPETASELPDGQIGEIWLHGNNIG 429
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 2122 RGYLNRPELTAEKF---VDDPF--------EPGAKMYKTGDLAKWLaDGNIEYAGRIDEQVKIRG 2175
Cdd:PRK07769  430 TGYWGKPEETAATFqniLKSRLseshaegaPDDALWVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
408-745 9.46e-10

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 63.86  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 VIYTSGTTGKPKGVMVEHGGI----VNSLQWKKAffkhSPADRVLVLYPYVFDAFILNFFGPLISGATLHLLPNEENKEt 483
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALlaqaLVLAVLQAI----DEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  484 faIQNAIKQERITH-FSTSPrllktMIEQMnredfihvqhvvvggEQLETDTVEKLHSLQ-----------------PRI 545
Cdd:cd17636    80 --VLELIEAERCTHaFLLPP-----TIDQI---------------VELNADGLYDLSSLRsspaapewndmatvdtsPWG 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  546 RINNEYGPTENSVVSTFHpVQSADEQITIGSPVANHQAYILGAHHQIQPIGIPGELYVGGAGVARGYLNRPELTEEKFVE 625
Cdd:cd17636   138 RKPGGYGQTEVMGLATFA-ALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  626 HLHvpgqkmyKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYVGE 705
Cdd:cd17636   217 GWH-------HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLK 289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 166797876  706 P--SLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKID 745
Cdd:cd17636   290 PgaSVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2276-2351 9.76e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 57.94  E-value: 9.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2276 APRTKAEEILVSAWESVLG--AENVSILDNFF-DLGGDSIKSIQVSSRLNQQ-GYKMEIKDLFQYATIAELSPHIKQNLR 2351
Cdd:COG0236     1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEEKLA 80
PRK09274 PRK09274
peptide synthase; Provisional
3291-3692 1.25e-09

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 64.53  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3291 EQAHRTPDNTAVVFEG----------KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAY 3360
Cdd:PRK09274   14 RAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3361 LPIDPDSPSERIRYILNDS-----------------------SISVLLYCGklqDDIGFSGTCIDLMEEHfyHEKDSSLA 3417
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAqpdafigipkahlarrlfgwgkpSVRRLVTVG---GRLLWGGTTLATLLRD--GAAAPFPM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3418 LSYQSSQLAYAIYTSGTTGKPKGTLIEHR---QVIHLIeglsRQVY---------------SAYDAELNIAMLAPYyFDA 3479
Cdd:PRK09274  169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGmfeAQIEAL----REDYgiepgeidlptfplfALFGPALGMTSVIPD-MDP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3480 SvqqmyasllsgHTLFIVPKEIVsdgAALcryyRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHL---LIGGEALSKTTV 3556
Cdd:PRK09274  244 T-----------RPATVDPAKLF---AAI----ERYGVTNLFGSPALLERLGRYGEANGIKLPSLrrvISAGAPVPIAVI 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3557 NKLKQLFgEHGAApgITNVYGPTETCVDASLFNIECSSDAWARSQNY--VPIGKPLGRNRMYIL----------DSKKRL 3624
Cdd:PRK09274  306 ERFRAML-PPDAE--ILTPYGATEALPISSIESREILFATRAATDNGagICVGRPVDGVEVRIIaisdapipewDDALRL 382
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 3625 qPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPfvPEDRMYRTGDLARLLPDGNIEYIGRIDHQVK 3692
Cdd:PRK09274  383 -ATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2364-2679 1.29e-09

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 64.01  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2364 LTPIQHWFFEQT--TTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGceaqneEIAQSGLYRLEV 2441
Cdd:cd19536     4 LSSLQEGMLFHSllNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLG------QPVQVVHRQAQV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2442 MNLKEDPDPGRTIEAKADE-IQSSMH----LSDGPLMKAGLFQCADGDH--LLIAIHHLIIDGISWRILLEDIVSGYKQA 2514
Cdd:cd19536    78 PVTELDLTPLEEQLDPLRAyKEETKIrrfdLGRAPLVRAALVRKDERERflLVISDHHSILDGWSLYLLVKEILAVYNQL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2515 ENGRVIQLPQkTDSFQLWAKRLSEYAQSEtikQEQEYWT-KIEQTEVKPLP-------KDFHETHTTAKDSETAAVEwtk 2586
Cdd:cd19536   158 LEYKPLSLPP-AQPYRDFVAHERASIQQA---ASERYWReYLAGATLATLPalseavgGGPEQDSELLVSVPLPVRS--- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2587 eetelllKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDisRTVGWFTSLYPVVLHAqPGKEI 2666
Cdd:cd19536   231 -------RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTL-SEETV 300
                         330
                  ....*....|...
gi 166797876 2667 SDYIKTTKEGLRQ 2679
Cdd:cd19536   301 EDLLKRAQEQELE 313
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
852-1277 1.40e-09

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 64.01  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  852 LTPIQHWFFEQKM--PHAHHYNQAVMLYSAEGFKEGPLRRTMERIASHHDALRMIFEKtpDGYAPRITGTDESELFHLEV 929
Cdd:cd19536     4 LSSLQEGMLFHSLlnPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIE--DGLGQPVQVVHRQAQVPVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  930 MNYKGETDPAQAIAD-KANEIQSSMVLDKGPLMKLGLFQCPDGDH--LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQ 1006
Cdd:cd19536    82 LDLTPLEEQLDPLRAyKEETKIRRFDLGRAPLVRAALVRKDERERflLVISDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1007 TIQLPQKTDsfpfWADQLSKYAAETDMEEEIAYWTE-LSSIKPQPLPKDT-ISEGSLLRDSEevtiqWTKEETEQLLKQA 1084
Cdd:cd19536   162 PLSLPPAQP----YRDFVAHERASIQQAASERYWREyLAGATLATLPALSeAVGGGPEQDSE-----LLVSVPLPVRSRS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1085 -NRAYNTDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPDADisRTIGWFTSQYPVVLRMeAGKNLSQRIKIVKE 1163
Cdd:cd19536   233 lAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTL-SEETVEDLLKRAQE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1164 GLRRIP--DKGMNYSIIKYISGHPEADSLqlkpeisFNYLgqfDQDLKHQA-LRISPFSTGLSMNENQERTAVlDLNGMI 1240
Cdd:cd19536   310 QELESLshEQVPLADIQRCSEGEPLFDSI-------VNFR---HFDLDFGLpEWGSDEGMRRGLLFSEFKSNY-DVNLSV 378
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 166797876 1241 A--EGTLSLTLSYSSKQYERSTMAQFARGLKESLQEVIA 1277
Cdd:cd19536   379 LpkQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELAT 417
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
869-1165 1.52e-09

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 63.87  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  869 HYNQAVmLYSAEGFKEGPLRRTMERIASHHDALRMIF---------EKTPDGYAPRITGTD---ESELFHLEVMNYKGET 936
Cdd:cd19547    24 YFNQNV-LELVGGTDEDVLREAWRRVADRYEILRTGFtwrdraeplQYVRDDLAPPWALLDwsgEDPDRRAELLERLLAD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  937 DPAQAIAdkaneiqssmvLDKGPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQ-AERRQtiqlPQKT 1014
Cdd:cd19547   103 DRAAGLS-----------LADCPLYRLTLVRLGGGRHyLLWSHHHILLDGWCLSLIWGDVFRVYEElAHGRE----PQLS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1015 DSFPF--WADQLSKYAAETDMEEEiaYWTE-LSSIKPQPLpkdtiSEGSLLRDSEEVTI--QWTKEETEqLLKQANRAYN 1089
Cdd:cd19547   168 PCRPYrdYVRWIRARTAQSEESER--FWREyLRDLTPSPF-----STAPADREGEFDTVvhEFPEQLTR-LVNEAARGYG 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 1090 TDINDLLLTSLGLAVHKWTGTEDIVVNLEGHGREPIIPDADIsrTIGWFTSQYPVVLRMEAGKNLSQRIKIVKEGL 1165
Cdd:cd19547   240 VTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4472-4818 1.67e-09

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 63.27  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4472 NDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQFAAMSFDV--CYQEMFSALSSGGILFIIGNEAKR 4549
Cdd:cd05944     2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVngSVVTLLTPLASGAHVVLAGPAGYR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4550 DIRQLNDF---VRTHGIqTAF--LPTAFLKLLA--------SEKhyfepFAECvdhiiaaGEQLIATRMLRDMLARHQVT 4616
Cdd:cd05944    82 NPGLFDNFwklVERYRI-TSLstVPTVYAALLQvpvnadisSLR-----FAMS-------GAAPLPVELRARFEDATGLP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4617 LHNHYGPSETHVVTmyTVD-PDTDQELQPIGKPI--SNTEIFILNEAGTLQ---PVGIVGELCISGVSLARGYHNREsLT 4690
Cdd:cd05944   149 VVEGYGLTEATCLV--AVNpPDGPKRPGSVGLRLpyARVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYTE-GN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4691 LETFVphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVkIRG-YRVELGEVEAALLKHVQEAVVLAKentdGQSDLYA 4769
Cdd:cd05944   226 KNAFV------ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAV----GQPDAHA 294
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4770 ------YFTAEQSLSIS--QLKEKLAGQIPGYM-IPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05944   295 gelpvaYVQLKPGAVVEeeELLAWARDHVPERAaVPKHIEVLEELPVTAVGKVFKPAL 352
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
4473-4818 1.80e-09

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 63.14  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4473 DLMYVIYTSGTTGQPKGVQLehkTMTNLLAY-EQDHTQL----RFDRVL---QFAAMsfdvcyQEMFSALSSGGILFIIG 4544
Cdd:PRK07824   36 DVALVVATSGTTGTPKGAML---TAAALTASaDATHDRLggpgQWLLALpahHIAGL------QVLVRSVIAGSEPVELD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4545 NEAKRDIRQLNDFVRTHG---IQTAFLPTAFLKLLASEKHyFEPFAEcVDHIIAAGEQLIATrmLRDMLARHQVTLHNHY 4621
Cdd:PRK07824  107 VSAGFDPTALPRAVAELGggrRYTSLVPMQLAKALDDPAA-TAALAE-LDAVLVGGGPAPAP--VLDAAAAAGINVVRTY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4622 GPSETHVVTMYTvdpdtdqelqpiGKPISNTEIFILNeagtlqpvgivGELCISGVSLARGYHNRESltletfvpHPYDS 4701
Cdd:PRK07824  183 GMSETSGGCVYD------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD--------PDPFA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4702 NQRMYKTGDLARyLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTD-GQSDLYAYFTAEQSL- 4777
Cdd:PRK07824  232 EPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHpaVADCAVFGLPDDRlGQRVVAAVVGDGGPAp 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 166797876 4778 SISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PRK07824  311 TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
3293-3781 1.81e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 63.94  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVF--EGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSE 3370
Cdd:PRK13391    7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3371 RIRYILNDSSiSVLLYCGKLQDDI--GFSGTCIDLMEEHFYHEKDSSLAlsYQSSQLAYA----------------IYTS 3432
Cdd:PRK13391   87 EAAYIVDDSG-ARALITSAAKLDVarALLKQCPGVRHRLVLDGDGELEG--FVGYAEAVAglpatpiadeslgtdmLYSS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3433 GTTGKPKGTLiehRQVIHL-------IEGLSRQVYsAYDAE---LNIAML---APYYFDASVQQMyasllsGHTLFIVPK 3499
Cdd:PRK13391  164 GTTGRPKGIK---RPLPEQppdtplpLTAFLQRLW-GFRSDmvyLSPAPLyhsAPQRAVMLVIRL------GGTVIVMEH 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3500 eivSDGAALCRYYRQHSIDITDGTPAH----LKLliaagdlqgvtlqhlliGGEALSKTTVNKLKQLFgeHGAAPG---- 3571
Cdd:PRK13391  234 ---FDAEQYLALIEEYGVTHTQLVPTMfsrmLKL-----------------PEEVRDKYDLSSLEVAI--HAAAPCppqv 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3572 -----------ITNVYGPTEtcvdASLFNIeCSSDAWARSQNYVpiGKPLgRNRMYILDSKKRLQPKGVQGELYIAGdGV 3640
Cdd:PRK13391  292 keqmidwwgpiIHEYYAATE----GLGFTA-CDSEEWLAHPGTV--GRAM-FGDLHILDDDGAELPPGEPGTIWFEG-GR 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3641 GRGYLNLPELTDEKFVADPfvpedRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVML-----------N 3709
Cdd:PRK13391  363 PFEYLNDPAKTAEARHPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLIthpkvadaavfG 437
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3710 VPD----------IQEAAAAALKDAddeyylcgyFAAdktiqisELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQ 3779
Cdd:PRK13391  438 VPNedlgeevkavVQPVDGVDPGPA---------LAA-------ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKR 501

                  ..
gi 166797876 3780 LL 3781
Cdd:PRK13391  502 LL 503
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2283-2341 1.91e-09

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 56.42  E-value: 1.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876  2283 EILVSAWESVLG--AENVSILDNFFDLGGDSIKSIQVSSRLNQQ-GYKMEIKDLFQYATIAE 2341
Cdd:pfam00550    1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
4606-4819 1.92e-09

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 63.86  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4606 LRDMLARHQVTLHNHYGPSET--HVVTMytvDPDtdQELQ---PIGKPISNTEIFILNEAgtlqpvgiVGELCISGVSLA 4680
Cdd:PRK07445  246 LLEQARQLQLRLAPTYGMTETasQIATL---KPD--DFLAgnnSSGQVLPHAQITIPANQ--------TGNITIQAQSLA 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4681 RGYhnresltletfVPHPYDSnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAK 4758
Cdd:PRK07445  313 LGY-----------YPQILDS-QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATglVQDVCVLGL 380
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 4759 ENTD-GQSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRALP 4819
Cdd:PRK07445  381 PDPHwGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
771-829 1.93e-09

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 56.42  E-value: 1.93e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876   771 ELLASIWQEVLG--AERIGILDNFFDFGGDSIKSIQVSSRLYQA-GYKVDMKHLFKHPSIAE 829
Cdd:pfam00550    1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
4339-4818 2.13e-09

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 64.12  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4339 EQQAERNPDHEAVMF-GN-----QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAA---- 4408
Cdd:cd05966    60 DRHLKERGDKVAIIWeGDepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhsvv 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4409 FLPIDPELPEKRrafmLKDSGADVLLTC-----AGHAIP----------------------------PLFEGEVLLLDDP 4455
Cdd:cd05966   140 FAGFSAESLADR----INDAQCKLVITAdggyrGGKVIPlkeivdealekcpsvekvlvvkrtggevPMTEGRDLWWHDL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4456 LLYQgRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQleHKTMTNLLayeqdHTQLRFDRVlqfaamsFDvcYQE------ 4529
Cdd:cd05966   216 MAKQ-SPECEPEWMDSEDPLFILYTSGSTGKPKGVV--HTTGGYLL-----YAATTFKYV-------FD--YHPddiywc 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4530 -------------MFSALSSGGILFII-GNEAKRDIRQLNDFVRTHGIQ---TAflPTAF------------------LK 4574
Cdd:cd05966   279 tadigwitghsyiVYGPLANGATTVMFeGTPTYPDPGRYWDIVEKHKVTifyTA--PTAIralmkfgdewvkkhdlssLR 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4575 LLASEKhyfEPFAEcvdhiiaagEqliATRMLRDMLARHQVTLHNHYGPSET--HVVTmytvdpdtdqelqPIG-----K 4647
Cdd:cd05966   357 VLGSVG---EPINP---------E---AWMWYYEVIGKERCPIVDTWWQTETggIMIT-------------PLPgatplK 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4648 PISNT------EIFILNEAGTLQPVGIVGELCISGV--SLARGYHNRESLTLET-FVPHPYdsnqrMYKTGDLARYLPEG 4718
Cdd:cd05966   409 PGSATrpffgiEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHERYEDTyFSKFPG-----YYFTGDGARRDEDG 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4719 NIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKEN-TDGQSdLYAYFTAEQSLSISQ-----LKEKLAGQI 4790
Cdd:cd05966   484 YYWITGRVDDVINVSGHRLGTAEVESALVAHpaVAEAAVVGRPHdIKGEA-IYAFVTLKDGEEPSDelrkeLRKHVRKEI 562
                         570       580
                  ....*....|....*....|....*...
gi 166797876 4791 PGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05966   563 GPIATPDKIQFVPGLPKTRSGKIMRRIL 590
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
4359-4818 2.53e-09

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 63.64  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4359 TYRQLNERSNQLARVLqdKGACTDQV---VAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:cd05928    43 SFRELGSLSRKAANVL--SGACGLQRgdrVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 C-----AGHAIP---PLFEGEVLLLDDP---------LLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTMt 4498
Cdd:cd05928   121 SdelapEVDSVAsecPSLKTKLLVSEKSrdgwlnfkeLLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSL- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4499 nLLAYEQDHtqlRFDRVLQFAAMSFDV--------CYQEMFSALSSGGILFIiGNEAKRDIRQLNDFVRTHGIQTAF-LP 4569
Cdd:cd05928   200 -GLGLKVNG---RYWLDLTASDIMWNTsdtgwiksAWSSLFEPWIQGACVFV-HHLPRFDPLVILKTLSSYPITTFCgAP 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4570 TAFLKLLASE--KHYFEPFAECVdhiiAAGEQLIAtRMLRDMLARHQVTLHNHYGPSETHVVTMYTvdpdTDQELQP--I 4645
Cdd:cd05928   275 TVYRMLVQQDlsSYKFPSLQHCV----TGGEPLNP-EVLEKWKAQTGLDIYEGYGQTETGLICANF----KGMKIKPgsM 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4646 GKPISNTEIFILNEAGTLQPVGIVGELCIS-----GVSLARGYHNRESLTLETFvphpydsNQRMYKTGDLARYLPEGNI 4720
Cdd:cd05928   346 GKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAATI-------RGDFYLTGDRGIMDEDGYF 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4721 EYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVLAKENTDGQSDLYAYFTAEQSLS------ISQLKEKLAGQIP 4791
Cdd:cd05928   419 WFMGRADDVINSSGYRIGPFEVESALIEHpavVESAVVSSPDPIRGEVVKAFVVLAPQFLShdpeqlTKELQQHVKSVTA 498
                         490       500
                  ....*....|....*....|....*..
gi 166797876 4792 GYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05928   499 PYKYPRKVEFVQELPKTVTGKIQRNEL 525
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
542-750 3.03e-09

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 63.09  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  542 QPRIRINNEYGPTEN-SVVSTFHPVQSADEQITIGSPVAnhqayilgaHHQIQpIGIP--GELYVGGAGVARGYLnrPEl 618
Cdd:PRK07445  252 QLQLRLAPTYGMTETaSQIATLKPDDFLAGNNSSGQVLP---------HAQIT-IPANqtGNITIQAQSLALGYY--PQ- 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  619 teekfvehlHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQL 698
Cdd:PRK07445  319 ---------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVV 389
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166797876  699 YAYYVGE-PSLTAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKALP 750
Cdd:PRK07445  390 TAIYVPKdPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PLN02574 PLN02574
4-coumarate--CoA ligase-like
4471-4818 3.46e-09

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 63.32  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4471 ENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLAYEQdhTQLRFDrVLQFAAMSFDVCYQEMFSALSSGGI-LFIIG----- 4544
Cdd:PLN02574  197 QDDVAAIMYSSGTTGASKGVVLTHR---NLIAMVE--LFVRFE-ASQYEYPGSDNVYLAALPMFHIYGLsLFVVGllslg 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4545 --------NEAKRDIRQLNDFVRTHgiqTAFLPTAFLKLLASEKHYFEPFAECVDHIiAAGEQLIATRMLRDML-ARHQV 4615
Cdd:PLN02574  271 stivvmrrFDASDMVKVIDRFKVTH---FPVVPPILMALTKKAKGVCGEVLKSLKQV-SCGAAPLSGKFIQDFVqTLPHV 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4616 TLHNHYGPSETHVVTMYTVDPDTDQELQPIGKPISNTEIFILN-EAGTLQPVGIVGELCISGVSLARGYHNRESLTLETF 4694
Cdd:PLN02574  347 DFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4695 VphpydsNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFT 4772
Cdd:PLN02574  427 D------KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHpeIIDAAVTAVPDKECGEIPVAFVV 500
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 166797876 4773 AEQ--SLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PLN02574  501 RRQgsTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
1800-2187 5.11e-09

