|
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
|
|