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Conserved domains on  [gi|260177242|gb|ACX33962|]
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putative non-ribosomal peptide synthetase [uncultured bacterium RM35]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1000107)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
 4-2433 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1865.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK12467 1116 PLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEE 1195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 --TDGSSWDEPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:PRK12467 1196 plLLAADKDEAQLKVYVEAEARQPFDLEQGPLlRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQS 1275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldvSTP-LDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRE 239
Cdd:PRK12467 1276 LQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGG---EQPvLELPTDRPRPAVQSHRGARLAFELPPALAEGLRA 1352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  240 SARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRV 319
Cdd:PRK12467 1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALE 1432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  320 TAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSFNEAirpegfghmlrwSRGPLGFEVEVPS--ELGSQLDLEVRC 397
Cdd:PRK12467 1433 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQA------------QAQLPGLSVESLSweSQTAQFDLTLDT 1500

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  398 YDFfSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHL 477
Cdd:PRK12467 1501 YES-SEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQL 1579

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERL--GEGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVT 635
Cdd:PRK12467 1660 RERLAYMIEDSGIELLLTQSHLQARLplPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNR 1739

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  636 HRNVVRLVRGSSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP-ESPTPEEIGRVVREHGVTTLWLTAPL 713
Cdd:PRK12467 1740 HGALVNRLCATQEAyQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPgAHRDPEQLIQLIERQQVTTLHFVPSM 1819

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FHAVA--DRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTG--SVPIGKPIA 789
Cdd:PRK12467 1820 LQQLLqmDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGrdSVPIGQPIA 1899

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  790 NTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDG 869
Cdd:PRK12467 1900 NLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF-GTVGSRLYRTGDLARYRADGVIEYLGRIDH 1978

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGdKRLVAYVVGREAEVPRF--------SELRKFLLQRLPDHMIP 941
Cdd:PRK12467 1979 QVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMVP 2057

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  942 AAVVALDKLPLVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAG 1021
Cdd:PRK12467 2058 AHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR 2137

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1022 AREVDLKLTVRQIFTHPTLSSLAAAAQATAVSGE-DQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKH 1100
Cdd:PRK12467 2138 ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSiDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAEL 2217

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1101 VDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSG---GPVPYE--VVDLSELpgeerraalEARAAEAQASLDLTDGPIL 1175
Cdd:PRK12467 2218 LEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEqerRPLLWQvvVADKEEL---------EALCEQAQRSLDLEEGPLL 2288

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1176 RVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWGERLLA-TVDEVVAAELPF 1254
Cdd:PRK12467 2289 RAVLATLPDGS-QRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTyAASAALADELGY 2367

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1255 WEALDGQGVRPLPRgcepaEDREGDAQT-----VEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAGGEAAY 1329
Cdd:PRK12467 2368 WQAQLQGASTELPC-----DHPQGGLQRrhaasVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTL 2442

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1330 VAVEGHGREELFPDIEVARTVGWFTTIHPVVLPGRPQSAGArLKAVKEAIRRVPKHGIGYGILRYLGSDEVVTRLARLPA 1409
Cdd:PRK12467 2443 IQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATS-IKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPV 2521

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1410 PEVAFNYLGRLDRALP--KDGPFVMAPEAAGPSVSPRGKRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQ 1487
Cdd:PRK12467 2522 PRITFNYLGQFDGSFDaeKQALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAE 2601

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1488 LLEELIAHAIDVGSEASwTPSDFPLARLEPHVLDALVDAdrARPLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALE 1567
Cdd:PRK12467 2602 ELRALIEHCCSNDQRGV-TPSDFPLAGLSQEQLDRLPVA--VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVE 2678

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1568 GaLDFDRLQQAWDETLGAHPALRASFLWEG-VPEPLQVVRRLVRIPTERIDARSMAVDGDAwIVERARDERRRGFALDAA 1646
Cdd:PRK12467 2679 G-LDVERFRTAWQAVIDRHEILRSGFLWDGeLEEPLQVVYKQARLPFSRLDWRDRADLEQA-LDALAAADRQQGFDLLSA 2756

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1647 PAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGgmqheaahRTAPRP---HRDYVAWLRGADAQSVERF 1723
Cdd:PRK12467 2757 PLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG--------QPPPARegrYRDYIAWLQAQDAEASEAF 2828

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1724 WRRELGGFREVTPLGIDRPPAGQRA-SSYRRFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGE 1802
Cdd:PRK12467 2829 WKEQLAALEEPTRLARALYPAPAEAvAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGA 2908

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1803 TVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAERTAYEHASLAQVQAWSEVPhGSALFESLIVVE 1882
Cdd:PRK12467 2909 TVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQG-GEALFDSILVFE 2987

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1883 NYPVAPAF--SGDE-LSVRLVGGDEQTNYPVTLVALPGRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTG 1959
Cdd:PRK12467 2988 NYPISEALkqGAPSgLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLG 3067