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 62.83  E-value: 5.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1800 LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVLMQR 1879
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1880 -------DVRKQLAYEGVTVLLDDESSYHQDGSD------LAPISDVSHL----------------AYVIYTSGSTGRPK 1930
Cdd:PLN02387  187 kqlkkliDISSQLETVKRVIYMDDEGVDSDSSLSgssnwtVSSFSEVEKLgkenpvdpdlpspndiAVIMYTSGSTGLPK 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1931 GVLIEHGGLTNYI---------WWAKEVYVkgekANFPLySSIsFDLTVTSIF----------TPLV---TGNAIIVYDG 1988
Cdd:PLN02387  267 GVMMTHGNIVATVagvmtvvpkLGKNDVYL----AYLPL-AHI-LELAAESVMaavgaaigygSPLTltdTSNKIKKGTK 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1989 EDKTALLESI----------VRD---PRVD----IIK------------------LTPAHLQ-------VLKEMNIADQT 2026
Cdd:PLN02387  341 GDASALKPTLmtavpaildrVRDgvrKKVDakggLAKklfdiaykrrlaaiegswFGAWGLEkllwdalVFKKIRAVLGG 420
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2027 AVRRMIVGGENLSTRLARSIHeqfegrieIC------NEYGPTETVVGCMIYRYDAAKDRResvpIGTAAANTSIYVLD- 2099
Cdd:PLN02387  421 RIRFMLSGGAPLSGDTQRFIN--------IClgapigQGYGLTETCAGATFSEWDDTSVGR----VGPPLPCCYVKLVSw 488
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2100 ------ENMKPAPigvPGEIYISGAGVARGYLNRPELTAEKFVDDpfEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKI 2173
Cdd:PLN02387  489 eeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKL 563
                         490
                  ....*....|....*
gi 166797876 2174 R-GYRIELGEIEAAL 2187
Cdd:PLN02387  564 QhGEYVSLGKVEAAL 578
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
263-649 5.58e-09

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 62.59  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  263 RTVYQLFEEQAERTPENAAVKFKND-----HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLE-MIVSIIAVWkA 336
Cdd:PRK08180   39 RRLTDRLVHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEhALLALAAMY-A 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  337 GGAYVPLDPEY-----PKERLQYLLH-----------------------DADADVLLVQHHLKnslafDGPVIDLND--E 386
Cdd:PRK08180  118 GVPYAPVSPAYslvsqDFGKLRHVLElltpglvfaddgaafaralaavvPADVEVVAVRGAVP-----GRAATPFAAllA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  387 ASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKK---AFFKHSPAdrVLVLY-PY--VFDAfIL 460
Cdd:PRK08180  193 TPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAqtfPFLAEEPP--VLVDWlPWnhTFGG-NH 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  461 NFFGPLISGATLHLlpnEENKET---FA--IQNaIKQERITHFSTSPRLLKTMIEQMNRED------FIHVQHVVVGGEQ 529
Cdd:PRK08180  270 NLGIVLYNGGTLYI---DDGKPTpggFDetLRN-LREISPTVYFNVPKGWEMLVPALERDAalrrrfFSRLKLLFYAGAA 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  530 LETDTVEKLHSLQ-----PRIRINNEYGPTENSVVSTF-HP--VQSADeqitIGSPVAnhqayilGAHHQIQPIGIPGEL 601
Cdd:PRK08180  346 LSQDVWDRLDRVAeatcgERIRMMTGLGMTETAPSATFtTGplSRAGN----IGLPAP-------GCEVKLVPVGGKLEV 414
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876  602 YVGGAGVARGYLNRPELTEEKFVEhlhvpgQKMYKTGDLARWL----P------DGRI 649
Cdd:PRK08180  415 RVKGPNVTPGYWRAPELTAEAFDE------EGYYRSGDAVRFVdpadPerglmfDGRI 466
PLN02654 PLN02654
acetate-CoA ligase
1797-2261 5.86e-09

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 62.61  E-value: 5.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1797 DRQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGILAVLKSGGAYVPIDPEYPQDRIRYMLDDSQAGIVL 1876
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1877 MQRDVRK----------------QLAYEGVTV----------LLDDESSYHQDGSDL--------APIS------DVSHL 1916
Cdd:PLN02654  198 TCNAVKRgpktinlkdivdaaldESAKNGVSVgicltyenqlAMKREDTKWQEGRDVwwqdvvpnYPTKcevewvDAEDP 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1917 AYVIYTSGSTGRPKGVLIEHGGltnYIWWAKEVYvkgeKANFPLYSS-----------ISFDLTVTsiFTPLVTGNAIIV 1985
Cdd:PLN02654  278 LFLLYTSGSTGKPKGVLHTTGG---YMVYTATTF----KYAFDYKPTdvywctadcgwITGHSYVT--YGPMLNGATVLV 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1986 YDGEDK---TALLESIVRDPRVDIIKLTPahlqvlkemniadqTAVRRMIVGGENLSTRLAR-------SIHEQF----- 2050
Cdd:PLN02654  349 FEGAPNypdSGRCWDIVDKYKVTIFYTAP--------------TLVRSLMRDGDEYVTRHSRkslrvlgSVGEPInpsaw 414
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2051 --------EGRIEICNEYGPTETVvGCMIYRYDAAkdrresVPIGTAAANTSIY-----VLDENMKPAPIGVPGEIYISG 2117
Cdd:PLN02654  415 rwffnvvgDSRCPISDTWWQTETG-GFMITPLPGA------WPQKPGSATFPFFgvqpvIVDEKGKEIEGECSGYLCVKK 487
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2118 A--GVAR---GYLNRPELTAekfvddpFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEV 2192
Cdd:PLN02654  488 SwpGAFRtlyGDHERYETTY-------FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2193 IKEAVVTARE-DVHGFKQLCAYYVSGGQTTAARLRKQLSQT----LASYMVPAYFIELDEMPLTSNGKINKKGL 2261
Cdd:PLN02654  561 CAEAAVVGIEhEVKGQGIYAFVTLVEGVPYSEELRKSLILTvrnqIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
4741-4812 6.54e-09

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 55.63  E-value: 6.54e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  4741 EVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTAEQ--SLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGK 4812
Cdd:pfam13193    1 EVESALVSHpaVAEAAVVGVPDELKGEAPVAFVVLKPgvELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3427-3775 6.91e-09

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 61.63  E-value: 6.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3427 YAIYTSGTTGKPKGTLIEHRQVIHLIEG---LSRQVYSAYDAELNIA---------MLAPYYFDASVQQMYASLLSGHTL 3494
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIFRMLMGgadFGTGEFTPSEDAHKAAaaaagtvmfPAPPLMHGTGSWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3495 FIVPKEIvsDGAALCRYYRQH---SIDITDGTPAH--LKLLIAAGDLQGVTLQHLLIGGEALSKTtvnkLKQLFGEHGAA 3569
Cdd:cd05924    87 VLPDDRF--DPEEVWRTIEKHkvtSMTIVGDAMARplIDALRDAGPYDLSSLFAISSGGALLSPE----VKQGLLELVPN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3570 PGITNVYGPTETcvdaslfniecSSDAWARSQNYVPIGKPLGR--NRMYILDSKKRLQPKGVQGELYIAGDG-VGRGYLN 3646
Cdd:cd05924   161 ITLVDAFGSSET-----------GFTGSGHSAGSGPETGPFTRanPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3647 LPELTDEKFvadPFVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADD 3726
Cdd:cd05924   230 DEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876 3727 EYYLCGYFAADKTIQIS--ELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK 3775
Cdd:cd05924   307 GQEVVAVVQLREGAGVDleELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2370-2554 6.98e-09

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 61.89  E-value: 6.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2370 WFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQneeIAQSGLYRLEVMNLKEDPD 2449
Cdd:cd20483    12 WFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQ---VLDDPSFHLIVIDLSEAAD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2450 PGRTIEAKADEIQSS-MHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGR---VIQLP- 2523
Cdd:cd20483    89 PEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFaLVLASHHIAWDRGSSKSIFEQFTALYDALRAGRdlaTVPPPp 168
                         170       180       190
                  ....*....|....*....|....*....|..
gi 166797876 2524 -QKTDsFQLWAKRLseyAQSETIKQEQEYWTK 2554
Cdd:cd20483   169 vQYID-FTLWHNAL---LQSPLVQPLLDFWKE 196
PRK09192 PRK09192
fatty acyl-AMP ligase;
289-743 7.81e-09

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 62.33  E-value: 7.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLdP--------EYPKERLQYLLHDAD 360
Cdd:PRK09192   50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-PlpmgfggrESYIAQLRGMLASAQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  361 ADVLLVQHHLK---------NSLAFDGPVIDLNDEASyhADCSLlsPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNS 431
Cdd:PRK09192  129 PAAIITPDELLpwvneathgNPLLHVLSHAWFKALPE--ADVAL--PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMAN 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  432 LQwkkAFFKHS----PADRVLVLYPYVFDAFILNFF-GPLISGATLHLLPNEEnketFAIQ-----NAIKQERIThFSTS 501
Cdd:PRK09192  205 LR---AISHDGlkvrPGDRCVSWLPFYHDMGLVGFLlTPVATQLSVDYLPTRD----FARRplqwlDLISRNRGT-ISYS 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  502 P----RLLKTMIEQMNREDF--IHVQHVVVGGEQLETDTvekLHSLQPRIRINN--------EYGPTENSVVSTFHP--- 564
Cdd:PRK09192  277 PpfgyELCARRVNSKDLAELdlSCWRVAGIGADMIRPDV---LHQFAEAFAPAGfddkafmpSYGLAEATLAVSFSPlgs 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  565 ---VQSADEQITIGSPVA---------------------NHQAYILG------AHHQIqpigipGELYVGGAGVARGYLN 614
Cdd:PRK09192  354 givVEEVDRDRLEYQGKAvapgaetrrvrtfvncgkalpGHEIEIRNeagmplPERVV------GHICVRGPSLMSGYFR 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  615 RPELTEEkfvehLHVPGqkMYKTGDLArWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVR--EAAVVAREDA 692
Cdd:PRK09192  428 DEESQDV-----LAADG--WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE 499
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876  693 DGAKQLyayYVGEPSLTAAQFREELSRELpNYMIPSRF--------IPLERIPLTSNGK 743
Cdd:PRK09192  500 NGEKIV---LLVQCRISDEERRGQLIHAL-AALVRSEFgveaavelVPPHSLPRTSSGK 554
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2364-2653 8.58e-09

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 61.35  E-value: 8.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2364 LTPIQHWFFEQTTTDQ-------HYYNQavmlHAPEGFQETQLRQTLQKLAEHHDALRMTFrtTENGceaQNEEIAQSGL 2436
Cdd:cd19535     4 LTDVQYAYWIGRQDDQelggvgcHAYLE----FDGEDLDPDRLERAWNKLIARHPMLRAVF--LDDG---TQQILPEVPW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2437 YRLEVMNLKEDPDPgrTIEAKADEIQSSMH-----LSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSG 2510
Cdd:cd19535    75 YGITVHDLRGLSEE--EAEAALEELRERLShrvldVERGPLFDIRLSLLPEGRTrLHLSIDLLVADALSLQILLRELAAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2511 YKQAEngrvIQLPQKTDSFQLWAKRLSEYAQSEtIKQEQEYWTkiEQTEVKP----LPkdfhethtTAKDSET------- 2579
Cdd:cd19535   153 YEDPG----EPLPPLELSFRDYLLAEQALRETA-YERARAYWQ--ERLPTLPpapqLP--------LAKDPEEikeprft 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2580 ------AAVEWTKeetellLKQANRAYHTEINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDisRTVGWFTSL 2653
Cdd:cd19535   218 rrehrlSAEQWQR------LKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVN--DVVGDFTSL 289
PRK07867 PRK07867
acyl-CoA synthetase; Validated
4329-4818 9.17e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 61.62  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4329 RIPTTIHQLFEQQAErnPDHEAVMFGNQTLTYRQLNERSNQLARVLQDkgactdqvvavLTDRSAHMIIGIL-------A 4401
Cdd:PRK07867    2 SSAPTVAELLLPLAE--DDDRGLYFEDSFTSWREHIRGSAARAAALRA-----------RLDPTRPPHVGVLldntpefS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4402 ILKAGAAFLPIDP-ELPEKRRAFMLKD----SGADVLLTCAGHAipPLFEG-----EVLLLDDP-----LLYQGRTDNLN 4466
Cdd:PRK07867   69 LLLGAAALSGIVPvGLNPTRRGAALARdiahADCQLVLTESAHA--ELLDGldpgvRVINVDSPawadeLAAHRDAEPPF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4467 LSCSENDLMYVIYTSGTTGQPKGVQLEHKTMT---NLLAyeqDHTQLRFDrvlqfaamsfDVCYQEM--FS--------- 4532
Cdd:PRK07867  147 RVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAsagVMLA---QRFGLGPD----------DVCYVSMplFHsnavmagwa 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4533 -ALSSGGILFIignEAKRDIRQLNDFVRTHGIQTAFL---PTAFLklLASEkhyfePFAECVDHI--IAAGEQlIATRML 4606
Cdd:PRK07867  214 vALAAGASIAL---RRKFSASGFLPDVRRYGATYANYvgkPLSYV--LATP-----ERPDDADNPlrIVYGNE-GAPGDI 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4607 RDMLARHQVTLHNHYGPSETHVVtmYTVDPDTdqelqP---IGKPISNTEIF-----------ILNEAGTLQPVGIVGEL 4672
Cdd:PRK07867  283 ARFARRFGCVVVDGFGSTEGGVA--ITRTPDT-----PpgaLGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGEL 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4673 C-ISGVSLARGYHNresltletfvpHPYDSNQRM----YKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALL 4747
Cdd:PRK07867  356 VnTAGPGGFEGYYN-----------DPEADAERMrggvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL 424
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4748 KH-------------------VQEAVVLAkENTDGQSDLYAYFTAEQslsiSQLKEKlagqipgyMIPSYFIQLEKLPLT 4808
Cdd:PRK07867  425 RYpdatevavyavpdpvvgdqVMAALVLA-PGAKFDPDAFAEFLAAQ----PDLGPK--------QWPSYVRVCAELPRT 491
                         570
                  ....*....|
gi 166797876 4809 GNGKVNRRAL 4818
Cdd:PRK07867  492 ATFKVLKRQL 501
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1320-1655 1.12e-08

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 61.34  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1320 PLTPMQKGMLFHSLFDPNSGAYFQQTMFDLHGDLEIDSFSKSLDGLSQKYDIFRTNFYRGWKDQPLQIIfkTKKIGFQFN 1399
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIL--DADAARPEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1400 DLREMKESQKEAMIQKYARedkmRGFDL--EKGALMRLFILrtDEKTYRFIWSFHHILMDGWCLPLITKEIFENYFALLQ 1477
Cdd:cd19546    84 PVVPATEEELPALLADRAA----HLFDLtrETPWRCTLFAL--SDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARRE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1478 QKQPEQSSIT-PYSQYIEW-----LGRQDAK----EAAAYWDQYLEGYEEQTGLPKDHH----AAEDGRYVPEKVTCDIS 1543
Cdd:cd19546   158 GRAPERAPLPlQFADYALWerellAGEDDRDsligDQIAYWRDALAGAPDELELPTDRPrpvlPSRRAGAVPLRLDAEVH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1544 SDLTsKMKRTAGkhhVTLNTLLQTAWAVLLQKYNRSRDVVFGSVVSgRPAGIPNVETMIGLFINTIPVRFRCEAGTTFAE 1623
Cdd:cd19546   238 ARLM-EAAESAG---ATMFTVVQAALAMLLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDLSGDPTFRE 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166797876 1624 LM---KEAQERAVASQK--FET-------------HPLY----DIQARTTQKQD 1655
Cdd:cd19546   313 LLgrvREAVREARRHQDvpFERlaellalppsadrHPVFqvalDVRDDDNDPWD 366
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
887-1149 1.59e-08

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 60.74  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  887 LRRTMERIASHHDALRM-IFEKTPDGYAPRITGTDeselFHLEVMNYKGETDPAQAIADKANEIQsSMVLD--KGPLMKL 963
Cdd:cd20483    41 LQKALSELVRRHEVLRTaYFEGDDFGEQQVLDDPS----FHLIVIDLSEAADPEAALDQLVRNLR-RQELDieEGEVIRG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  964 GLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYeQAERRQ----TIQLP--QKTDsFPFWADQLskyAAETDMEEE 1036
Cdd:cd20483   116 WLVKLPDEEFaLVLASHHIAWDRGSSKSIFEQFTALY-DALRAGrdlaTVPPPpvQYID-FTLWHNAL---LQSPLVQPL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1037 IAYWTE-LSSIkPQ-----PLPKdtiSEGSLLRDSEEVTIQWT-KEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTG 1109
Cdd:cd20483   191 LDFWKEkLEGI-PDaskllPFAK---AERPPVKDYERSTVEATlDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTE 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 166797876 1110 TEDIVVNLEGHGRepiiPDADISRTIGWFTSQYPVVLRME 1149
Cdd:cd20483   267 DEDLTIGMVDGDR----PHPDFDDLVGFFVNMLPIRCRMD 302
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
3429-3715 1.82e-08

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 59.98  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3429 IYTSGTTGKPKGTLIEHR-------QVIHLIeGLSrqvysayDAELNIAMLaPYYFDASVQQMYASLLSGHTLFIVPKei 3501
Cdd:cd17637     6 IHTAAVAGRPRGAVLSHGnliaanlQLIHAM-GLT-------EADVYLNML-PLFHIAGLNLALATFHAGGANVVMEK-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3502 vSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHL-LIGGEALSKTTvnklkQLFGEHGAAPGITnVYGPTE 3580
Cdd:cd17637    75 -FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrHVLGLDAPETI-----QRFEETTGATFWS-LYGQTE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3581 TCVDASLfniecsSDAWARSQNyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpf 3660
Cdd:cd17637   148 TSGLVTL------SPYRERPGS---AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF----- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3661 vpEDRMYRTGDLARLLPDGNIEYIGRIDHQ--VKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd17637   214 --RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAE 268
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
4355-4818 2.70e-08

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 60.13  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4355 NQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLL 4434
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4435 TCaghaipplfegevllLDDPLLYQGRTDNLNLSCSE-NDLMYVIYTSGTTGQPKGVQLEHktmtnllayeqdhtqLRFD 4513
Cdd:cd05939    81 FN---------------LLDPLLTQSSTEPPSQDDVNfRDKLFYIYTSGTTGLPKAAVIVH---------------SRYY 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4514 RVLQFAAMSF-----DVCYQEMFSALSSGGILfiigneakrDIRQLNDFVRTHGIQTAFLPTAFlkllasekhyfepFAE 4588
Cdd:cd05939   131 RIAAGAYYAFgmrpeDVVYDCLPLYHSAGGIM---------GVGQALLHGSTVVIRKKFSASNF-------------WDD 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4589 CVDHIIAAGeQLIAtRMLRDMLA--------RHQVTL---------------------------------------HNHY 4621
Cdd:cd05939   189 CVKYNCTIV-QYIG-EICRYLLAqppseeeqKHNVRLavgnglrpqiweqfvrrfgipqigefygategnsslvniDNHV 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4622 G--------PSETHVVTMYTVDPDTdqelqpiGKPISNTEIFIL----NEAGTLqpVGIVgelcISGVSLAR--GYHNrE 4687
Cdd:cd05939   267 GacgfnsriLPSVYPIRLIKVDEDT-------GELIRDSDGLCIpcqpGEPGLL--VGKI----IQNDPLRRfdGYVN-E 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4688 SLTLETFVPHPYDSNQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAAL--LKHVQEAVVLAKE--NTDG 4763
Cdd:cd05939   333 GATNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILsnVLGLEDVVVYGVEvpGVEG 412
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 4764 QSDLYAYFTAEQSLSISQLKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05939   413 RAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PLN03102 PLN03102
acyl-activating enzyme; Provisional
3297-3776 2.71e-08

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 60.42  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYCGKLQDDIGFSGTCIDLMEEH------FYHEKDSSLALSYQSSQLAYAI--------------------- 3429
Cdd:PLN03102  108 RHAKPKILFVDRSFEPLAREVLHLLSSEDSNlnlpviFIHEIDFPKRPSSEELDYECLIqrgeptpslvarmfriqdehd 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3430 -----YTSGTTGKPKGTLIEHR----QVIHLIEGLSRQVYSAYDAELNIAMLAPYYFDASVQ-QMYASLLSGHtlfIVPK 3499
Cdd:PLN03102  188 pislnYTSGTTADPKGVVISHRgaylSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAaRGGTSVCMRH---VTAP 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3500 EIVSDgaalcryYRQHSIDITDGTPAHLKLLiaagdLQGVTLQ--------HLLIGGEALSKTTVNKLKQLFGEHGAAPG 3571
Cdd:PLN03102  265 EIYKN-------IEMHNVTHMCCVPTVFNIL-----LKGNSLDlsprsgpvHVLTGGSPPPAALVKKVQRLGFQVMHAYG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3572 ITNVYGPTETCvdaslfniecssdAWARSQNYVPIGKPL---GRNRMYIL-----DSKKRLQPKGV------QGELYIAG 3637
Cdd:PLN03102  333 LTEATGPVLFC-------------EWQDEWNRLPENQQMelkARQGVSILgladvDVKNKETQESVprdgktMGEIVIKG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3638 DGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAA 3717
Cdd:PLN03102  400 SSIMKGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETA 472
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 3718 AAALKDADDEYYLCGYFAADK----------TIQISE--LRKRMARHLPGYMIPAHFVQLDKMPLTPNGKL 3776
Cdd:PLN03102  473 VVAMPHPTWGETPCAFVVLEKgettkedrvdKLVTRErdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKI 543
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1423-1646 3.07e-08

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 59.51  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1423 RGFDLEKGALMRLFILRTdekTYRFIWSfhHILMDgwclpLITKEIFENYFALLQQKQPEQSSITPYSQYIEWlGRQDAK 1502
Cdd:cd19537    91 RPFDLEREDPIRVFISPD---TLLVVMS--HIICD-----LTTLQLLLREVSAAYNGKLLPPVRREYLDSTAW-SRPASP 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1503 EAAAYWDQYLEGYeeqtGLPKDHHAAEDGRYVPEKVTCDISSDLTSKMKRTAGKHHVTLNTLLQTAWAVLLQKYNRSRDV 1582
Cdd:cd19537   160 EDLDFWSEYLSGL----PLLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDI 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1583 VFGSVVSGRPAgiPNVETMIGLFINTIPVR--FRCEAGTTFAELMKEAQER---AVA--------------SQKFETHPL 1643
Cdd:cd19537   236 VLGAPYLNRTS--EEDMETVGLFLEPLPIRirFPSSSDASAADFLRAVRRSsqaALAhaipwhqllehlglPPDSPNHPL 313

                  ...
gi 166797876 1644 YDI 1646
Cdd:cd19537   314 FDV 316
PRK05857 PRK05857
fatty acid--CoA ligase;
4326-4828 3.57e-08

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 60.02  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4326 AEKRIPTTIHQLFEQQAERNPdhEAVMF----GNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILA 4401
Cdd:PRK05857    8 AMPQLPSTVLDRVFEQARQQP--EAIALrrcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4402 ILKAGAAFLPIDPELPEK---------RRAFMLKDSGADV---LLTCAGHAIPPLfEGEVLLLDDPLLYQGRTDNL--NL 4467
Cdd:PRK05857   86 CAKLGAIAVMADGNLPIAaierfcqitDPAAALVAPGSKMassAVPEALHSIPVI-AVDIAAVTRESEHSLDAASLagNA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4468 SCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLAYeqdhtqLRFDRVLQFAAMSFDVCYQEMfSALSSGGILFII---- 4543
Cdd:PRK05857  165 DQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDI------LQKEGLNWVTWVVGETTYSPL-PATHIGGLWWILtclm 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4544 -------GNEAKRDIRQLndfVRTHGIQTAFLPTAFLKLLASEKHYFEPFAECVDHIIAAGEQLIAT--RMLRDMLAR-H 4613
Cdd:PRK05857  238 hgglcvtGGENTTSLLEI---LTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAAdvRFIEATGVRtA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4614 QVtlhnhYGPSETHvVTMYTVDPDTDQ----ELQPIGKPISNTEIFILNEAG------TLQPVGIVGELCISGVSLARGY 4683
Cdd:PRK05857  315 QV-----YGLSETG-CTALCLPTDDGSivkiEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGY 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4684 HNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVE--AALLKHVQEAVV--LAKE 4759
Cdd:PRK05857  389 WNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDriAEGVSGVREAACyeIPDE 461
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 4760 NTDGQSDLYAYFTAEQSLSIS-QLKEKLAG----QIPGYMIPSYFIQLEKLPLTGNGKVNRRALPMPEAGLQTG 4828
Cdd:PRK05857  462 EFGALVGLAVVASAELDESAArALKHTIAArfrrESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKAR 535
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
3414-3785 3.60e-08

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 59.81  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3414 SSLALSYQSSQLAYAIYTSGTTGKPKGTLIEHRQVIhlIEGLSRQV---YSAYDAELNIAMLAPYYFDASVQQMyasLLS 3490
Cdd:PLN02860  163 TELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALI--VQSLAKIAivgYGEDDVYLHTAPLCHIGGLSSALAM---LMV 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3491 GHTLFIVPKeivSDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGV-----TLQHLLIGGEALSKTTVNKLKQLFge 3565
Cdd:PLN02860  238 GACHVLLPK---FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTwkvfpSVRKILNGGGSLSSRLLPDAKKLF-- 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3566 hgAAPGITNVYGPTETCVDAS---LFNIECSSDAWARSQNYVP------------IGKPLGRNRMYI-LDSKKRLqpkgv 3629
Cdd:PLN02860  313 --PNAKLFSAYGMTEACSSLTfmtLHDPTLESPKQTLQTVNQTksssvhqpqgvcVGKPAPHVELKIgLDESSRV----- 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3630 qGELYIAGDGVGRGYLNLPELTDEKFVADPFVPedrmyrTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLN 3709
Cdd:PLN02860  386 -GRILTRGPHVMLGYWGQNSETASVLSNDGWLD------TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQ 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3710 -----------VPD------------IQEAAAAALKDADDeyylcgyfaADKTIQISE--LRK--RMaRHLPGYMIPAHF 3762
Cdd:PLN02860  459 hpgvasvvvvgVPDsrltemvvacvrLRDGWIWSDNEKEN---------AKKNLTLSSetLRHhcRE-KNLSRFKIPKLF 528
                         410       420
                  ....*....|....*....|....
gi 166797876 3763 VQLDK-MPLTPNGKLNRQLLPAPV 3785
Cdd:PLN02860  529 VQWRKpFPLTTTGKIRRDEVRREV 552
PLN02479 PLN02479
acetate-CoA ligase
3288-3787 4.77e-08

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 59.47  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3288 LFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDpds 3367
Cdd:PLN02479   25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVN--- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3368 pserIRyiLNDSSISVLLycgklqddiGFSGTCIDLMEEHFYHEKDSSLAL--------------------SYQSSQLAY 3427
Cdd:PLN02479  102 ----IR--LNAPTIAFLL---------EHSKSEVVMVDQEFFTLAEEALKIlaekkkssfkppllivigdpTCDPKSLQY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3428 AI---------------------------------YTSGTTGKPKGTLIEHRqvihlieglsrqvySAYDAELNIAM--- 3471
Cdd:PLN02479  167 ALgkgaieyekfletgdpefawkppadewqsialgYTSGTTASPKGVVLHHR--------------GAYLMALSNALiwg 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3472 ----------LAPYYFDASVQQMYASLLSGHTLF---IVPKEIVSdgaALCRYYRQHSIditdGTPAHLKLLIAAGDLQG 3538
Cdd:PLN02479  233 mnegavylwtLPMFHCNGWCFTWTLAALCGTNIClrqVTAKAIYS---AIANYGVTHFC----AAPVVLNTIVNAPKSET 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3539 VT----LQHLLIGGEALSKTTVNKLKQLFGEHGAAPGITNVYGPTETCvdaslfniecssdAWARSQNYVPigkPLGRNR 3614
Cdd:PLN02479  306 ILplprVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYGPSTVC-------------AWKPEWDSLP---PEEQAR 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3615 M-------YI----LD--SKKRLQP----KGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLP 3677
Cdd:PLN02479  370 LnarqgvrYIglegLDvvDTKTMKPvpadGKTMGEIVMRGNMVMKGYLKNPKANEEAF-------ANGWFHSGDLGVKHP 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3678 DGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYYLC-------GYFAADKTIQISELRKRMA 3750
Cdd:PLN02479  443 DGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCafvtlkpGVDKSDEAALAEDIMKFCR 522
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 166797876 3751 RHLPGYMIPAHFVqLDKMPLTPNGKLNRQLLPA------PVKK 3787
Cdd:PLN02479  523 ERLPAYWVPKSVV-FGPLPKTATGKIQKHVLRAkakemgPVKK 564
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1917-2274 5.26e-08

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 59.72  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1917 AYVIYTSGSTGRPKGVLIEHGGLTNYIWWAKEVyvkgekANF----------PLYSsiSFDLTVtSIFTPLVTGNAIIVY 1986
Cdd:PRK08043  368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTI------ADFtpndrfmsalPLFH--SFGLTV-GLFTPLLTGAEVFLY 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1987 DGEDKTALLESIVRDPRVDIIKLTPAHL-QVLKEMNIADQTAVRRMIVGGENLSTRLARSIHEQFEgrIEICNEYGPTET 2065
Cdd:PRK08043  439 PSPLHYRIVPELVYDRNCTVLFGTSTFLgNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKFG--LRILEGYGVTEC 516
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2066 --VVGCmiyrydaakdrreSVPIgtAAANTSIYVLDENMKPAPIGVPG-----EIYISGAGVARGYL---NRPELTAEKF 2135
Cdd:PRK08043  517 apVVSI-------------NVPM--AAKPGTVGRILPGMDARLLSVPGieqggRLQLKGPNIMNGYLrveKPGVLEVPTA 581
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2136 VDDPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQEEVIKEAVVTAREDVHGFKQLCAYyv 2215
Cdd:PRK08043  582 ENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLF-- 659
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 2216 sggqTTAARL-RKQLSQTLASYMVPAYFIELD-----EMPLTSNGKinkkglpaPDF-ELQDRAEY 2274
Cdd:PRK08043  660 ----TTDSELtREKLQQYAREHGVPELAVPRDirylkQLPLLGSGK--------PDFvTLKSMVDE 713
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
3311-3784 5.52e-08

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 59.33  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3311 YEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL----- 3385
Cdd:PRK12406   14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahadl 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3386 --------------------------YcgKLQDD--------IGFSGTCidlmeehfyheKDSSLALSYQSSQLAYAIYT 3431
Cdd:PRK12406   94 lhglasalpagvtvlsvptppeiaaaY--RISPAlltppagaIDWEGWL-----------AQQEPYDGPPVPQPQSMIYT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3432 SGTTGKPKGT---------LIEHRQVIHLIEGLSRQVysaydaelNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKeiv 3502
Cdd:PRK12406  161 SGTTGHPKGVrraaptpeqAAAAEQMRALIYGLKPGI--------RALLTGPLYHSAPNAYGLRAGRLGGVLVLQPR--- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3503 SDGAALCRYYRQHSIDITDGTPAH----LKL---LIAAGDLQgvTLQHLLiggealskttvnklkqlfgeHGAAPGITNV 3575
Cdd:PRK12406  230 FDPEELLQLIERHRITHMHMVPTMfirlLKLpeeVRAKYDVS--SLRHVI--------------------HAAAPCPADV 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3576 ---------------YGPTETCVDASlfnieCSSDAWARSQNYVpiGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGV 3640
Cdd:PRK12406  288 kramiewwgpviyeyYGSTESGAVTF-----ATSEDALSHPGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGN 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3641 GR-GYLNLPELTDEkfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQEAAAA 3719
Cdd:PRK12406  361 PDfTYHNKPEKRAE-------IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVF 433
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3720 ALKDADDEYYLCGYFAADK--TIQISELRKRMARHLPGYMIPAHFVQLDKMPLTPNGKLNRQLLPAP 3784
Cdd:PRK12406  434 GIPDAEFGEALMAVVEPQPgaTLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PLN02246 PLN02246
4-coumarate--CoA ligase
3261-3715 5.56e-08

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 59.22  E-value: 5.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3261 TQQEKEYLlsrFQSN--DMHYPREKTIHELFEEQAHRTPDNTAVV--FEGKQFTYEELNRRANQLARTLQAKGVQADQLV 3336
Cdd:PLN02246    2 ASASEEFI---FRSKlpDIYIPNHLPLHDYCFERLSEFSDRPCLIdgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3337 GIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL----YCGKLQD---DIGFSGTCIDLMEE--- 3406
Cdd:PLN02246   79 MLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIItqscYVDKLKGlaeDDGVTVVTIDDPPEgcl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3407 HFyhekdSSLALSYQSSQLAYAI---------YTSGTTGKPKGTLIEHRQvihLIEGLSRQV--------YSAYDAELNI 3469
Cdd:PLN02246  159 HF-----SELTQADENELPEVEIspddvvalpYSSGTTGLPKGVMLTHKG---LVTSVAQQVdgenpnlyFHSDDVILCV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3470 AMLAPYYFDASVqqMYASLLSGHTLFIVPK-EIvsdgAALCRYYRQHSIDITDGTPAhLKLLIA------AGDLQGVTLq 3542
Cdd:PLN02246  231 LPMFHIYSLNSV--LLCGLRVGAAILIMPKfEI----GALLELIQRHKVTIAPFVPP-IVLAIAkspvveKYDLSSIRM- 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3543 hLLIGGEALSKttvnKLKQLFGEHGAAPGITNVYGPTE--TCVDASLfniecssdAWARSQNYVPIGK--PLGRN-RMYI 3617
Cdd:PLN02246  303 -VLSGAAPLGK----ELEDAFRAKLPNAVLGQGYGMTEagPVLAMCL--------AFAKEPFPVKSGScgTVVRNaELKI 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3618 LD-----SKKRLQPkgvqGELYIAGDGVGRGYLNLPELTDEKfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVK 3692
Cdd:PLN02246  370 VDpetgaSLPRNQP----GEICIRGPQIMKGYLNDPEATANT------IDKDGWLHTGDIGYIDDDDELFIVDRLKELIK 439
                         490       500
                  ....*....|....*....|...
gi 166797876 3693 IQGFRIELGEIESVMLNVPDIQE 3715
Cdd:PLN02246  440 YKGFQVAPAELEALLISHPSIAD 462
prpE PRK10524
propionyl-CoA synthetase; Provisional
288-692 5.92e-08

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 59.19  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  288 HLTYRELNEKASRLARTLRNCGVQ------------PDTLVAILA-------------------------DRSLEMIVSI 330
Cdd:PRK10524   84 TYTFRQLHDEVNRMAAMLRSLGVQrgdrvliympmiAEAAFAMLAcarigaihsvvfggfashslaaridDAKPVLIVSA 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  331 IAVWKaGGAYVPLDPeypkerlqyLLHDA-------DADVLLVQHHLKNSLAFDGPVIDLNDEASYHADCSLlsPVA--G 401
Cdd:PRK10524  164 DAGSR-GGKVVPYKP---------LLDEAialaqhkPRHVLLVDRGLAPMARVAGRDVDYATLRAQHLGARV--PVEwlE 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  402 HSHLAYVIYTSGTTGKPKGVMVEHGGIVNSL----------QWKKAFFKHSPADRVlVLYPYVfdafilnFFGPLISGAT 471
Cdd:PRK10524  232 SNEPSYILYTSGTTGKPKGVQRDTGGYAVALatsmdtifggKAGETFFCASDIGWV-VGHSYI-------VYAPLLAGMA 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  472 ------LHLLPNEenketfAIQNAI-KQERITHFSTSP---RLLKTM-IEQMNREDFIHVQHVVVGGEQLETDTVEKLH- 539
Cdd:PRK10524  304 timyegLPTRPDA------GIWWRIvEKYKVNRMFSAPtaiRVLKKQdPALLRKHDLSSLRALFLAGEPLDEPTASWISe 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  540 SLQPRIrINNeYGPTEnsvvsTFHPVQSA-----DEQITIGSPVANHQAYILGAHHQI--QPIGiPGElyvGGAGVARGY 612
Cdd:PRK10524  378 ALGVPV-IDN-YWQTE-----TGWPILAIargveDRPTRLGSPGVPMYGYNVKLLNEVtgEPCG-PNE---KGVLVIEGP 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  613 LNRPELT-----EEKFVE-HLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAV 686
Cdd:PRK10524  447 LPPGCMQtvwgdDDRFVKtYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAV 526

                  ....*.
gi 166797876  687 VAREDA 692
Cdd:PRK10524  527 VGVKDA 532
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
2111-2257 6.44e-08

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 58.85  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2111 GEIYISGAGVARGYLnrPeltaekfvddPFEPGAKMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQE 2190
Cdd:PRK07445  302 GNITIQAQSLALGYY--P----------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 2191 EVIKEAVVTAREDVHGFKQLCAYYV-SGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKIN 2257
Cdd:PRK07445  370 GLVQDVCVLGLPDPHWGEVVTAIYVpKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKIN 437
PRK08162 PRK08162
acyl-CoA synthetase; Validated
4339-4504 7.65e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 58.81  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4339 EQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPE 4418
Cdd:PRK08162   25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4419 KRRAFMLKDSGADVLLT------CAGHAIpPLFEGEVLLL---DDP---------------LLYQGRTD-NLNLSCSEND 4473
Cdd:PRK08162  105 ASIAFMLRHGEAKVLIVdtefaeVAREAL-ALLPGPKPLVidvDDPeypggrfigaldyeaFLASGDPDfAWTLPADEWD 183
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 166797876 4474 LMYVIYTSGTTGQPKGVQLEHK-----TMTNLLAYE 4504
Cdd:PRK08162  184 AIALNYTSGTTGNPKGVVYHHRgaylnALSNILAWG 219
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2389-2554 9.24e-08

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 58.10  E-value: 9.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2389 HAPEGFQETQ------LRQTLQKLAEHHDALRMTFRTTENGCEAQNEEIAQSGLYRLEVMNLKEDPDPGRtIEAKADEiq 2462
Cdd:cd20484    25 NVPLCFRFSSkldvekFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDISSLKESEIIAY-LREKAKE-- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2463 sSMHLSDGPLMKAGLFQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGR-VIQLPQKTD--SFQLWAKRLSE 2538
Cdd:cd20484   102 -PFVLENGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKqPTLASSPASyyDFVAWEQDMLA 180
                         170
                  ....*....|....*.
gi 166797876 2539 YAQSEtikQEQEYWTK 2554
Cdd:cd20484   181 GAEGE---EHRAYWKQ 193
PLN02246 PLN02246
4-coumarate--CoA ligase
4357-4828 1.33e-07

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 58.07  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4357 TLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDP-----ELPEKRRAfmlkdSGAD 4431
Cdd:PLN02246   50 VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPfytpaEIAKQAKA-----SGAK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4432 VLLT--CAGHAIPPLFEGE---VLLLDDP---------LLYQGRTDNLNLSCSENDLMYVIYTSGTTGQPKGVQLEHKTM 4497
Cdd:PLN02246  125 LIITqsCYVDKLKGLAEDDgvtVVTIDDPpegclhfseLTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4498 TNLLAYEQD--HTQLRF---DRVLQFAAMsFDVcY---QEMFSALSSGGILFIIgneAKRDIRQLNDFVRTHGIQTA-FL 4568
Cdd:PLN02246  205 VTSVAQQVDgeNPNLYFhsdDVILCVLPM-FHI-YslnSVLLCGLRVGAAILIM---PKFEIGALLELIQRHKVTIApFV 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4569 PTAFLKLLASekhyfePFAECVDhiiaageqLIATRM-----------LRDML-AR-HQVTLHNHYGPSETH-VVTMYTV 4634
Cdd:PLN02246  280 PPIVLAIAKS------PVVEKYD--------LSSIRMvlsgaaplgkeLEDAFrAKlPNAVLGQGYGMTEAGpVLAMCLA 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4635 DPDTDQELQP--IGKPISNTEIFILN-EAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFvphpyDSNQRMYkTGDL 4711
Cdd:PLN02246  346 FAKEPFPVKSgsCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTI-----DKDGWLH-TGDI 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4712 ARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH---VQEAVVLAKENTDGQSDLyAYFTAEQSLSISQ--LKEKL 4786
Cdd:PLN02246  420 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHpsiADAAVVPMKDEVAGEVPV-AFVVRSNGSEITEdeIKQFV 498
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 166797876 4787 AGQIPGY-MIPS-YFIqlEKLPLTGNGKVNRRALpmpEAGLQTG 4828
Cdd:PLN02246  499 AKQVVFYkRIHKvFFV--DSIPKAPSGKILRKDL---RAKLAAG 537
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
255-429 1.36e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 58.45  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  255 TVRDFSGSRTVYQL--FEEQAertpenaavkfkndHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIA 332
Cdd:PTZ00216  100 VVKDADGKERTMEVthFNETR--------------YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYG 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  333 VWK----AGGAYVPLDpeypKERLQYLLHDADADVLL-----VQHHLK--NSLAFDGPVIDLNDE--ASYHA-DCSLLS- 397
Cdd:PTZ00216  166 IWSqsmvAATVYANLG----EDALAYALRETECKAIVcngknVPNLLRlmKSGGMPNTTIIYLDSlpASVDTeGCRLVAw 241
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876  398 --------------PVAGHSH---LAYVIYTSGTTGKPKGVMVEHGGIV 429
Cdd:PTZ00216  242 tdvvakghsagshhPLNIPENnddLALIMYTSGTTGDPKGVMHTHGSLT 290
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
289-749 1.39e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 58.26  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRN-CGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLLVQ 367
Cdd:PRK05620   39 TTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  368 HHLKNSLA-------------FDGPViDLNDEASY---HADC----SLLS--------PVAGHSHLAYVIYTSGTTGKPK 419
Cdd:PRK05620  119 PRLAEQLGeilkecpcvravvFIGPS-DADSAAAHmpeGIKVysyeALLDgrstvydwPELDETTAAAICYSTGTTGAPK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  420 GVMVEHggivnslqwkKAFFKHS----PADRVLVLYPYVFDA-----FILNFFGPL---ISGATLHLLPNEENKETFAIQ 487
Cdd:PRK05620  198 GVVYSH----------RSLYLQSlslrTTDSLAVTHGESFLCcvpiyHVLSWGVPLaafMSGTPLVFPGPDLSAPTLAKI 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  488 NAIKQERITHfsTSPRL--------LKTMIEQMNredfihVQHVVVGGEQL---------ETDTVEKLHSlqpririnne 550
Cdd:PRK05620  268 IATAMPRVAH--GVPTLwiqlmvhyLKNPPERMS------LQEIYVGGSAVppilikaweERYGVDVVHV---------- 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  551 YGPTENSVVSTF-HPVQSADEQ------ITIGS-PVA-----NHQAYILGAHHQIQpigipGELYVGGAGVARGYLNRPE 617
Cdd:PRK05620  330 WGMTETSPVGTVaRPPSGVSGEarwayrVSQGRfPASleyriVNDGQVMESTDRNE-----GEIQVRGNWVTASYYHSPT 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  618 LTE----EKFVEHLHVPGQKMY------KTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVV 687
Cdd:PRK05620  405 EEGggaaSTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVI 484
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  688 AREDADGAKQLYAYYVGEPSL-----TAAQFREELSRELPNYMIPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK05620  485 GYPDDKWGERPLAVTVLAPGIeptreTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
958-1136 2.48e-07