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1960 DLPLLSAHERRQVVADWNDTARAYARERCIHELFESSVERSPGSVALCYDGVpPLTYSDLNGRANRLGWLLRGLGAGPEE 2039
Cdd:PRK12467 3068 ELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQ-QLSYAELNRRANRLAHRLIAIGVGPDV 3146

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2040 RVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLgaveiaaRQLGIEHVV-SLDGDG 2118
Cdd:PRK12467 3147 LVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLL-------EQLPAPAGDtALTLDR 3219

                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2119 KDADGnvvihgrraladLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSP 2198
Cdd:PRK12467 3220 LDLNG------------YSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF 3287

                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2199 SFDLSVYDVFGMLAAGGSIHIASeDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRiEDGSQLRLAFLSGDWVPI 2278
Cdd:PRK12467 3288 SFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG-ADCASLDIYVFGGEAVPP 3365

                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2279 GMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDG-IDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCV 2357
Cdd:PRK12467 3366 AAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGdAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGL 3445

                        2410      2420      2430      2440      2450      2460      2470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 2358 SFGYYADPSQTAERFVPDPFSGEpGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:PRK12467 3446 ARGYHQRPSLTAERFVADPFSGS-GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 4-2433 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1865.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK12467 1116 PLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEE 1195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 --TDGSSWDEPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:PRK12467 1196 plLLAADKDEAQLKVYVEAEARQPFDLEQGPLlRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQS 1275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldvSTP-LDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRE 239
Cdd:PRK12467 1276 LQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGG---EQPvLELPTDRPRPAVQSHRGARLAFELPPALAEGLRA 1352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  240 SARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRV 319
Cdd:PRK12467 1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALE 1432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  320 TAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSFNEAirpegfghmlrwSRGPLGFEVEVPS--ELGSQLDLEVRC 397
Cdd:PRK12467 1433 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQA------------QAQLPGLSVESLSweSQTAQFDLTLDT 1500

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  398 YDFfSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHL 477
Cdd:PRK12467 1501 YES-SEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQL 1579

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERL--GEGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVT 635
Cdd:PRK12467 1660 RERLAYMIEDSGIELLLTQSHLQARLplPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNR 1739

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  636 HRNVVRLVRGSSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP-ESPTPEEIGRVVREHGVTTLWLTAPL 713
Cdd:PRK12467 1740 HGALVNRLCATQEAyQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPgAHRDPEQLIQLIERQQVTTLHFVPSM 1819

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FHAVA--DRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTG--SVPIGKPIA 789
Cdd:PRK12467 1820 LQQLLqmDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGrdSVPIGQPIA 1899

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  790 NTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDG 869
Cdd:PRK12467 1900 NLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF-GTVGSRLYRTGDLARYRADGVIEYLGRIDH 1978

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGdKRLVAYVVGREAEVPRF--------SELRKFLLQRLPDHMIP 941
Cdd:PRK12467 1979 QVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMVP 2057

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  942 AAVVALDKLPLVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAG 1021
Cdd:PRK12467 2058 AHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR 2137

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1022 AREVDLKLTVRQIFTHPTLSSLAAAAQATAVSGE-DQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKH 1100
Cdd:PRK12467 2138 ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSiDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAEL 2217

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1101 VDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSG---GPVPYE--VVDLSELpgeerraalEARAAEAQASLDLTDGPIL 1175
Cdd:PRK12467 2218 LEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEqerRPLLWQvvVADKEEL---------EALCEQAQRSLDLEEGPLL 2288

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1176 RVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWGERLLA-TVDEVVAAELPF 1254
Cdd:PRK12467 2289 RAVLATLPDGS-QRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTyAASAALADELGY 2367

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1255 WEALDGQGVRPLPRgcepaEDREGDAQT-----VEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAGGEAAY 1329
Cdd:PRK12467 2368 WQAQLQGASTELPC-----DHPQGGLQRrhaasVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTL 2442

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1330 VAVEGHGREELFPDIEVARTVGWFTTIHPVVLPGRPQSAGArLKAVKEAIRRVPKHGIGYGILRYLGSDEVVTRLARLPA 1409
Cdd:PRK12467 2443 IQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATS-IKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPV 2521

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1410 PEVAFNYLGRLDRALP--KDGPFVMAPEAAGPSVSPRGKRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQ 1487
Cdd:PRK12467 2522 PRITFNYLGQFDGSFDaeKQALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAE 2601

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1488 LLEELIAHAIDVGSEASwTPSDFPLARLEPHVLDALVDAdrARPLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALE 1567
Cdd:PRK12467 2602 ELRALIEHCCSNDQRGV-TPSDFPLAGLSQEQLDRLPVA--VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVE 2678

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1568 GaLDFDRLQQAWDETLGAHPALRASFLWEG-VPEPLQVVRRLVRIPTERIDARSMAVDGDAwIVERARDERRRGFALDAA 1646
Cdd:PRK12467 2679 G-LDVERFRTAWQAVIDRHEILRSGFLWDGeLEEPLQVVYKQARLPFSRLDWRDRADLEQA-LDALAAADRQQGFDLLSA 2756