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 56.92  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  958 GPLMKLGLFQCPDGDH-LLIAIHHLLIDGVSWRILLEDFASGYEQAERRQT------IQLPQKTDSFP---FWADQLSky 1027
Cdd:cd19545    99 GPLVRLALVEDPDTERyFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPppfsrfVKYLRQLDDEAaaeFWRSYLA-- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1028 aaetdmEEEIAYWTELSSIKPQPLPKDTIsegsllrdseEVTIQWTkeeteqllkqANRAYNTDINDLLLTSLGLAVHKW 1107
Cdd:cd19545   177 ------GLDPAVFPPLPSSRYQPRPDATL----------EHSISLP----------SSASSGVTLATVLRAAWALVLSRY 230
                         170       180
                  ....*....|....*....|....*....
gi 166797876 1108 TGTEDIVVNLEGHGREpiIPDADISRTIG 1136
Cdd:cd19545   231 TGSDDVVFGVTLSGRN--APVPGIEQIVG 257
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
4342-4755 2.55e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 57.36  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4342 AERNPDHEAVMFgnqtLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPelpekrr 4421
Cdd:PRK12582   69 AQREPGHGQWRK----VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSP------- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4422 AFMLKDSGADVLLTCAGHAIP--------PLFEG---EVLLLDDPLLYQGRTDNLNLSCSENDLMY-------------- 4476
Cdd:PRK12582  138 AYSLMSHDHAKLKHLFDLVKPrvvfaqsgAPFARalaALDLLDVTVVHVTGPGEGIASIAFADLAAtpptaavaaaiaai 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4477 -------VIYTSGTTGQPKGVQLEHKTMTNLLAYEQdhtQLRFDRVLQFAAMSFD-VCYQEMFS-------ALSSGGILF 4541
Cdd:PRK12582  218 tpdtvakYLFTSGSTGMPKAVINTQRMMCANIAMQE---QLRPREPDPPPPVSLDwMPWNHTMGgnanfngLLWGGGTLY 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4542 IIG--------NEAKRDIRQLNdfvrthgiQTAFL--PTAFLKL---LASEKHYFEPFAECVDHIIAAGEQL---IATRM 4605
Cdd:PRK12582  295 IDDgkplpgmfEETIRNLREIS--------PTVYGnvPAGYAMLaeaMEKDDALRRSFFKNLRLMAYGGATLsddLYERM 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4606 lrDMLA----RHQVTLHNHYGPSETHVVTMyTVDPDTDQElQPIGKPISNTEIfilneagTLQPVGIVGELCISGVSLAR 4681
Cdd:PRK12582  367 --QALAvrttGHRIPFYTGYGATETAPTTT-GTHWDTERV-GLIGLPLPGVEL-------KLAPVGDKYEVRVKGPNVTP 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4682 GYHNRESLTLETFvphpydSNQRMYKTGDLARYL----PEGNIEYAGRRDHQVKI-RGYRVELGEVEAALLK----HVQE 4752
Cdd:PRK12582  436 GYHKDPELTAAAF------DEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLsTGTWVSVGTLRPDAVAacspVIHD 509

                  ...
gi 166797876 4753 AVV 4755
Cdd:PRK12582  510 AVV 512
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
290-749 3.14e-07

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 56.68  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  290 TYRELNEKASRLARTLRNCGVQPDTLVAILA---DRSLEM---IVSIIAV--------------WKAGGA---------- 339
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAwntWRHLEAwygIMGIGAIchtvnprlfpeqiaWIINHAedrvvitdlt 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  340 YVPL----DPEYPKERLQYLLHDADAdvlLVQHHLKNSLAFDgpviDLNDEAsyHADCSLLSPVAGHShlAYVIYTSGTT 415
Cdd:PRK06018  121 FVPIlekiADKLPSVERYVVLTDAAH---MPQTTLKNAVAYE----EWIAEA--DGDFAWKTFDENTA--AGMCYTSGTT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  416 GKPKGVMVEH-GGIVNSLQWKKA-FFKHSPADRVLVLYPyVF--DAFILNFFGPLiSGATLhLLPNEEnKETFAIQNAIK 491
Cdd:PRK06018  190 GDPKGVLYSHrSNVLHALMANNGdALGTSAADTMLPVVP-LFhaNSWGIAFSAPS-MGTKL-VMPGAK-LDGASVYELLD 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  492 QERITHFSTSPRLLKTMIEQMNREDFI--HVQHVVVGGEQLETDTVEKLHSLQPRIRinNEYGPTENSVVSTFHPVQ--- 566
Cdd:PRK06018  266 TEKVTFTAGVPTVWLMLLQYMEKEGLKlpHLKMVVCGGSAMPRSMIKAFEDMGVEVR--HAWGMTEMSPLGTLAALKppf 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  567 ---SADEQITI----GSPVANHQAYILGAHHQIQPIG--IPGELYVGGAGVARGYLnRPE---LTEEKFvehlhvpgqkm 634
Cdd:PRK06018  344 sklPGDARLDVlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYY-RVDgeiLDDDGF----------- 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  635 YKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAredadgakqLYAYYVGEPSLTAAQFR 714
Cdd:PRK06018  412 FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIG---------VYHPKWDERPLLIVQLK 482
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876  715 --EELSR-ELPNYM--------IPSRFIPLERIPLTSNGKIDLKAL 749
Cdd:PRK06018  483 pgETATReEILKYMdgkiakwwMPDDVAFVDAIPHTATGKILKTAL 528
PRK03584 PRK03584
acetoacetate--CoA ligase;
275-508 3.66e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 56.73  E-value: 3.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  275 RTPENAAVKFKND-----HLTYRELNEKASRLARTLRNCGVQ------------PDTLVAILAdrslemIVSIIAVWKAG 337
Cdd:PRK03584   96 RRDDRPAIIFRGEdgprrELSWAELRRQVAALAAALRALGVGpgdrvaaylpniPETVVAMLA------TASLGAIWSSC 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  338 GayvpldPEY-------------PKerlqyLL------------HDADADV------------LLVQHHLKNSLAFDGP- 379
Cdd:PRK03584  170 S------PDFgvqgvldrfgqiePK-----VLiavdgyryggkaFDRRAKVaelraalpslehVVVVPYLGPAAAAAALp 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  380 -VIDLNDEASYHADCSL-LSPVAgHSHLAYVIYTSGTTGKPKGVMVEHGGIVnsLQWKKAFFKHS---PADRVLvlypyv 454
Cdd:PRK03584  239 gALLWEDFLAPAEAAELeFEPVP-FDHPLWILYSSGTTGLPKCIVHGHGGIL--LEHLKELGLHCdlgPGDRFF------ 309
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876  455 fdafilnFF------------GPLISGATLHL------LPNEEnketfAIQNAIKQERITHFSTSPRLLKTM 508
Cdd:PRK03584  310 -------WYttcgwmmwnwlvSGLLVGATLVLydgspfYPDPN-----VLWDLAAEEGVTVFGTSAKYLDAC 369
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
3280-3687 3.74e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 56.59  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3280 PREKTIHELFEEQAHRTPDNTAVVFEG------KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGV 3353
Cdd:PRK12582   46 PYPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3354 LKAGGAYLPIdpdSPSerirYILNDSSISVLLYCGKL--------QDDIGFSGTCIDLMEE-----HFYHEKDSSLALSY 3420
Cdd:PRK12582  126 MQAGVPAAPV---SPA----YSLMSHDHAKLKHLFDLvkprvvfaQSGAPFARALAALDLLdvtvvHVTGPGEGIASIAF 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3421 Q-------SSQLAYAI------------YTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYDAELNIAM--LAPYYFDA 3479
Cdd:PRK12582  199 AdlaatppTAAVAAAIaaitpdtvakylFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdwMPWNHTMG 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3480 SVQQMYASLLSGHTLFI-----VPKEIVSDGAALcryyRQHSIDITDGTPAHLKLLIAAGDLQGV-------TLQHLLIG 3547
Cdd:PRK12582  279 GNANFNGLLWGGGTLYIddgkpLPGMFEETIRNL----REISPTVYGNVPAGYAMLAEAMEKDDAlrrsffkNLRLMAYG 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3548 GEALSKTTVNKLKQL-FGEHGAAPGITNVYGPTETCVDAslfniecSSDAWARSQNYVpIGKPL-GrnrmyildSKKRLQ 3625
Cdd:PRK12582  355 GATLSDDLYERMQALaVRTTGHRIPFYTGYGATETAPTT-------TGTHWDTERVGL-IGLPLpG--------VELKLA 418
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 3626 PKGVQGELYIAGDGVGRGYLNLPELTDEKFvadpfvPEDRMYRTGDLARLL----PDGNIEYIGRI 3687
Cdd:PRK12582  419 PVGDKYEVRVKGPNVTPGYHKDPELTAAAF------DEEGFYRLGDAARFVdpddPEKGLIFDGRV 478
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
3310-3713 4.68e-07

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 56.34  E-value: 4.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3310 TYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIR---YILNDSSISVLLY 3386
Cdd:cd05908    17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKLklnKVWNTLKNPYLIT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3387 CGKLQDDigfsgtcidlMEEHfyhekdsslalsyqssqLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVysAYDAE 3466
Cdd:cd05908    97 EEEVLCE----------LADE-----------------LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST--EWKTK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3467 LNIAMLAPYYFDASVQQMY-ASLLSGHTLFIVPKEIVSDGAALCRY-YRQHSIDITDGTPAHLKLLIA------AGDLQG 3538
Cdd:cd05908   148 DRILSWMPLTHDMGLIAFHlAPLIAGMNQYLMPTRLFIRRPILWLKkASEHKATIVSSPNFGYKYFLKtlkpekANDWDL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3539 VTLQHLLIGGEALSKTTVNKLKQLFGEHG-AAPGITNVYGPTETCVDASLFN--------------------IECSSDAW 3597
Cdd:cd05908   228 SSIRMILNGAEPIDYELCHEFLDHMSKYGlKRNAILPVYGLAEASVGASLPKaqspfktitlgrrhvthgepEPEVDKKD 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3598 ARSQNYVPIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVADPFVpedrmyRTGDLArLLP 3677
Cdd:cd05908   308 SECLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIR 380
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 166797876 3678 DGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:cd05908   381 NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGV 416
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
3422-3711 4.75e-07

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 56.66  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3422 SSQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGL--------SRQVYSAYDAELNIAMLAPYYFDASVQQM--YASLLS- 3490
Cdd:PLN02387  249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVmtvvpklgKNDVYLAYLPLAHILELAAESVMAAVGAAigYGSPLTl 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3491 ------------------GHTLFI-VP-----------KEIVSDGAALCR-----YYRQHS-IDIT-DGTPAHLKLL--- 3530
Cdd:PLN02387  329 tdtsnkikkgtkgdasalKPTLMTaVPaildrvrdgvrKKVDAKGGLAKKlfdiaYKRRLAaIEGSwFGAWGLEKLLwda 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3531 -----IAAgdLQGVTLQHLLIGGEALSKTTVNKLKQLFGehgaAPgITNVYGPTETCVDASLFNIECSSDA--------- 3596
Cdd:PLN02387  409 lvfkkIRA--VLGGRIRFMLSGGAPLSGDTQRFINICLG----AP-IGQGYGLTETCAGATFSEWDDTSVGrvgpplpcc 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3597 ------WArSQNYVPIGKPLGRnrmyildskkrlqpkgvqGELYIAGDGVGRGYLNLPELTDEKFVADpfvpED--RMYR 3668
Cdd:PLN02387  482 yvklvsWE-EGGYLISDKPMPR------------------GEIVIGGPSVTLGYFKNQEKTDEVYKVD----ERgmRWFY 538
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 166797876 3669 TGDLARLLPDGNIEYIGRIDHQVKIQ-GFRIELGEIESVMLNVP 3711
Cdd:PLN02387  539 TGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
30-222 5.40e-07

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 55.79  E-value: 5.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   30 ADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDRTSLILGIPTVSK-QKAGQSAVN- 107
Cdd:cd20484   206 ADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRpEERFDSLIGy 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  108 --NIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMPLIHT------VVSLNEIHSLQCK- 178
Cdd:cd20484   286 fiNMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVaffyqnFLQSTSLQQFLAEy 365
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  179 ---------EDTATDTLFHFDLE----NNGIHLKLFYNGNLYDERYINQIVSHLDQL 222
Cdd:cd20484   366 qdvlsiefvEGIHQEGEYELVLEvyeqEDRFTLNIKYNPDLFDASTIERMMEHYVKL 422
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
3427-3781 6.12e-07

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 55.85  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3427 YAIYTSGTTGKPKGTLIEHRQV-IHLIEGLSRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFIVPKeivSDG 3505
Cdd:cd05929   129 KMLYSGGTTGRPKGIKRGLPGGpPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEK---FDP 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3506 AALCRYYRQHSIDITDGTPAHLKLLiaagdlqgvtlqhLLIGGEALSKTTVNKLKQLFgeHGAAPG-------------- 3571
Cdd:cd05929   206 EEFLRLIERYRVTFAQFVPTMFVRL-------------LKLPEAVRNAYDLSSLKRVI--HAAAPCppwvkeqwidwggp 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3572 -ITNVYGPTEtcvdASLFNIeCSSDAWARSQNYVpiGKPLGrNRMYILDSKKRLQPKGVQGELYIAGdGVGRGYLNLPEL 3650
Cdd:cd05929   271 iIWEYYGGTE----GQGLTI-INGEEWLTHPGSV--GRAVL-GKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEK 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3651 TDEKfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDI--------------QEA 3716
Cdd:cd05929   342 TAAA------RNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVldaavvgvpdeelgQRV 415
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3717 AAAALKDADdeyylcgyfaADKTIQISE-----LRKRMARhlpgYMIPAHFVQLDKMPLTPNGKLNRQLL 3781
Cdd:cd05929   416 HAVVQPAPG----------ADAGTALAEeliafLRDRLSR----YKCPRSIEFVAELPRDDTGKLYRRLL 471
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
4353-4494 6.25e-07

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 55.76  E-value: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4353 FGNQTLTYRQLNERSNQLARVLQDK-GACTDQVVAVLTDRSAHMIIGILAILKAG--AAFLPIDPelpeKRRAFM--LKD 4427
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNTNI----RSKSLLhcFRC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4428 SGADVLLTCaghaiPPLFEG--EVL--LLDD--PLLYQGRTDNLN--------LSCSENDL---------------MYvI 4478
Cdd:cd05938    77 CGAKVLVVA-----PELQEAveEVLpaLRADgvSVWYLSHTSNTEgvislldkVDAASDEPvpaslrahvtikspaLY-I 150
                         170
                  ....*....|....*.
gi 166797876 4479 YTSGTTGQPKGVQLEH 4494
Cdd:cd05938   151 YTSGTTGLPKAARISH 166
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
288-717 6.55e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 55.92  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  288 HLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAG-------GAYvplDPEYPKERLQyllhDAD 360
Cdd:PRK00174   98 KITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGF---SAEALADRII----DAG 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  361 ADVLLV---------QHHLKNSL--AFDGP-----VI--------------------DLNDEASyhADCSllsPVAGHS- 403
Cdd:PRK00174  171 AKLVITadegvrggkPIPLKANVdeALANCpsvekVIvvrrtggdvdwvegrdlwwhELVAGAS--DECE---PEPMDAe 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 HLAYVIYTSGTTGKPKGVMVEHGGIvnsLQWKKAFFKhspadrvlvlypYVFD-------------------AFILnfFG 464
Cdd:PRK00174  246 DPLFILYTSGSTGKPKGVLHTTGGY---LVYAAMTMK------------YVFDykdgdvywctadvgwvtghSYIV--YG 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  465 PLISGATLHLL---PNEENKETFAiqNAIKQERITHFSTSPRLLKTMIEQmnredfihvqhvvvgGEQLETDTveKLHSL 541
Cdd:PRK00174  309 PLANGATTLMFegvPNYPDPGRFW--EVIDKHKVTIFYTAPTAIRALMKE---------------GDEHPKKY--DLSSL 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  542 qpRI------RINNE----Y----GPTENSVVSTFHpvQSADEQITIgSPVAnhqayilGAHHQ-----IQPI-GIPGEL 601
Cdd:PRK00174  370 --RLlgsvgePINPEawewYykvvGGERCPIVDTWW--QTETGGIMI-TPLP-------GATPLkpgsaTRPLpGIQPAV 437
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  602 Y------VGGAGvaRGYL--NRP----ELT----EEKFVEHL--HVPGqkMYKTGDLARWLPDGRIEYLGRIDHQVKIRG 663
Cdd:PRK00174  438 VdeegnpLEGGE--GGNLviKDPwpgmMRTiygdHERFVKTYfsTFKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSG 513
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876  664 YRIEIGEVEAAMFNLENVREAAVVAREDADGAKQLYAYYV---GEPslTAAQFREEL 717
Cdd:PRK00174  514 HRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkgGEE--PSDELRKEL 568
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
2381-2677 6.65e-07

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 55.40  E-value: 6.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2381 YYNQAVmLHAPEGFQETQLRQTLQKLAEHHDALRMTFRTtengceaqnEEIAQSGLY-RLEVMN-------LKEDPDPGR 2452
Cdd:cd19547    24 YFNQNV-LELVGGTDEDVLREAWRRVADRYEILRTGFTW---------RDRAEPLQYvRDDLAPpwalldwSGEDPDRRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2453 TIEAK--ADEIQSSMHLSDGPLMKAGLFQCADGDHLLI-AIHHLIIDGISWRILLEDIVSGYKQAENGRVIQLP--QKTD 2527
Cdd:cd19547    94 ELLERllADDRAAGLSLADCPLYRLTLVRLGGGRHYLLwSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSpcRPYR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2528 SFQLWAKrlSEYAQSEtikQEQEYWTKIEQtEVKPLPkdfheTHTTAKDSE----TAAVEWTKEETElLLKQANRAYHTE 2603
Cdd:cd19547   174 DYVRWIR--ARTAQSE---ESERFWREYLR-DLTPSP-----FSTAPADREgefdTVVHEFPEQLTR-LVNEAARGYGVT 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2604 INDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDIsrTVGWFTSLYPVVLHAQPGKEISDYIKTTKEGL 2677
Cdd:cd19547   242 TNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
4472-4815 7.24e-07

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 55.57  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4472 NDLMYVIYTSGTTGQPKGVQLEHKTM-TNLLAYEQDHTQLRFDRVLQFAAMSFDVcyqemfsALSSGGILFIIGNeAKRD 4550
Cdd:cd05908   106 DELAFIQFSSGSTGDPKGVMLTHENLvHNMFAILNSTEWKTKDRILSWMPLTHDM-------GLIAFHLAPLIAG-MNQY 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4551 IRQLNDFVR----------THGIQTAFLPT----AFLKLLASEKhyfepfAECVD----HIIAAGEQLIATRM---LRDM 4609
Cdd:cd05908   178 LMPTRLFIRrpilwlkkasEHKATIVSSPNfgykYFLKTLKPEK------ANDWDlssiRMILNGAEPIDYELcheFLDH 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4610 LARHQV---TLHNHYGPSETHV--------------------VTMYTVDPDTDQELQ------PIGKPISNTEIFILNEA 4660
Cdd:cd05908   252 MSKYGLkrnAILPVYGLAEASVgaslpkaqspfktitlgrrhVTHGEPEPEVDKKDSecltfvEVGKPIDETDIRICDED 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4661 GTLQPVGIVGELCISGVSLARGYHNRESLTLETFVPHPYdsnqrmYKTGDLArYLPEGNIEYAGRRDHQVKIRGYRV--- 4737
Cdd:cd05908   332 NKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVyph 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4738 ------------ELGEVEAALL---KHVQEAVVLAKENTDGQSDLYAYftaeqslsiSQLKEKLAGQIPGYMIpSYFIQL 4802
Cdd:cd05908   405 dieriaeelegvELGRVVACGVnnsNTRNEEIFCFIEHRKSEDDFYPL---------GKKIKKHLNKRGGWQI-NEVLPI 474
                         410
                  ....*....|...
gi 166797876 4803 EKLPLTGNGKVNR 4815
Cdd:cd05908   475 RRIPKTTSGKVKR 487
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
4946-5344 7.52e-07

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 56.21  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4946 YNMTGILETEGKLPLNRLLTAFQRLMQGHEPLRTVVEMVREEAVQVIKSQVEFSMERYE--ATADEVEECFRAFVRPfDL 5023
Cdd:PRK10252   30 WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEIIdlRTQPDPHAAAQALMQA-DL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5024 SQA-------PLLRAGLIELEQDLHIFMFDMHHIITDGASMNIFVEKLIQLY---------DGKELAPLRIQYKDFTEWK 5087
Cdd:PRK10252  109 QQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYcawlrgeptPASPFTPFADVVEEYQRYR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5088 hQKEQRERIKSqeeYWLGVFHEELPSFELPKdfARPPVRSFDGKRHNFTLDKTVTQGIKQLEELTGSTAYMILFSAYSIL 5167
Cdd:PRK10252  189 -ASEAWQRDAA---FWAEQRRQLPPPASLSP--APLPGRSASADILRLKLEFTDGAFRQLAAQASGVQRPDLALALVALW 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5168 LAKYSGQDDIVVGTPIAGRPHADLEPIIGMFVNTLAIRTAPMAEKTFLDYITETKETMLKAFEHQEYPFEELVeklgvkR 5247
Cdd:PRK10252  263 LGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIV------R 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 5248 DLSR----NPLFDTMF-VLQNTEQTDI-EVDSLAvrpyEQTETAAKFDLQLNFLID-QDEIQGSFDYCTKLFKKKTIAVL 5320
Cdd:PRK10252  337 DSGRaagdEPLFGPVLnIKVFDYQLDFpGVQAQT----HTLATGPVNDLELALFPDeHGGLSIEILANPQRYDEATLIAH 412
                         410       420
                  ....*....|....*....|....
gi 166797876 5321 AKDYVMILSAIMRNPSIPLKDIQL 5344
Cdd:PRK10252  413 AERLKALIAQFAADPALLCGDVDI 436
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
4472-4728 7.70e-07

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 55.68  E-value: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4472 NDLMYVIYTSGTTGQPKGVQLEHKTMTNLLA----YEQDHTQLR-FDRVLQFAAMS--FDVCYQEMFsaLSSGG-ILFII 4543
Cdd:cd05927   114 EDLATICYTSGTTGNPKGVMLTHGNIVSNVAgvfkILEILNKINpTDVYISYLPLAhiFERVVEALF--LYHGAkIGFYS 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4544 GneakrDIRQLND----------------FVRTH-GIQTAFLPTAFLK-------------LLASEKHYFEPFAE-CVDH 4592
Cdd:cd05927   192 G-----DIRLLLDdikalkptvfpgvprvLNRIYdKIFNKVQAKGPLKrklfnfalnyklaELRSGVVRASPFWDkLVFN 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4593 IIAAG-----EQLI--ATRMLRDMLARHQVTLHNH----YGPSETHVVTMYTVDPDTDqeLQPIGKPISNTEI------- 4654
Cdd:cd05927   267 KIKQAlggnvRLMLtgSAPLSPEVLEFLRVALGCPvlegYGQTECTAGATLTLPGDTS--VGHVGGPLPCAEVklvdvpe 344
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 4655 ---FILNEAGTlqpvgivGELCISGVSLARGYHNRESLTLETFvphpyDSNQrMYKTGDLARYLPEGNIEYAGRRDH 4728
Cdd:cd05927   345 mnyDAKDPNPR-------GEVCIRGPNVFSGYYKDPEKTAEAL-----DEDG-WLHTGDIGEWLPNGTLKIIDRKKN 408
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
293-744 8.60e-07

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 55.54  E-value: 8.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  293 ELNEKASRLARTLRNCGvqPDTLVAILADRSLEMIVSIIAVWKAGGAyVPLDP---------EYPKERLQYLLHDADADV 363
Cdd:PRK05851   36 EVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAA-VSILPgpvrgaddgRWADATLTRFAGIGVRTV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  364 LLVQHHLKNSLAFDG--PVIDLNDEASYHADCSLLSPvaGHSHLAYVIYTSGTTGKPKGVMVEHGGIVNSLqwkKAFFKH 441
Cdd:PRK05851  113 LSHGSHLERLRAVDSsvTVHDLATAAHTNRSASLTPP--DSGGPAVLQGTAGSTGTPRTAILSPGAVLSNL---RGLNAR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  442 ----SPADRVLVLYPYVFD---AFILNFFgplISGATLHLLPneenkeTFAIQNA-------IKQERIThFSTSPRLLKT 507
Cdd:PRK05851  188 vgldAATDVGCSWLPLYHDmglAFLLTAA---LAGAPLWLAP------TTAFSASpfrwlswLSDSRAT-LTAAPNFAYN 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  508 MIEQMNRE----DFIHVQHVVVGGEQLETDTVEKLHSLQPRIRIN-----NEYGPTENSVVST---------FHPVQSAD 569
Cdd:PRK05851  258 LIGKYARRvsdvDLGALRVALNGGEPVDCDGFERFATAMAPFGFDagaaaPSYGLAESTCAVTvpvpgiglrVDEVTTDD 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  570 EQIT-----IGSPVANHQAYILGAHHqiqPIGIP----GELYVGGAGVARGYLNRPELTeekfvehlhvPGQkMYKTGDL 640
Cdd:PRK05851  338 GSGArrhavLGNPIPGMEVRISPGDG---AAGVAgreiGEIEIRGASMMSGYLGQAPID----------PDD-WFPTGDL 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  641 ArWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLENVREAAVVAREDADGAKQ----LYAYYVGePSLTAAqfREE 716
Cdd:PRK05851  404 G-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARpglvIAAEFRG-PDEAGA--RSE 479
                         490       500       510
                  ....*....|....*....|....*....|..
gi 166797876  717 LSRELPNY--MIPSR--FIPLERIPLTSNGKI 744
Cdd:PRK05851  480 VVQRVASEcgVVPSDvvFVAPGSLPRTSSGKL 511
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
289-663 8.76e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 55.51  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  289 LTYRELNEKASRLARTLRNCGvQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPL-DPEYP--KERLQYLLHDADADVLL 365
Cdd:PRK07769   56 LTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAIL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  366 --------VQHHLKNSLAFDGPVIDLNDEASYHADCSLLSPVAGHSHLAYVIYTSGTTGKPKGVMVEHGGI-VNSLQWKK 436
Cdd:PRK07769  135 tttdsaegVRKFFRARPAKERPRVIAVDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLpTNVLQVID 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  437 AfFKHSPADRVLVLYPYVFDAFILNFFGPLISGATLHLL--------PNEENKETFAIQNaikqERITHFSTSPRLL--K 506
Cdd:PRK07769  215 A-LEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMspaafvrrPGRWIRELARKPG----GTGGTFSAAPNFAfeH 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  507 TMIEQMNRE-----DFIHVQHVVVGGEQLETDTVEKL------HSLQPRIrINNEYGPTENSV-VST------------- 561
Cdd:PRK07769  290 AAARGLPKDgepplDLSNVKGLLNGSEPVSPASMRKFneafapYGLPPTA-IKPSYGMAEATLfVSTtpmdeeptviyvd 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  562 --------FHPVQSADE----QITIGSPVANHQAYILGAHHQI-QPIGIPGELYVGGAGVARGYLNRPELTEEKFVEHLH 628
Cdd:PRK07769  369 rdelnagrFVEVPADAPnavaQVSAGKVGVSEWAVIVDPETASeLPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILK 448
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 166797876  629 VP-----------GQKMYKTGDLARWLpDGRIEYLGRIDHQVKIRG 663
Cdd:PRK07769  449 SRlseshaegapdDALWVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
3310-3687 9.16e-07

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 55.44  E-value: 9.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3310 TYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL---- 3385
Cdd:cd05933    10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVvenq 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3386 -----------YCGKLQDDIGFSG----------TCIDLME------EHFYHEKDSSLalsyQSSQLAYAIYTSGTTGKP 3438
Cdd:cd05933    90 kqlqkilqiqdKLPHLKAIIQYKEplkekepnlySWDEFMElgrsipDEQLDAIISSQ----KPNQCCTLIYTSGTTGMP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3439 KGTLIEH----------RQVIHLIEGLSRQ--VYS----------AYDAELNIAMLAPYYFdASVQQMYASLLSG----- 3491
Cdd:cd05933   166 KGVMLSHdnitwtakaaSQHMDLRPATVGQesVVSylplshiaaqILDIWLPIKVGGQVYF-AQPDALKGTLVKTlrevr 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3492 HTLFI-VPK------EIVSDGAALCRYYRQhsiditdgtpahlKLLIAAgdlQGVTLQH--LLIGGEA--------LSKT 3554
Cdd:cd05933   245 PTAFMgVPRvwekiqEKMKAVGAKSGTLKR-------------KIASWA---KGVGLETnlKLMGGESpsplfyrlAKKL 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3555 TVNKLKQLFG-EH------GAAP--------------GITNVYGPTETcvdASLFNIeCSSDAWarsqNYVPIGKPLGRN 3613
Cdd:cd05933   309 VFKKVRKALGlDRcqkfftGAAPisretlefflslniPIMELYGMSET---SGPHTI-SNPQAY----RLLSCGKALPGC 380
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 3614 RMYILDskkrlQPKGVQGELYIAGDGVGRGYLNLPELTDEKfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRI 3687
Cdd:cd05933   381 KTKIHN-----PDADGIGEICFWGRHVFMGYLNMEDKTEEA------IDEDGWLHSGDLGKLDEDGFLYITGRI 443
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
3614-3685 9.91e-07

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 54.62  E-value: 9.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 3614 RMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNLPELTDEKFVadpfvpeDRMYRTGDLARLLPDGNIEYIG 3685
Cdd:cd17636   173 QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGWHHTNDLGRREPDGSLSFVG 237
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
4356-4760 1.22e-06

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 54.91  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4356 QTLTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLLT 4435
Cdd:cd17639     4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4436 caghaipplfegevlllddpllyqgrtdnlnlSCSENDLMYVIYTSGTTGQPKGVQLEHKTMTNLLA------YEQDHTQ 4509
Cdd:cd17639    84 --------------------------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAglgdrvPELLGPD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4510 lrfDRVLQF--AAMSFDVCYQemFSALSSGGIL-FiiGNeakrdIRQLND--FVRTHGIQTAFLPTAF------------ 4572
Cdd:cd17639   132 ---DRYLAYlpLAHIFELAAE--NVCLYRGGTIgY--GS-----PRTLTDksKRGCKGDLTEFKPTLMvgvpaiwdtirk 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4573 ----------------------LKLLASEKHYFEPFAEC-------------VDHIIAAGEQL-IATR-----MLRDMLa 4611
Cdd:cd17639   200 gvlaklnpmgglkrtlfwtayqSKLKALKEGPGTPLLDElvfkkvraalggrLRYMLSGGAPLsADTQeflniVLCPVI- 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4612 rhqvtlhNHYGPSEThvVTMYTVDPDTDQELQPIGKPISNTEIFILN--EAG--TLQPVGiVGELCISGVSLARGYHNRE 4687
Cdd:cd17639   279 -------QGYGLTET--CAGGTVQDPGDLETGRVGPPLPCCEIKLVDweEGGysTDKPPP-RGEILIRGPNVFKGYYKNP 348
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 4688 SLTLETFVPhpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKIR-GYRVELGEVEAALLKH--VQEAVVLAKEN 4760
Cdd:cd17639   349 EKTKEAFDG------DGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNplVNNICVYADPD 418
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1917-2257 1.33e-06

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 55.36  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1917 AYVIYTSGSTGRPKGVLIEHGG-LTNYIWWAKEVYVKGEKANF---PLYSSisFDLTVTSIFtPLVTGNAIIVYdgedkt 1992
Cdd:PRK06814  796 AVILFTSGSEGTPKGVVLSHRNlLANRAQVAARIDFSPEDKVFnalPVFHS--FGLTGGLVL-PLLSGVKVFLY------ 866
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1993 allesivrdPrvdiiklTPAHLQVLKEM--------------------NIA---DQTAVRRMIVGGENLSTRLARSIHEQ 2049
Cdd:PRK06814  867 ---------P-------SPLHYRIIPELiydtnatilfgtdtflngyaRYAhpyDFRSLRYVFAGAEKVKEETRQTWMEK 930
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2050 FegRIEICNEYGPTETVvgcmiyrydaakdrresvPIgtAAANTSIY-----------VLDENMKPAPiGVP--GEIYIS 2116
Cdd:PRK06814  931 F--GIRILEGYGVTETA------------------PV--IALNTPMHnkagtvgrllpGIEYRLEPVP-GIDegGRLFVR 987
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2117 GAGVARGYLNrpeltAEK-FVDDPFEPGakMYKTGDLAKWLADGNIEYAGRIDEQVKIRGYRIELGEIEAalLQEEVIKE 2195
Cdd:PRK06814  988 GPNVMLGYLR-----AENpGVLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAELWPD 1058
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2196 A--VVTAREDVHGFKQLCAYYVSGGQTTAARLRKQLSQTLASYMVPAYFIELDEMPLTSNGKIN 2257
Cdd:PRK06814 1059 AlhAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
3425-3715 1.62e-06

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 54.77  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3425 LAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSAYDAELNIAMLaPYYFDASVQQMYASLLSGHTLFIVPKEIVS- 3503
Cdd:cd17632   225 LALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFM-PMSHIAGRISLYGTLARGGTAYFAAASDMSt 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3504 --DGAALCR-----------------YYRQHSIDITDGTPAhlkllIAAGDLQGVTLQHLLIGGEALSKTTvnklkqlfg 3564
Cdd:cd17632   304 lfDDLALVRptelflvprvcdmlfqrYQAELDRRSVAGADA-----ETLAERVKAELRERVLGGRLLAAVC--------- 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3565 ehGAAPGITNVYGPTETCVDASLFNIECSSDAWARSQNYVPIGKPlgrnrmyILDSK------------KRLQPKGvqgE 3632
Cdd:cd17632   370 --GSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILDGVIVRPP-------VLDYKlvdvpelgyfrtDRPHPRG---E 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3633 LYIAGDGVGRGYLNLPELTDEKFVADPFvpedrmYRTGD-LARLLPDgNIEYIGRIDHQVKI-QGFRIELGEIESVMLNV 3710
Cdd:cd17632   438 LLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAAS 510

                  ....*
gi 166797876 3711 PDIQE 3715
Cdd:cd17632   511 PLVRQ 515
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
69-223 1.84e-06

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 53.92  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   69 YLILLAGIECLLYKYTDRTSLILGIPTVSK-QKAGQSAVN---NIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPF 144
Cdd:cd19539   248 FMVLLAAYCVLLRRYTGQTDIVVGTPVAGRnHPRFESTVGffvNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPF 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  145 RKMARHLSVQYNDEHMPLIHTV--------VSLNEIHSLQCKEDTATDTLFHFDL------ENNGIHLKLFYNGNLYDER 210
Cdd:cd19539   328 QQLVAELPVDRDAGRHPLVQIVfqvtnapaGELELAGGLSYTEGSDIPDGAKFDLnltvteEGTGLRGSLGYATSLFDEE 407
                         170
                  ....*....|...
gi 166797876  211 YINQIVSHLDQLL 223
Cdd:cd19539   408 TIQGFLADYLQVL 420
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
3429-3709 1.97e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 54.34  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3429 IYTSGTTGKPKGTLIEHRQvihliegLSRQVYSAYDAelniAMLAPYYFDASVQQM-----------YASLLSGHTLFIV 3497
Cdd:PTZ00342  310 VYTSGTSGKPKGVMLSNKN-------LYNTVVPLCKH----SIFKKYNPKTHLSYLpishiyerviaYLSFMLGGTINIW 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3498 PKEI--------VSDGAAL-------CRYYRQHSIDItDGTPAHLKLLIA--------------AGDLQGVT-------- 3540
Cdd:PTZ00342  379 SKDInyfskdiyNSKGNILagvpkvfNRIYTNIMTEI-NNLPPLKRFLVKkilslrksnnnggfSKFLEGIThisskikd 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3541 -----LQHLLIGGEALSKTTVNKLKQLFGEHgaapgITNVYGPTET-----CVDASLFNIECssdawarsqnyvpIGKPL 3610
Cdd:PTZ00342  458 kvnpnLEVILNGGGKLSPKIAEELSVLLNVN-----YYQGYGLTETtgpifVQHADDNNTES-------------IGGPI 519
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3611 GRNRMY------ILDSKKRLqPKGvqgELYIAGDGVGRGYLNLPELTDEKFVadpfvpEDRMYRTGDLARLLPDGNIEYI 3684
Cdd:PTZ00342  520 SPNTKYkvrtweTYKATDTL-PKG---ELLIKSDSIFSGYFLEKEQTKNAFT------EDGYFKTGDIVQINKNGSLTFL 589
                         330       340
                  ....*....|....*....|....*.
gi 166797876 3685 GRIDHQVKIQGfrielGE-IESVMLN 3709
Cdd:PTZ00342  590 DRSKGLVKLSQ-----GEyIETDMLN 610
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
3306-3445 2.13e-06

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 53.97  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3306 GKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYILNDSSISVLL 3385
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3386 YcgKLQDDigfsgtcidlMEEHFYHEKDSSLALSYQSsQLAYaIYTSGTTGKPKGTLIEH 3445
Cdd:cd05939    81 F--NLLDP----------LLTQSSTEPPSQDDVNFRD-KLFY-IYTSGTTGLPKAAVIVH 126
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2278-2350 2.20e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 48.79  E-value: 2.20e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876   2278 RTKAEEILVSAWESVLGAENVSILD---NFFDLGGDSIKSIQVSSRLNQQ-GYKMEIKDLFQYATIAELSPHIKQNL 2350
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAAEL 86
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
3296-3792 2.69e-06

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 53.86  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3296 TPDNTAVVFEG------KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAG-------GAYLP 3362
Cdd:cd05967    64 RGDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3363 ------IDPDSP------------SERIRYI-LNDSSIS--------VLLYC-GKLQDDIGFSGTCID---LMEEHFYHE 3411
Cdd:cd05967   144 kelasrIDDAKPklivtascgiepGKVVPYKpLLDKALElsghkphhVLVLNrPQVPADLTKPGRDLDwseLLAKAEPVD 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3412 kdsslALSYQSSQLAYAIYTSGTTGKPKGtliehrqVIHLIEGlsrqvysaYDAELNIAMLAPY-------YFDAS---- 3480
Cdd:cd05967   224 -----CVPVAATDPLYILYTSGTTGKPKG-------VVRDNGG--------HAVALNWSMRNIYgikpgdvWWAASdvgw 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3481 -VQQ---MYASLLSGHTLFIVPKEIVS--DGAALCRYYRQHSIDITDGTPAHLKLlIAAGDLQGV--------TLQHLLI 3546
Cdd:cd05967   284 vVGHsyiVYGPLLHGATTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRA-IRKEDPDGKyikkydlsSLRTLFL 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3547 GGEALSKTTVNKLKQLFGehgaAPGITNvYGPTET--CVDASLFNIECssdawarsqnyVPI-----GKPLGRNRMYILD 3619
Cdd:cd05967   363 AGERLDPPTLEWAENTLG----VPVIDH-WWQTETgwPITANPVGLEP-----------LPIkagspGKPVPGYQVQVLD 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3620 SKKRLQPKGVQGELYIAGDgVGRGYLNLPELTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIE 3699
Cdd:cd05967   427 EDGEPVGPNELGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLS 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3700 LGEIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS------ELRKRMARHLPGYMIPAHFVQLDKMPLTPN 3773
Cdd:cd05967   506 TGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelekELVALVREQIGPVAAFRLVIFVKRLPKTRS 585
                         570
                  ....*....|....*....
gi 166797876 3774 GKLNRQLLPAPVKKRDSGI 3792
Cdd:cd05967   586 GKILRRTLRKIADGEDYTI 604
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
3422-3715 2.85e-06

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 53.62  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3422 SSQLAYAIY-TSGTTGKPKgtLIEHRQVIHLIeGL---SRQVYSAYDAELNIAMLAPYYFDASVQQMYASLLSGHTLFI- 3496
Cdd:cd05928   172 GSQEPMAIYfTSGTTGSPK--MAEHSHSSLGL-GLkvnGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVh 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3497 -VPKeivSDGAALCRYYRQHSIDITDGTPAHLKLLIAAgDL---QGVTLQHLLIGGEALSKTTVNKLKQLFGEHgaapgI 3572
Cdd:cd05928   249 hLPR---FDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLssyKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-----I 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3573 TNVYGPTET---CVDASLFNIECSSdawarsqnyvpIGKPLGRNRMYILDSKKRLQPKGVQGELYIAGD-----GVGRGY 3644
Cdd:cd05928   320 YEGYGQTETgliCANFKGMKIKPGS-----------MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGY 388
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166797876 3645 LNLPELTDEKFVADpfvpedrMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05928   389 VDNPEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVE 452
PRK08162 PRK08162
acyl-CoA synthetase; Validated
3297-3682 3.51e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 53.41  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3297 PDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSERIRYIL 3376
Cdd:PRK08162   32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3377 NDSSISVLLYcgklqdDIGFSGTCIDLMEE-------------------HFYHEKDSSLALSYQSSQLAY--------AI 3429
Cdd:PRK08162  112 RHGEAKVLIV------DTEFAEVAREALALlpgpkplvidvddpeypggRFIGALDYEAFLASGDPDFAWtlpadewdAI 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3430 ---YTSGTTGKPKGTLIEHRqvihlieglsrqvySAY-DAELNIAMLA----PYY-------------FDASVqqmyaSL 3488
Cdd:PRK08162  186 alnYTSGTTGNPKGVVYHHR--------------GAYlNALSNILAWGmpkhPVYlwtlpmfhcngwcFPWTV-----AA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3489 LSGHTLF---IVPKEIVSDgaalcryYRQHSIDITDGTPAHLKLLI-AAGDLQGVTLQ--HLLIGGEALSKTTVNKLKQL 3562
Cdd:PRK08162  247 RAGTNVClrkVDPKLIFDL-------IREHGVTHYCGAPIVLSALInAPAEWRAGIDHpvHAMVAGAAPPAAVIAKMEEI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3563 fgehgaapGI--TNVYGPTETCVDASLfnieCssdAWARSQNYVPIGKPLGRN-----RMYILDSKKRLQPKGVQ----- 3630
Cdd:PRK08162  320 --------GFdlTHVYGLTETYGPATV----C---AWQPEWDALPLDERAQLKarqgvRYPLQEGVTVLDPDTMQpvpad 384
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876 3631 ----GELYIAGDGVGRGYLNLPELTDEKFvadpfvpEDRMYRTGDLARLLPDGNIE 3682
Cdd:PRK08162  385 getiGEIMFRGNIVMKGYLKNPKATEEAF-------AGGWFHTGDLAVLHPDGYIK 433
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
4476-4818 3.98e-06

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 53.15  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4476 YVIYTSGTTGQPKGVQLEH---KTMTNLLAYEQDHTQLRFDRV-LQFAAMSFDVCYQEMFSALSSGGILFIIGN-EAKRD 4550
Cdd:cd05929   129 KMLYSGGTTGRPKGIKRGLpggPPDNDTLMAAALGFGPGADSVyLSPAPLYHAAPFRWSMTALFMGGTLVLMEKfDPEEF 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4551 IRqlndFVRTHGIQ-TAFLPTAFLKLLA--SEKHYFEPFAECVDHIIAAGEQLIATRmlRDMLARHQVTLHNHYGPSETH 4627
Cdd:cd05929   209 LR----LIERYRVTfAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVK--EQWIDWGGPIIWEYYGGTEGQ 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4628 VVTMYtvdpDTDQELQ---PIGKPISNtEIFILNEAGTLQPVGIVGELCISGVSlARGYHNRESLTLETFVPHPYDSnqr 4704
Cdd:cd05929   283 GLTII----NGEEWLThpgSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWST--- 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4705 mykTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTD-GQSDLYAYFTAEQSLSISQ 4781
Cdd:cd05929   354 ---LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHpkVLDAAVVGVPDEElGQRVHAVVQPAPGADAGTA 430
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 166797876 4782 LKEKLA----GQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:cd05929   431 LAEELIaflrDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
898-1054 5.46e-06

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 52.65  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  898 HDALRMIFEKTPDGYAPRITGTDESELfHLEVMnykgETDPAQAIADKANEIQSSMVLDKGPLMKLGLFQCPDGDH-LLI 976
Cdd:cd19538    52 HESLRTVFPEEDGVPYQLILEEDEATP-KLEIK----EVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHvLLL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  977 AIHHLLIDGVSWRILLEDFASGYEQAERRQTI---QLPQKTDSFPFWADQL--SKYAAETDMEEEIAYWTE-LSSIKPQ- 1049
Cdd:cd19538   127 LLHHIAADGWSLAPLTRDLSKAYRARCKGEAPelaPLPVQYADYALWQQELlgDESDPDSLIARQLAYWKKqLAGLPDEi 206

                  ....*
gi 166797876 1050 PLPKD 1054
Cdd:cd19538   207 ELPTD 211
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
2111-2256 6.31e-06

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 52.46  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2111 GEIYISGAGVARGYLNrpeltaekfvDDPFEPGaKMYKTGDLAkWLADGNIEYAGRIDEQVKIRGYRIELGEIEAALLQE 2190
Cdd:PRK05851  373 GEIEIRGASMMSGYLG----------QAPIDPD-DWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQV 440
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876 2191 EVIKE-AVVTAREDVHGFKQ---LCAYYVSGGQTTAarlRKQLSQTLASY--MVPA--YFIELDEMPLTSNGKI 2256
Cdd:PRK05851  441 RGVREgAVVAVGTGEGSARPglvIAAEFRGPDEAGA---RSEVVQRVASEcgVVPSdvVFVAPGSLPRTSSGKL 511
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
746-835 6.45e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 47.24  E-value: 6.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    746 LKALPAADentraeneyiaPRNTIEELLASIWQEVLGAERIGILD---NFFDFGGDSIKSIQVSSRLYQA-GYKVDMKHL 821
Cdd:smart00823    1 LAALPPAE-----------RRRLLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAAtGLRLPATLV 69
                            90
                    ....*....|....
gi 166797876    822 FKHPSIAELSQFVA 835
Cdd:smart00823   70 FDHPTPAALAEHLA 83
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
3426-3708 6.58e-06

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 52.51  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3426 AYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRqVYSAYDAELNIAMLAPYYFDASVQQMYASLLSG-HTLF----IVPKE 3500
Cdd:PRK06334  186 AVILFTSGTEKLPKGVPLTHANLLANQRACLK-FFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGvPVVFaynpLYPKK 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3501 IVsdgaalcRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHL---LIGGEALSKTTVNKLKQLFgehgaaPGIT--NV 3575
Cdd:PRK06334  265 IV-------EMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLrfvVIGGDAFKDSLYQEALKTF------PHIQlrQG 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3576 YGPTEtCVDASLFNIECSSdawarsQNYVPIGKPL-GRNRMYILDSKKRLQPKGVQGELYIAGDGVGRGYLNlpeltdek 3654
Cdd:PRK06334  332 YGTTE-CSPVITINTVNSP------KHESCVGMPIrGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLG-------- 396
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 3655 fvADP---FVP--EDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVML 3708
Cdd:PRK06334  397 --EDFgqgFVElgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILM 453
PRK09192 PRK09192
fatty acyl-AMP ligase;
4358-4734 9.91e-06

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 51.93  E-value: 9.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4358 LTYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAG--AAFLPIdPELPEKRRAF------MLKDSG 4429
Cdd:PRK09192   50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPL-PMGFGGRESYiaqlrgMLASAQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4430 ADVLLTcaghaiPPLFEGevlLLDD-----PLLYQGRTDNLNL---------SCSENDLMYVIYTSGTTGQPKGVQLEHK 4495
Cdd:PRK09192  129 PAAIIT------PDELLP---WVNEathgnPLLHVLSHAWFKAlpeadvalpRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4496 T-MTNLLAYEQDHTQLRF-DRvlqfaAMSFDVCYQEMfsALSsGGILFIIGNEAKRDIRQLNDFVRThgiqtaflPTAFL 4573
Cdd:PRK09192  200 AlMANLRAISHDGLKVRPgDR-----CVSWLPFYHDM--GLV-GFLLTPVATQLSVDYLPTRDFARR--------PLQWL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4574 KLLASEK---HYFEPFaecvdhiiaaGEQLIATRM------------LR------DMLaRHQVtLHNH------------ 4620
Cdd:PRK09192  264 DLISRNRgtiSYSPPF----------GYELCARRVnskdlaeldlscWRvagigaDMI-RPDV-LHQFaeafapagfddk 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4621 -----YGPSE-THVVTMY---------TVDPDTdQELQPI-----------------GKPISNTEIFILNEAGTLQPVGI 4668
Cdd:PRK09192  332 afmpsYGLAEaTLAVSFSplgsgivveEVDRDR-LEYQGKavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERV 410
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166797876 4669 VGELCISGVSLARGYHNREsltlETfvphpydsnQRMYK------TGDLArYLPEGNIEYAGRRDHQVKIRG 4734
Cdd:PRK09192  411 VGHICVRGPSLMSGYFRDE----ES---------QDVLAadgwldTGDLG-YLLDGYLYITGRAKDLIIING 468
PLN02654 PLN02654
acetate-CoA ligase
286-744 9.98e-06

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 52.21  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  286 NDHLTYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLLHDADADVLL 365
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  366 VQHHLK----------------NSLAFDGPVIDL-----NDEA---------------------SYHADCSLlSPVAGHS 403
Cdd:PLN02654  198 TCNAVKrgpktinlkdivdaalDESAKNGVSVGIcltyeNQLAmkredtkwqegrdvwwqdvvpNYPTKCEV-EWVDAED 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  404 HLaYVIYTSGTTGKPKGVMVEHGG-IVNSLQWKKAFFKHSPADRV--------LVLYPYVfdafilnFFGPLISGATLHL 474
Cdd:PLN02654  277 PL-FLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYwctadcgwITGHSYV-------TYGPMLNGATVLV 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  475 LPNEEN-KETFAIQNAIKQERITHFSTSPRLLKTMIEQmnredfihvqhvvvGGEQLETDTVEKLHSL----QPrirIN- 548
Cdd:PLN02654  349 FEGAPNyPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRD--------------GDEYVTRHSRKSLRVLgsvgEP---INp 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  549 -------NEYGPTENSVVSTFHPVQSADEQITigsPVAnhqayilGAHHQ-----------IQPIgIPGELYVGGAGVAR 610
Cdd:PLN02654  412 sawrwffNVVGDSRCPISDTWWQTETGGFMIT---PLP-------GAWPQkpgsatfpffgVQPV-IVDEKGKEIEGECS 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  611 GYL----NRPELTEEKFVEH------LHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVKIRGYRIEIGEVEAAMFNLEN 680
Cdd:PLN02654  481 GYLcvkkSWPGAFRTLYGDHeryettYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876  681 VREAAVVAREDADGAKQLYAYYV---GEPsltaaqFREELSREL--------PNYMIPSRFIPLERIPLTSNGKI 744
Cdd:PLN02654  561 CAEAAVVGIEHEVKGQGIYAFVTlveGVP------YSEELRKSLiltvrnqiGAFAAPDKIHWAPGLPKTRSGKI 629
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2370-2621 1.05e-05

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 52.35  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2370 WFFEQTTTDQHYYN--QAVMLHAPegFQETQLRQTLQKLAEHHDALRMTFRTTENGCEAQNEeiAQSGLYRLEVMNLKED 2447
Cdd:PRK10252   18 WMAEKLSPLPSAWSvaHYVELTGE--LDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVD--PALTFPLPEIIDLRTQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2448 PDPGRTIEA--KADEIQSSMHLSDGPLMKAGLFQCADGDHLL-IAIHHLIIDGISWRILLEDIVSGYKQAENGRviqlPQ 2524
Cdd:PRK10252   94 PDPHAAAQAlmQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWyQRYHHLLVDGFSFPAITRRIAAIYCAWLRGE----PT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2525 KTDSFQLWAKRLSEYA---QSETIKQEQEYWTkiEQTEVKPLPKDFHETHTTAKDSETAAVEWTKE-ETELLLKQANRAY 2600
Cdd:PRK10252  170 PASPFTPFADVVEEYQryrASEAWQRDAAFWA--EQRRQLPPPASLSPAPLPGRSASADILRLKLEfTDGAFRQLAAQAS 247
                         250       260
                  ....*....|....*....|.
gi 166797876 2601 HTEINDLLLTSLGLSISHWSG 2621
Cdd:PRK10252  248 GVQRPDLALALVALWLGRLCG 268
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
3292-3715 1.15e-05

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 51.79  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3292 QAHRTPDNTAVVFEG------KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPI-- 3363
Cdd:cd05966    62 HLKERGDKVAIIWEGdepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfa 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3364 --DPDSPSERIryilNDSSISVLLYC------GKLQD---------DIGFS----------GTCIDLME--EHFYHE--- 3411
Cdd:cd05966   142 gfSAESLADRI----NDAQCKLVITAdggyrgGKVIPlkeivdealEKCPSvekvlvvkrtGGEVPMTEgrDLWWHDlma 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3412 --KDSSLALSYQSSQLAYAIYTSGTTGKPKGtlIEHRQVIHLieglsrqVYSAYDAElniamlapYYFDASVQQMYASL- 3488
Cdd:cd05966   218 kqSPECEPEWMDSEDPLFILYTSGSTGKPKG--VVHTTGGYL-------LYAATTFK--------YVFDYHPDDIYWCTa 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3489 ----LSGHTlFIV--P-----KEIVSDGAAL----CRYYR---QHSIDITDGTPAHLKLLIAAGD--LQGVTLQHL-LIG 3547
Cdd:cd05966   281 digwITGHS-YIVygPlangaTTVMFEGTPTypdpGRYWDiveKHKVTIFYTAPTAIRALMKFGDewVKKHDLSSLrVLG 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3548 --GEALSKTTVNKLKQLFGEhGAAPgITNVYGPTET-----------------CVDASLFNIEcssdawarsqnyvPIgk 3608
Cdd:cd05966   360 svGEPINPEAWMWYYEVIGK-ERCP-IVDTWWQTETggimitplpgatplkpgSATRPFFGIE-------------PA-- 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3609 plgrnrmyILDSKKRLQPKGVQGELYIAGD--GVGRGYLNlpelTDEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGR 3686
Cdd:cd05966   423 --------ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYG----DHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGR 490
                         490       500
                  ....*....|....*....|....*....
gi 166797876 3687 IDHQVKIQGFRIELGEIESVMLNVPDIQE 3715
Cdd:cd05966   491 VDDVINVSGHRLGTAEVESALVAHPAVAE 519
PRK03584 PRK03584
acetoacetate--CoA ligase;
1771-1936 1.20e-05

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 51.72  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1771 FPQTpvhQL-FEEQ--SQRTPDQAAVI----DKDRQ-LTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESVVGIL 1842
Cdd:PRK03584   81 FPGA---RLnYAENllRHRRDDRPAIIfrgeDGPRReLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAML 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1843 AVLKSGGAYVPIDPEY-PQ---DRI--------------RYmlddsqAGIVLMQRD----VRKQLAYEGVTVLLDdessY 1900
Cdd:PRK03584  158 ATASLGAIWSSCSPDFgVQgvlDRFgqiepkvliavdgyRY------GGKAFDRRAkvaeLRAALPSLEHVVVVP----Y 227
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 1901 HQDGSDLAPISDVSHLA----------------------YVIYTSGSTGRPK-------GVLIEH 1936
Cdd:PRK03584  228 LGPAAAAAALPGALLWEdflapaeaaelefepvpfdhplWILYSSGTTGLPKcivhghgGILLEH 292
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2-171 1.21e-05

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 51.33  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876    2 SVFKTQETYWENLFDEEDGLSAFPyfkaADKASLVRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLY 81
Cdd:cd19546   189 SLIGDQIAYWRDALAGAPDELELP----TDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLT 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   82 KYTDRTSLILGipTVSKQKAGQSAVNNIV-------LLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQ 154
Cdd:cd19546   265 RLGAGTDVTVG--TVLPRDDEEGDLEGMVgpfarplALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALP 342
                         170
                  ....*....|....*..
gi 166797876  155 YNDEHMPLIHTVVSLNE 171
Cdd:cd19546   343 PSADRHPVFQVALDVRD 359
PRK07868 PRK07868
acyl-CoA synthetase; Validated
3288-3366 1.34e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 52.03  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3288 LFEEQAHRTPDNTAVVFEGKQFTYEELNRRANQLARTLQAKGVQADQLVGIM--TERSLEMVVGILGVLKAGGAYLPIDP 3365
Cdd:PRK07868  452 IIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLmeTRPSALVAIAALSRLGAVAVLMPPDT 531

                  .
gi 166797876 3366 D 3366
Cdd:PRK07868  532 D 532
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
283-675 1.35e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 51.66  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  283 KFKNDHL------TYRELNEKASRLARTLRNCGVQPDTLVAILADRSLEMIVSIIAVWKAGGAYVPLDPEYPKERLQYLL 356
Cdd:PLN02387   95 KFEKLHLgeyewiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSL 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  357 HDADADVLL-----------VQHHL---KNSLAFD--GPVIDLNDEASYHADCSLLS---------PVAGH----SHLAY 407
Cdd:PLN02387  175 NETEVTTVIcdskqlkklidISSQLetvKRVIYMDdeGVDSDSSLSGSSNWTVSSFSeveklgkenPVDPDlpspNDIAV 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  408 VIYTSGTTGKPKGVMVEHGGIVNSLQW-KKAFFKHSPADRVLVLYPYvfdAFILNFFGPLI---SGATL-----HLLPNE 478
Cdd:PLN02387  255 IMYTSGSTGLPKGVMMTHGNIVATVAGvMTVVPKLGKNDVYLAYLPL---AHILELAAESVmaaVGAAIgygspLTLTDT 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  479 ENKETFAIQNAIKQERITHFSTSPRLLKTMIEQMNRE--------------------------------------DFI-- 518
Cdd:PLN02387  332 SNKIKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKvdakgglakklfdiaykrrlaaiegswfgawglekllwDALvf 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  519 ---------HVQHVVVGGEQLETDTvEKLHSLQPRIRINNEYGPTENSVVSTFhpvqSADEQITIG---SPVANhqAYIL 586
Cdd:PLN02387  412 kkiravlggRIRFMLSGGAPLSGDT-QRFINICLGAPIGQGYGLTETCAGATF----SEWDDTSVGrvgPPLPC--CYVK 484
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  587 -----GAHHQIQPIGIP-GELYVGGAGVARGYLNRPELTEEkfVEHLHVPGQKMYKTGDLARWLPDGRIEYLGRIDHQVK 660
Cdd:PLN02387  485 lvsweEGGYLISDKPMPrGEIVIGGPSVTLGYFKNQEKTDE--VYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVK 562
                         490
                  ....*....|....*.
gi 166797876  661 IR-GYRIEIGEVEAAM 675
Cdd:PLN02387  563 LQhGEYVSLGKVEAAL 578
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
4475-4815 1.62e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 51.28  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4475 MYVIYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQFAAMSFD-VCYQEMFSALSSGGILFIIGNEA-KRDIR 4552
Cdd:PTZ00237  257 LYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGwVSFHGFLYGSLSLGNTFVMFEGGiIKNKH 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4553 QLNDFVRT---HGIQTAF-LPTAFLKLLASEkhyfePFAECVD---------HIIAAGEqLIATRMLRDMLARHQVTLHN 4619
Cdd:PTZ00237  337 IEDDLWNTiekHKVTHTLtLPKTIRYLIKTD-----PEATIIRskydlsnlkEIWCGGE-VIEESIPEYIENKLKIKSSR 410
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4620 HYGPSETHVVTMYTVDPDTDQeLQPIGKPISNTEIFILNEAGTLQPVGIVGELCIS---GVSLARGYHNRESLTLETFVP 4696
Cdd:PTZ00237  411 GYGQTEIGITYLYCYGHINIP-YNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSK 489
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4697 HP-YdsnqrmYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKH--VQEAVVLAKENTDGQSDLYAYFTA 4773
Cdd:PTZ00237  490 FPgY------YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHplVLECCSIGIYDPDCYNVPIGLLVL 563
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 166797876 4774 EQSLSISQLK-EKLAGQI--------PGYMIPSYFIQLEKLPLTGNGKVNR 4815
Cdd:PTZ00237  564 KQDQSNQSIDlNKLKNEInniitqdiESLAVLRKIIIVNQLPKTKTGKIPR 614
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
3431-3687 1.89e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 51.15  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3431 TSGTTGKPKGTLIEHRQVIHLIEGLSrqVYSAYDAELNI-----------AMLA----PYYFDASVqqmyasllsghtLF 3495
Cdd:PRK07768  160 TSGSTGSPKAVQITHGNLYANAEAMF--VAAEFDVETDVmvswlplfhdmGMVGfltvPMYFGAEL------------VK 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3496 IVPKEIVSDG---AALCRYYRQhsiDITDGtPAHLKLLIA--------AGDLQGVTLQHLLIGGEALSKTTVNKLKQLFG 3564
Cdd:PRK07768  226 VTPMDFLRDPllwAELISKYRG---TMTAA-PNFAYALLArrlrrqakPGAFDLSSLRFALNGAEPIDPADVEDLLDAGA 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3565 EHGAAPG-ITNVYGPTETC----------------VDASLFNIEC----SSDAWARSqnYVPIGKPLGRNRMYILD-SKK 3622
Cdd:PRK07768  302 RFGLRPEaILPAYGMAEATlavsfspcgaglvvdeVDADLLAALRravpATKGNTRR--LATLGPPLPGLEVRVVDeDGQ 379
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166797876 3623 RLQPKGVqGELYIAGDGVGRGYlnlpeLTDEKFVadPFVPEDRMYRTGDLARLLPDGNIEYIGRI 3687
Cdd:PRK07768  380 VLPPRGV-GVIELRGESVTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRV 436
PRK05857 PRK05857
fatty acid--CoA ligase;
3271-3715 1.89e-05

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 51.16  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3271 RFQSNDmHYPreKTIHELFEEQAHRTPDNTAVV-FEG-KQFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVV 3348
Cdd:PRK05857    5 KFQAMP-QLP--STVLDRVFEQARQQPEAIALRrCDGtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3349 GILGVLKAGGAYLPIDPDSPS---ERIRYILNDSSISVLLYCG---KLQDDIGFSGTCIDLMEEHFYHEKDSSLALSYQS 3422
Cdd:PRK05857   82 SVLACAKLGAIAVMADGNLPIaaiERFCQITDPAAALVAPGSKmasSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3423 SQLAYA-------IYTSGTTGKPKGTLIEHRQV-----IHLIEGLSRQVYsaYDAELNIAMLAPYYFdASVQQMYASLLS 3490
Cdd:PRK05857  162 GNADQGsedplamIFTSGTTGEPKAVLLANRTFfavpdILQKEGLNWVTW--VVGETTYSPLPATHI-GGLWWILTCLMH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3491 GhTLFIVPKEivsDGAALCRYYRQHSIDITDGTPAHLKLLIAAGDLQGVTLQHLLIGGEALSKTTVNKLKqlFGEhgaAP 3570
Cdd:PRK05857  239 G-GLCVTGGE---NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVR--FIE---AT 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3571 GI--TNVYGPTET-----CV---DASLFNIECSSdawarsqnyvpIGKPLGRNRMYILD------SKKRLQPKGVQGELY 3634
Cdd:PRK05857  310 GVrtAQVYGLSETgctalCLptdDGSIVKIEAGA-----------VGRPYPGVDVYLAAtdgigpTAPGAGPSASFGTLW 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3635 IAGDGVGRGYLNLPELTDEkFVADPFVpedrmyRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIELGEIESVMLNVPDIQ 3714
Cdd:PRK05857  379 IKSPANMLGYWNNPERTAE-VLIDGWV------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVR 451

                  .
gi 166797876 3715 E 3715
Cdd:PRK05857  452 E 452
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
4646-4756 2.12e-05

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 50.38  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4646 GKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGR 4725
Cdd:cd17636   166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGWHHTNDLGRREPDGSLSFVGP 238
                          90       100       110
                  ....*....|....*....|....*....|...
gi 166797876 4726 RDHQVKIRGYRVELGEVEAALLKH--VQEAVVL 4756
Cdd:cd17636   239 KTRMIKSGAENIYPAEVERCLRQHpaVADAAVI 271
PRK09192 PRK09192
fatty acyl-AMP ligase;
1798-2273 2.64e-05

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 50.77  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1798 RQLTYGELNKRANRLARTLRAKGVQTDQPVAIITRNSIESV--------VGILAV-------LKSGGAYVpidpeypqDR 1862
Cdd:PRK09192   48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVeaffacqyAGLVPVplplpmgFGGRESYI--------AQ 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1863 IRYMLDDSQAGIVLMQRD---------VRKQLAYEGVTVLLDDESSyhqDGSDLAPISDvSHLAYVIYTSGSTGRPKGVL 1933
Cdd:PRK09192  120 LRGMLASAQPAAIITPDEllpwvneatHGNPLLHVLSHAWFKALPE---ADVALPRPTP-DDIAYLQYSSGSTRFPRGVI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1934 IEHG-GLTNY----------------IWWakevyvkgekanFPLY--------------SSISFDLTVTSIFT--PLV-- 1978
Cdd:PRK09192  196 ITHRaLMANLraishdglkvrpgdrcVSW------------LPFYhdmglvgflltpvaTQLSVDYLPTRDFArrPLQwl 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1979 ---TGN-AIIVY-------------DGEDKTALLESIVR------DP-RVDIIK-----LTPAHLQ---VLKEMNIADQT 2026
Cdd:PRK09192  264 dliSRNrGTISYsppfgyelcarrvNSKDLAELDLSCWRvagigaDMiRPDVLHqfaeaFAPAGFDdkaFMPSYGLAEAT 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2027 -AVRRMIVGGENLSTRLARSIHEQFEGRIEICNEYGPTETVVGCmiyrydaakdrresvpiGTAAANTSIYVLDENMKPA 2105
Cdd:PRK09192  344 lAVSFSPLGSGIVVEEVDRDRLEYQGKAVAPGAETRRVRTFVNC-----------------GKALPGHEIEIRNEAGMPL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2106 PIGVPGEIYISGAGVARGYLNRPELTAEKFVDDPFEpgakmykTGDLAkWLADGNIEYAGRIDEQVKIRGYRIELGEIEA 2185
Cdd:PRK09192  407 PERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLD-------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEW 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2186 ALLQEEVIKE----AVVTARED-------VHgfkqlCayyvsggQTTAARLRKQLSQTLASY------------MVPAYf 2242
Cdd:PRK09192  479 IAEQEPELRSgdaaAFSIAQENgekivllVQ-----C-------RISDEERRGQLIHALAALvrsefgveaaveLVPPH- 545
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 166797876 2243 ieldEMPLTSNGKIN----KKGLPAPDFELQDRAE 2273
Cdd:PRK09192  546 ----SLPRTSSGKLSrakaKKRYLSGAFASLDVAA 576
PLN02614 PLN02614
long-chain acyl-CoA synthetase
4472-4732 2.98e-05

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 50.79  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4472 NDLMYVIYTSGTTGQPKGVQLEHKTMTNLLA------YEQDHTQLRFDRVLQFAAMS--FDVCYQEMFsaLSSGGILFII 4543
Cdd:PLN02614  223 SDICTIMYTSGTTGDPKGVMISNESIVTLIAgvirllKSANAALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGFW 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4544 GNEAKRDIRQLNDFVRT-------------HGIQTAFLPTAFLKLLASEKHYFEPFAEcvdhiIAAGEQLIATRMLRDML 4610
Cdd:PLN02614  301 RGDVKLLIEDLGELKPTifcavprvldrvySGLQKKLSDGGFLKKFVFDSAFSYKFGN-----MKKGQSHVEASPLCDKL 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4611 ARHQVT----------------LHNH----------------YGPSETHVVTMYTVdPDTDQELQPIGKPISNTEIFILN 4658
Cdd:PLN02614  376 VFNKVKqglggnvriilsgaapLASHvesflrvvacchvlqgYGLTESCAGTFVSL-PDELDMLGTVGPPVPNVDIRLES 454
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 4659 ----EAGTLQPVGiVGELCISGVSLARGYHNRESLTLETFVphpydsnQRMYKTGDLARYLPEGNIEYAGRRDHQVKI 4732
Cdd:PLN02614  455 vpemEYDALASTP-RGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
48-167 3.13e-05

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 49.95  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   48 SLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDRTSLILGIPTVSKqkaGQSAVN-------NIVLLKNTLSNES 120
Cdd:cd20483   229 TLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDR---PHPDFDdlvgffvNMLPIRCRMDCDM 305
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 166797876  121 TFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMPLIHTVV 167
Cdd:cd20483   306 SFDDLLESTKTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAV 352
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
2365-2787 3.59e-05

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 49.99  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2365 TPIQHWFFEQTTTDQHYYNQAVMLHAPEGFQETQLRQTLQKLAEHHDALRMTF--RTTENGCEAQneeIAQSGLYRLEVM 2442
Cdd:cd19545     5 TPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvqSDSGGLLQVV---VKESPISWTEST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2443 NLKEdpdpgrtieAKADEIQSSMHLsDGPLMKAGLFQ-CADGDHLLIAIHHLIIDGISWRILLEDIVSGYKQAENGRviq 2521
Cdd:cd19545    82 SLDE---------YLEEDRAAPMGL-GGPLVRLALVEdPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ--- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2522 lpqktdsfQLWAKRLSEYAQSETIKQEQEYWtkieQTEVKPL-PKDFhethTTAKDSETAAVEWTKEETELLLKQANRAY 2600
Cdd:cd19545   149 --------PPPFSRFVKYLRQLDDEAAAEFW----RSYLAGLdPAVF----PPLPSSRYQPRPDATLEHSISLPSSASSG 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2601 HTeINDLLLTSLGLSISHWSGLEQIPIHLEGHGREQIIQDIDisRTVG-WFTSLyPVVLHAQPGKEISDYIKTT-KEGLR 2678
Cdd:cd19545   213 VT-LATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIE--QIVGpTIATV-PLRVRIDPEQSVEDFLQTVqKDLLD 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2679 QIPHKGIGYGIARYLSGGMPSKLNPEISFNYLGQFDQDLQRHGVQLSSYSCGSDSSGHqerPYVLNINGMITDGRLKLTI 2758
Cdd:cd19545   289 MIPFEHTGLQNIRRLGPDARAACNFQTLLVVQPALPSSTSESLELGIEEESEDLEDFS---SYGLTLECQLSGSGLRVRA 365
                         410       420
                  ....*....|....*....|....*....
gi 166797876 2759 SYSSKQYAKETIMRLSETIQSRLRTIITH 2787
Cdd:cd19545   366 RYDSSVISEEQVERLLDQFEHVLQQLASA 394
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
4470-4842 4.94e-05

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 49.96  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4470 SENDLMYVIYTSGTTGQPKGVQLEHKtmtNLLA-YEQDHTQLRF---DRVlqFAAM----SFdvcyqemfsALSSGGILF 4541
Cdd:PRK06814  791 DPDDPAVILFTSGSEGTPKGVVLSHR---NLLAnRAQVAARIDFspeDKV--FNALpvfhSF---------GLTGGLVLP 856
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4542 IIgneakrdirqlndfvrtHGIQTAFLPTA-----------------------FLKLLASEKHYFEPFAecVDHIIAAGE 4598
Cdd:PRK06814  857 LL-----------------SGVKVFLYPSPlhyriipeliydtnatilfgtdtFLNGYARYAHPYDFRS--LRYVFAGAE 917
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4599 QLIA-TRMLrdMLARHQVTLHNHYGPSEThvvtmytvdpdtdqelQPIgkpIS-NTEIFilNEAGT-----------LQP 4665
Cdd:PRK06814  918 KVKEeTRQT--WMEKFGIRILEGYGVTET----------------APV---IAlNTPMH--NKAGTvgrllpgieyrLEP 974
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4666 V-GIV--GELCISGVSLARGYhnresLTLE---TFVPHPYDsnqrMYKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVEL 4739
Cdd:PRK06814  975 VpGIDegGRLFVRGPNVMLGY-----LRAEnpgVLEPPADG----WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISL 1045
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4740 GEVE---AALLKHVQEAVVLAKENTDGQSdlYAYFTAEQSLSISQ-LKEKLAGQIPGYMIPSYFIQLEKLPLTGNGKvnr 4815
Cdd:PRK06814 1046 AAVEelaAELWPDALHAAVSIPDARKGER--IILLTTASDATRAAfLAHAKAAGASELMVPAEIITIDEIPLLGTGK--- 1120
                         410       420
                  ....*....|....*....|....*..
gi 166797876 4816 ralpmpeaglqtgTDYVAPRTNMEEQL 4842
Cdd:PRK06814 1121 -------------IDYVAVTKLAEEAA 1134
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
3293-3713 5.99e-05

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 49.65  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVvfEGKQFTYEELNRRANQLARTLQAK-GVQADQLVGIMTERSLEMVVGILGVLKAGGAYLPIDPDSPSER 3371
Cdd:cd05905     1 AYTLLDSKGK--EATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3372 IRYILNDSSI-----SVLLYCG--KLQDDIGFSGTCIDLM---------EEHFY---HEKDSSLALSYQSSQLAYAIYTS 3432
Cdd:cd05905    79 LGFLLGTCKVrvaltVEACLKGlpKKLLKSKTAAEIAKKKgwpkildfvKIPKSkrsKLKKWGPHPPTRDGDTAYIEYSF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3433 GTTGKPKGTLIEHRQVIHLIEGLSRQVysAYDAELNIAMLAPYYFDAS-VQQMYASLLSG-HTLFIVPKEIVSDGAALCR 3510
Cdd:cd05905   159 SSDGSLSGVAVSHSSLLAHCRALKEAC--ELYESRPLVTVLDFKSGLGlWHGCLLSVYSGhHTILIPPELMKTNPLLWLQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3511 YYRQHSIDITDGTPA-------HLKLLIAAGDLQGVTLQHL----LIGGEALSKTTVNKLKQLFGEHGAAP-GITNVYG- 3577
Cdd:cd05905   237 TLSQYKVRDAYVKLRtlhwclkDLSSTLASLKNRDVNLSSLrmcmVPCENRPRISSCDSFLKLFQTLGLSPrAVSTEFGt 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3578 ---------------PTETCVDA-SLFN--IECSSDAWARSQNYVPIGKPLGRNRMYILDSKKRLQPK-GVQGELYIAGD 3638
Cdd:cd05905   317 rvnpficwqgtsgpePSRVYLDMrALRHgvVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKdGEIGEIWVNSP 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3639 GVGRGYLNLPELTDEKFVADP------FVPEDRMYRTGDLARLLP----DGNIEY------IGRIDHQVKIQGFRIELGE 3702
Cdd:cd05905   397 ANASGYFLLDGETNDTFKVFPstrlstGITNNSYARTGLLGFLRPtkctDLNVEEhdllfvVGSIDETLEVRGLRHHPSD 476
                         490
                  ....*....|..
gi 166797876 3703 IE-SVMLNVPDI 3713
Cdd:cd05905   477 IEaTVMRVHPYR 488
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
4359-4726 7.58e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 49.22  E-value: 7.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4359 TYRQLNERSNQLARVLQDKGACTDQVVAVLTDRSAHMIIGILAILKAGAAF-----------LPIDPElpEKRRAFMLKD 4427
Cdd:PRK07768   31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLtmlhqptprtdLAVWAE--DTLRVIGMIG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4428 SGAdVLLTCAGHAIPPLFEGE---VLLLDDpLLYQGRTDNLNLScsENDLMYVIYTSGTTGQPKGVQLEHKTM-TNLLAy 4503
Cdd:PRK07768  109 AKA-VVVGEPFLAAAPVLEEKgirVLTVAD-LLAADPIDPVETG--EDDLALMQLTSGSTGSPKAVQITHGNLyANAEA- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4504 eqdhtqlrfdrvlQFAAMSFDVCYQEMFSAL----SSGGILFII-----GNEAKRdIRQLnDFVRT-----------HGI 4563
Cdd:PRK07768  184 -------------MFVAAEFDVETDVMVSWLplfhDMGMVGFLTvpmyfGAELVK-VTPM-DFLRDpllwaeliskyRGT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4564 QTA---FLPTAFLKLLA----------SEKHYFEPFAECVDHiiAAGEQLIatrmlrDMLARHQV---TLHNHYGPSETH 4627
Cdd:PRK07768  249 MTAapnFAYALLARRLRrqakpgafdlSSLRFALNGAEPIDP--ADVEDLL------DAGARFGLrpeAILPAYGMAEAT 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4628 V-VTMY---------TVDPD--------------TDQELQPIGKPISNTEIFILNEAGTLQPVGIVGELCISGVSLARGY 4683
Cdd:PRK07768  321 LaVSFSpcgaglvvdEVDADllaalrravpatkgNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 166797876 4684 hnresLTLETFVPHPYDSNqrMYKTGDLArYLPE-GNIEYAGRR 4726
Cdd:PRK07768  401 -----LTMDGFIPAQDADG--WLDTGDLG-YLTEeGEVVVCGRV 436
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
3293-3790 8.19e-05

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 49.19  E-value: 8.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3293 AHRTPDNTAVVFEGK-----QFTYEELNRRANQLARTLQAKGVQA-DQLVGIMTErSLEMVVGILGVLKAGGAYLPIDPD 3366
Cdd:cd05943    78 RHADADDPAAIYAAEdgertEVTWAELRRRVARLAAALRALGVKPgDRVAGYLPN-IPEAVVAMLATASIGAIWSSCSPD 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3367 ----SPSERIRYILNDSSISVL--LYCGKLQD------------------------------DIGFSGTCIDLmEEHFYH 3410
Cdd:cd05943   157 fgvpGVLDRFGQIEPKVLFAVDayTYNGKRHDvrekvaelvkglpsllavvvvpytvaagqpDLSKIAKALTL-EDFLAT 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3411 EKDSSLALSYQS-SQLAYAIYTSGTTGKPK-------GTLIEHRQViHLIEGLSR--QVYsaydaelniamlapYYFDAS 3480
Cdd:cd05943   236 GAAGELEFEPLPfDHPLYILYSSGTTGLPKcivhgagGTLLQHLKE-HILHCDLRpgDRL--------------FYYTTC 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3481 VQQMY----ASLLSGHTLFIV---PkeIVSDGAALCRYYRQHSIDITDGTPAHLKLLIAAG-------DLQgvTLQHLLI 3546
Cdd:cd05943   301 GWMMWnwlvSGLAVGATIVLYdgsP--FYPDTNALWDLADEEGITVFGTSAKYLDALEKAGlkpaethDLS--SLRTILS 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3547 GGEALSKTT---VNKlkqlfgehGAAPGI--TNVYGPTETCvdaSLFNIECSSDAwarsqnyVPIGKPLGRN---RMYIL 3618
Cdd:cd05943   377 TGSPLKPESfdyVYD--------HIKPDVllASISGGTDII---SCFVGGNPLLP-------VYRGEIQCRGlgmAVEAF 438
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3619 DSKKRLQPkGVQGELYIA-----------GDGVGrgylnlpeltdEKFVADPFVPEDRMYRTGDLARLLPDGNIEYIGRI 3687
Cdd:cd05943   439 DEEGKPVW-GEKGELVCTkpfpsmpvgfwNDPDG-----------SRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRS 506
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3688 DHQVKIQGFRIELGEIESVMLNVPDIQEAAAAALKDADDEYY------LCGYFAAD----KTIQiSELRKRM-ARHlpgy 3756
Cdd:cd05943   507 DGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERvilfvkLREGVELDdelrKRIR-STIRSALsPRH---- 581
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 166797876 3757 mIPAHFVQLDKMPLTPNGK----LNRQLLP-APVKKRDS 3790
Cdd:cd05943   582 -VPAKIIAVPDIPRTLSGKkvevAVKKIIAgRPVKNAGA 619
PRK07868 PRK07868
acyl-CoA synthetase; Validated
4336-4435 9.52e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 48.95  E-value: 9.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4336 QLFEQQAERNPDHEAVMFGNQTLTYRQLNERSNQLARVLQDKGACTDQVVAVL--TDRSAHMIIGILAILKAGAAFLPID 4413
Cdd:PRK07868  451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLmeTRPSALVAIAALSRLGAVAVLMPPD 530
                          90       100
                  ....*....|....*....|..
gi 166797876 4414 PELPEkrrafMLKDSGADVLLT 4435
Cdd:PRK07868  531 TDLAA-----AVRLGGVTEIIT 547
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
3522-3713 9.65e-05

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 48.61  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3522 GTPAHLKLLIAAGDLQGV-----TLQHLLIGGEALSKTTVNKLKQLFGehgaapgIT--NVYGPTETCVDASlfnIECSS 3594
Cdd:COG1541   181 GTPSYLLYLAEVAEEEGIdprdlSLKKGIFGGEPWSEEMRKEIEERWG-------IKayDIYGLTEVGPGVA---YECEA 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3595 DA----WARSQnYVPI-----GKPLgrnrmyildskkrlqPKGVQGELYIAGdgvgrgylnlpeLTDEKFvadPFVpedR 3665
Cdd:COG1541   251 QDglhiWEDHF-LVEIidpetGEPV---------------PEGEEGELVVTT------------LTKEAM---PLI---R 296
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 166797876 3666 mYRTGDLARLLPDGN--------IEYI-GRIDHQVKIQGFRIELGEIESVMLNVPDI 3713
Cdd:COG1541   297 -YRTGDLTRLLPEPCpcgrthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
4357-4500 1.14e-04

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 48.50  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4357 TLTYRQLNERSNQLARVLQDKGACT--DQVVAVLTDrSAHMIIGILAILKAGAAFLPIDPELPEKRRAFMLKDSGADVLL 4434
Cdd:cd05905    14 TLTWGKLLSRAEKIAAVLQKKVGLKpgDRVALMYPD-PLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4435 T---CA-GH-----------------AIPPLFEgevllLDDPLLYQGRTDNLNLS---CSENDLMYVIYTSGTTGQPKGV 4490
Cdd:cd05905    93 TveaCLkGLpkkllksktaaeiakkkGWPKILD-----FVKIPKSKRSKLKKWGPhppTRDGDTAYIEYSFSSDGSLSGV 167
                         170
                  ....*....|
gi 166797876 4491 QLEHKTMTNL 4500
Cdd:cd05905   168 AVSHSSLLAH 177
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
3805-3865 1.17e-04

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.78  E-value: 1.17e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876   3805 LTAIWEDVLGL---EQVGIRDHFFEIGGHSLRATALIAKIQKQMHVQIPLRDVFRFPTIEQLAR 3865
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
33-230 1.19e-04

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 48.13  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   33 ASLVRTGYqekcicrsLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDRTSLILGIPTV------SKQKAGQsaV 106
Cdd:cd19533   215 AFLRRTAE--------LPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMgrlgaaARQTPGM--V 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  107 NNIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEH--------MPL-----IHTVVSLNEIH 173
Cdd:cd19533   285 ANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELHPlfgptvnyMPFdygldFGGVVGLTHNL 364
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  174 --------SLQCKEDTATDTL-FHFDlenngihlklfYNGNLYDERYINQIVSHLDQLLSVILFQP 230
Cdd:cd19533   365 ssgptndlSIFVYDRDDESGLrIDFD-----------ANPALYSGEDLARHQERLLRLLEEAAADP 419
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
4670-4746 1.26e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 48.57  E-value: 1.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166797876 4670 GELCISGVSLARGYHNRESLTLETFvphPYDSN-QRMYKTGDLARYLPEGNIEYAGRRDHQVKIR-GYRVELGEVEAAL 4746
Cdd:PLN02387  503 GEIVIGGPSVTLGYFKNQEKTDEVY---KVDERgMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
4647-4818 1.47e-04

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 48.21  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4647 KPISNTEIF------ILNEAGTLQPVGIVGELCI--SGVSLAR---GYHNReslTLETFVPHPYDsnqrMYKTGDLARYL 4715
Cdd:PRK00174  422 KPGSATRPLpgiqpaVVDEEGNPLEGGEGGNLVIkdPWPGMMRtiyGDHER---FVKTYFSTFKG----MYFTGDGARRD 494
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4716 PEGNIEYAGRRDHQVKIRGYRveLG--EVEAALLKH--VQE-AVVLAKENTDGQSdLYAYFTAEQSLSIS-----QLKEK 4785
Cdd:PRK00174  495 EDGYYWITGRVDDVLNVSGHR--LGtaEIESALVAHpkVAEaAVVGRPDDIKGQG-IYAFVTLKGGEEPSdelrkELRNW 571
                         170       180       190
                  ....*....|....*....|....*....|....
gi 166797876 4786 LAGQIPGYMIPSyFIQL-EKLPLTGNGKVNRRAL 4818
Cdd:PRK00174  572 VRKEIGPIAKPD-VIQFaPGLPKTRSGKIMRRIL 604
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
3260-3687 1.58e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 48.43  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3260 LTQQEKEYLLSRFQSNDMHY-PREKTIHELFEEQAHRTPDNTAVVFEGKQF-TYEELNRRANQLARTLQAKGVQADQLVG 3337
Cdd:PTZ00216   71 FLQRLERICKERGDRRALAYrPVERVEKEVVKDADGKERTMEVTHFNETRYiTYAELWERIVNFGRGLAELGLTKGSNVA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3338 IMTERSLEMVVGILGV----LKAGGAYLPIDPDSPSERIR------YILNDSSISVLLycgKLQDDIGFSGTCI------ 3401
Cdd:PTZ00216  151 IYEETRWEWLASIYGIwsqsMVAATVYANLGEDALAYALReteckaIVCNGKNVPNLL---RLMKSGGMPNTTIiyldsl 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3402 ----DLMEEHFY---------HEKDSSLALSYQSS--QLAYAIYTSGTTGKPKGTLIEHRQVIHLIEGLSRQVYSaydae 3466
Cdd:PTZ00216  228 pasvDTEGCRLVawtdvvakgHSAGSHHPLNIPENndDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLND----- 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3467 lniaMLAPYyfdaSVQQMYASLLS-GHTL-FIVPKEIVSDGAALC---------RYYRQHSiDITD-------GTP---- 3524
Cdd:PTZ00216  303 ----LIGPP----EEDETYCSYLPlAHIMeFGVTNIFLARGALIGfgsprtltdTFARPHG-DLTEfrpvfliGVPrifd 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3525 --------------------------AHLKLLIAAGD--------------LQGVTLQHLLIGGEALSKTTVNKLKQLFG 3564
Cdd:PTZ00216  374 tikkaveaklppvgslkrrvfdhayqSRLRALKEGKDtpywnekvfsapraVLGGRVRAMLSGGGPLSAATQEFVNVVFG 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3565 ehgaapGITNVYGPTETCVDAS---LFNIECSSdawarsqnyvpIGKPLGRNRMYILDS---KKRLQPKGvQGELYIAGD 3638
Cdd:PTZ00216  454 ------MVIQGWGLTETVCCGGiqrTGDLEPNA-----------VGQLLKGVEMKLLDTeeyKHTDTPEP-RGEILLRGP 515
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 166797876 3639 GVGRGYLNLPELTDEkfVADpfvpEDRMYRTGDLARLLPDGNIEYIGRI 3687
Cdd:PTZ00216  516 FLFKGYYKQEELTRE--VLD----EDGWFHTGDVGSIAANGTLRIIGRV 558
PLN02654 PLN02654
acetate-CoA ligase
4706-4818 2.01e-04

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 47.97  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 4706 YKTGDLARYLPEGNIEYAGRRDHQVKIRGYRVELGEVEAALLKHVQ--EAVVLAKENTDGQSDLYAYFTAEQSLSIS-QL 4782
Cdd:PLN02654  515 YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQcaEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeEL 594
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 166797876 4783 KEKLA----GQIPGYMIPSYFIQLEKLPLTGNGKVNRRAL 4818
Cdd:PLN02654  595 RKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
10-230 2.05e-04

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 47.40  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   10 YWENLfdEEDGLSAFPYFKAADKASlvRTGYQEKCICRSLSPEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDRTSL 89
Cdd:cd19066   192 YWTSY--LHGLPPPLPLPKAKRPSQ--VASYEVLTLEFFLRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDV 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   90 ILGIPTVSKQKAGQSAV----NNIVLLKNTLSNESTFKTVFGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMPLI-H 164
Cdd:cd19066   268 VIGLTFLNRPDEAVEDTiglfLNLLPLRIDTSPDATFPELLKRTKEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFeP 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  165 TVVSLNEIHSLQCKEDTATDTLFH-------FDLE-------NNGIHLKLFYNGNLYDERYINQIVSHLDQLLSVILFQP 230
Cdd:cd19066   348 VFTFKNNQQQLGKTGGFIFTTPVYtssegtvFDLDleasedpDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
PRK07867 PRK07867
acyl-CoA synthetase; Validated
3618-3715 2.44e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 47.37  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3618 LDSKKRLQPKGVQGELY-IAGDGVGRGYLNLPELTDEKFVadpfvpeDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGF 3696
Cdd:PRK07867  340 DADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMR-------GGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGE 412
                          90
                  ....*....|....*....
gi 166797876 3697 RIELGEIESVMLNVPDIQE 3715
Cdd:PRK07867  413 NLGTAPIERILLRYPDATE 431
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
3915-4112 2.78e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 47.01  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3915 MTVEGKLDRDKLQQAFRTLILRHESLRTGFKMADGEPVQYVLDHAAfEAEWYQGEEDDAdlyirQFIRPFHLDEPPLLRV 3994
Cdd:PRK09294   28 AHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLL-HPGIVVVDGDAA-----RPLPELQLDQGVSLLA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3995 GLIELQPDRGILMFDMHHIISDGTSMSVLIKEFIRIY-----EGETLPPLRIQYKdyavwQTGEARLQQ--IQKQEAYWL 4067
Cdd:PRK09294  102 LDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYtdvvtTGDPGPIRPQPAP-----QSLEAVLAQrgIRRQALSGA 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 166797876 4068 E-----LYSGDVPvLHLPADYIRPSARDFAGATMHFTLDKQKSDGLKQLA 4112
Cdd:PRK09294  177 ErfmpaMYAYELP-PTPTAAVLAKPGLPQAVPVTRCRLSKAQTSSLAAFG 225
PLN02736 PLN02736
long-chain acyl-CoA synthetase
405-654 3.18e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 47.40  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  405 LAYVIYTSGTTGKPKGVMVEHGGIVNSLQWKKAFFKHSPADRVLVLYP--YVFD---AFILNFFGPLI---SGATLHLL- 475
Cdd:PLN02736  223 VATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPlaHIYErvnQIVMLHYGVAVgfyQGDNLKLMd 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  476 -------------PNEENKETFAIQNAIK-----QERITHF-------------STSPRLLKTMIEQMNREDFIHVQHVV 524
Cdd:PLN02736  303 dlaalrptifcsvPRLYNRIYDGITNAVKesgglKERLFNAaynakkqalengkNPSPMWDRLVFNKIKAKLGGRVRFMS 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  525 VGGEQLETDTVEKLhslqpRI----RINNEYGPTENS-VVSTfhpVQSADEQIT-IGSPVANHQAYI-----LGAHHQIQ 593
Cdd:PLN02736  383 SGASPLSPDVMEFL-----RIcfggRVLEGYGMTETScVISG---MDEGDNLSGhVGSPNPACEVKLvdvpeMNYTSEDQ 454
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166797876  594 PigIP-GELYVGGAGVARGYLNRPELTEEKFVEH--LHvpgqkmykTGDLARWLPDGRIEYLGR 654
Cdd:PLN02736  455 P--YPrGEICVRGPIIFKGYYKDEVQTREVIDEDgwLH--------TGDIGLWLPGGRLKIIDR 508
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
411-692 4.43e-04

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 46.30  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  411 TSGTTGKPKGVMVEHggivNSLQWKKAFFKHS-------PADRVLVLYPYvfdafilnffGPLISGATLHL--------- 474
Cdd:COG1541    91 SSGTTGKPTVVGYTR----KDLDRWAELFARSlraagvrPGDRVQNAFGY----------GLFTGGLGLHYgaerlgatv 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  475 LP----NEEnketFAIQnAIKQERITHFSTSPRLLKTMIEQMNREDF----IHVQHVVVGGE--------QLEtdtvEKL 538
Cdd:COG1541   157 IPagggNTE----RQLR-LMQDFGPTVLVGTPSYLLYLAEVAEEEGIdprdLSLKKGIFGGEpwseemrkEIE----ERW 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  539 HslqprIRINNEYGPTEnsvvstfhpvqsadeqitIGSPVAN----HQAYILGAHHQ----IQPI-------GIPGELYV 603
Cdd:COG1541   228 G-----IKAYDIYGLTE------------------VGPGVAYeceaQDGLHIWEDHFlveiIDPEtgepvpeGEEGELVV 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  604 GGagvargylnrpeLTEEkfvehlhvpGQKM--YKTGDLARWLPDG--------RIEY-LGRIDHQVKIRGYRIEIGEVE 672
Cdd:COG1541   285 TT------------LTKE---------AMPLirYRTGDLTRLLPEPcpcgrthpRIGRiLGRADDMLIIRGVNVFPSQIE 343
                         330       340
                  ....*....|....*....|..
gi 166797876  673 AAMFNLENVREA--AVVAREDA 692
Cdd:COG1541   344 EVLLRIPEVGPEyqIVVDREGG 365
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
51-230 4.44e-04

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 46.49  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876   51 PEVSQRIMTMANHSDMAAYLILLAGIECLLYKYTDRTSLILGIPTVSKQKAGQSA-----VNNIVLLKNTlSNESTFKTV 125
Cdd:cd19538   231 SELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDlvgffVNTLVLRTDT-SGNPSFREL 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  126 FGQLKEAVNDSLKNQNLPFRKMARHLSVQYNDEHMPLIHTVVSLN-------EIHSLQCKEDTATDTLFHFDL------- 191
Cdd:cd19538   310 LERVKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQntpqpslDLPGLEAKLELRTVGSAKFDLtfelreq 389
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 166797876  192 ----ENNGIHLKLFYNGNLYDERYINQIVSHLDQLLSVILFQP 230
Cdd:cd19538   390 yndgTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
3631-3715 5.12e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 46.73  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3631 GELYIAGDGVGRGYLNLPELTDEkfvadpfVPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKI-QGFRIELGEIESVMLN 3709
Cdd:PLN02430  466 GEICVRGKCLFSGYYKNPELTEE-------VMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQ 538

                  ....*.
gi 166797876 3710 VPDIQE 3715
Cdd:PLN02430  539 NPIVED 544
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
3702-3775 7.20e-04

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 41.38  E-value: 7.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166797876  3702 EIESVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQIS--ELRKRMARHLPGYMIPAHFVQLDKMPLTPNGK 3775
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLeeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2399-2554 1.09e-03

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 45.16  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2399 LRQTLQKLAEHHDALRMTFrtTENGCEAQNEEI-AQSGLYRLEVMNLKEDPDPGRTIEAKADEIQSSmhlSDGPlMKAGL 2477
Cdd:cd19546    44 LEAALGDVAARHEILRTTF--PGDGGDVHQRILdADAARPELPVVPATEEELPALLADRAAHLFDLT---RETP-WRCTL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2478 FQCADGDH-LLIAIHHLIIDGISWRILLEDIVSGYKQAENGRVIQ---LPQKTDSFQLWAKRLSEYAQS-ETIKQEQ-EY 2551
Cdd:cd19546   118 FALSDTEHvLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPErapLPLQFADYALWERELLAGEDDrDSLIGDQiAY 197

                  ...
gi 166797876 2552 WTK 2554
Cdd:cd19546   198 WRD 200
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
972-1115 1.22e-03

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 44.87  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876  972 DHLLIAIHHLLIDGVSWRILLEDFASGYEQaerRQTIQLPQKTDSFPFWADQLSkyaaetdmEEEIAYWTE-LSSIKPQP 1050
Cdd:cd19537   108 DTLLVVMSHIICDLTTLQLLLREVSAAYNG---KLLPPVRREYLDSTAWSRPAS--------PEDLDFWSEyLSGLPLLN 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166797876 1051 LPKDTIS---EGSllrdSEEVTIqwtKEETEQLLKQANRAYNTDINDLLLTSLGLAVHKWTGTEDIVV 1115
Cdd:cd19537   177 LPRRTSSksyRGT----SRVFQL---PGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVL 237
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
1912-2179 2.18e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 44.71  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1912 DVSHLAYVIYTSGSTGRPKGVLIEHGGLTN-----YIWWAKEVYvkGEKANFPlYSSISFDLTVTSIFTPLVTGNAI--- 1983
Cdd:PTZ00342  302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNtvvplCKHSIFKKY--NPKTHLS-YLPISHIYERVIAYLSFMLGGTIniw 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 1984 ---IVYDGEDktaLLES----IVRDPRV----------DIIKLTPahlqvLKEMNIADQTAVRR---------------- 2030
Cdd:PTZ00342  379 skdINYFSKD---IYNSkgniLAGVPKVfnriytnimtEINNLPP-----LKRFLVKKILSLRKsnnnggfskflegith 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2031 ---------------MIVGGENLSTRLARSIHEQFEgrIEICNEYGPTETvvGCMIYRYDAAKDRRESV--PIgtaAANT 2093
Cdd:PTZ00342  451 isskikdkvnpnlevILNGGGKLSPKIAEELSVLLN--VNYYQGYGLTET--TGPIFVQHADDNNTESIggPI---SPNT 523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 2094 SIYVLDENMKPAPIGVP-GEIYISGAGVARGYLNRPELTAEKFVDDPFepgakmYKTGDLAKWLADGNIEYAGRIDEQVK 2172
Cdd:PTZ00342  524 KYKVRTWETYKATDTLPkGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVK 597

                  ....*...
gi 166797876 2173 I-RGYRIE 2179
Cdd:PTZ00342  598 LsQGEYIE 605
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
4478-4517 2.76e-03

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 44.27  E-value: 2.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 166797876 4478 IYTSGTTGQPKGVQLEHKTMTNLLAYEQDHTQLRFDRVLQ 4517
Cdd:cd05933   156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQ 195
PRK09192 PRK09192
fatty acyl-AMP ligase;
3308-3478 2.84e-03

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 44.23  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3308 QFTYEELNRRANQLARTLQAKGVQADQLVGIMTERSLEMVVGILGVLKAGG--AYLPIdP------DSPSERIRYILNDS 3379
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPL-PmgfggrESYIAQLRGMLASA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3380 SISVLLYCGKL----QDDIGFSGTCIDLMEEHFYHEKDSSLALSYQS-SQLAYAIYTSGTTGKPKGTLIEHRQVIHLIEG 3454
Cdd:PRK09192  128 QPAAIITPDELlpwvNEATHGNPLLHVLSHAWFKALPEADVALPRPTpDDIAYLQYSSGSTRFPRGVIITHRALMANLRA 207
                         170       180
                  ....*....|....*....|....
gi 166797876 3455 LSRQVYSAYDAELNIAMLaPYYFD 3478
Cdd:PRK09192  208 ISHDGLKVRPGDRCVSWL-PFYHD 230
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
4854-4906 4.31e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.54  E-value: 4.31e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 166797876   4854 EIGVKDNFFDLGGHSLRGMTLIAKIHKQFSKNISLREVFQCPTVGEMAQAIAE 4906
Cdd:smart00823   32 AIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3623-3777 4.73e-03

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 43.42  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3623 RLQP-KGVQ--GELYIAGDGVGRGYLnlpeLTDEKFVADPfvPEDRMYRTGDLARLLPDGNIEYIGRIDHQVKIQGFRIE 3699
Cdd:PRK06814  971 RLEPvPGIDegGRLFVRGPNVMLGYL----RAENPGVLEP--PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMIS 1044
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166797876 3700 LGEIE-----------SVMLNVPDIQEAAAAALKDADDEYYLCGYFAADKTIQISELrkrmarhlpgyMIPAHFVQLDKM 3768
Cdd:PRK06814 1045 LAAVEelaaelwpdalHAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASEL-----------MVPAEIITIDEI 1113

                  ....*....
gi 166797876 3769 PLTPNGKLN 3777
Cdd:PRK06814 1114 PLLGTGKID 1122
prpE PRK10524
propionyl-CoA synthetase; Provisional
4472-4491 6.38e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 43.01  E-value: 6.38e-03
                          10        20
                  ....*....|....*....|
gi 166797876 4472 NDLMYVIYTSGTTGQPKGVQ 4491
Cdd:PRK10524  233 NEPSYILYTSGTTGKPKGVQ 252
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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