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1647 PAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGgmqheaahRTAPRP---HRDYVAWLRGADAQSVERF 1723
Cdd:PRK12467 2757 PLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG--------QPPPARegrYRDYIAWLQAQDAEASEAF 2828

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1724 WRRELGGFREVTPLGIDRPPAGQRA-SSYRRFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGE 1802
Cdd:PRK12467 2829 WKEQLAALEEPTRLARALYPAPAEAvAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGA 2908

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1803 TVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAERTAYEHASLAQVQAWSEVPhGSALFESLIVVE 1882
Cdd:PRK12467 2909 TVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQG-GEALFDSILVFE 2987

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1883 NYPVAPAF--SGDE-LSVRLVGGDEQTNYPVTLVALPGRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTG 1959
Cdd:PRK12467 2988 NYPISEALkqGAPSgLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLG 3067

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1960 DLPLLSAHERRQVVADWNDTARAYARERCIHELFESSVERSPGSVALCYDGVpPLTYSDLNGRANRLGWLLRGLGAGPEE 2039
Cdd:PRK12467 3068 ELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQ-QLSYAELNRRANRLAHRLIAIGVGPDV 3146

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2040 RVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLgaveiaaRQLGIEHVV-SLDGDG 2118
Cdd:PRK12467 3147 LVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLL-------EQLPAPAGDtALTLDR 3219

                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2119 KDADGnvvihgrraladLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSP 2198
Cdd:PRK12467 3220 LDLNG------------YSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF 3287

                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2199 SFDLSVYDVFGMLAAGGSIHIASeDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRiEDGSQLRLAFLSGDWVPI 2278
Cdd:PRK12467 3288 SFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG-ADCASLDIYVFGGEAVPP 3365

                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2279 GMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDG-IDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCV 2357
Cdd:PRK12467 3366 AAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGdAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGL 3445

                        2410      2420      2430      2440      2450      2460      2470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 2358 SFGYYADPSQTAERFVPDPFSGEpGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:PRK12467 3446 ARGYHQRPSLTAERFVADPFSGS-GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 3-1324 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: 895.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    3 TPLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSL-----ADVS 77
Cdd:COG1020    16 APLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIqpvvaAPLP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   78 AVDFGVTDGSSWDEPTAAAWLQAEAARPFDLRAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVE 157
Cdd:COG1020    96 VVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  158 GRAATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLDvsTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRV 237
Cdd:COG1020   176 GAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLP--PLLELPTDRPRPAVQSYRGARVSFRLPAELTAAL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  238 RESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNAL 317
Cdd:COG1020   254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETL 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  318 RVTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFqeirSFNEAIRPEGFGHMLRWSRGPLGFEVevpselgSQLDLEVRC 397
Cdd:COG1020   334 LAAYAHQDLPFERLVEELQPERDLSRNPLFQVMF----VLQNAPADELELPGLTLEPLELDSGT-------AKFDLTLTV 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  398 YDFfSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHL 477
Cdd:COG1020   403 VET-GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHEL 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:COG1020   482 FEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYP 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDeDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHR 637
Cdd:COG1020   562 AERLAYMLEDAGARLVLTQSALAARLPELGVPVLALD-ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHR 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  638 NVVRLVRG-SSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPES-PTPEEIGRVVREHGVTTLWLTAPLFH 715
Cdd:COG1020   641 ALVNLLAWmQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEArRDPAALAELLARHRVTVLNLTPSLLR 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  716 AVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRG-MGTGSVPIGKPIANTHVY 794
Cdd:COG1020   721 ALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPdADGGSVPIGRPIANTRVY 800

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  795 LLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIR 874
Cdd:COG1020   801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-GFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIR 879

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  875 GFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVP 954
Cdd:COG1020   880 GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTG 959

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  955 SGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGAREVDLKLTVRQI 1034
Cdd:COG1020   960 NGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1035 FTHPTLSSLAAAAQATAVSGEDQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDA 1114
Cdd:COG1020  1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1115 LRLRFVAEDGMWRARGMPSGGPVPYEVVDLSELPGEERRAALEARAAEAQASLDLTDGPILRVVQFRLGPGEPDRLLVVV 1194
Cdd:COG1020  1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1195 HHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWgERLLATVDEVVAAELPFWEALDGQGVRPLPRGCEPAE 1274
Cdd:COG1020  1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALL-ALAALLALAALAALAAALLALALALLALALLLLALAL 1278

                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242 1275 DREGDAQTVEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAG 1324
Cdd:COG1020  1279 LLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 477-963 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: 670.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:cd12117     2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 PSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDnvsAENLAYVMYTSGSTGKPKGVAVTH 636
Cdd:cd12117    82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVS---PDDLAYVMYTSGSTGRPKGVAVTH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  637 RNVVRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESP-TPEEIGRVVREHGVTTLWLTAPLFH 715
Cdd:cd12117   159 RGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAALFN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  716 AVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRG-MGTGSVPIGKPIANTHVY 794
Cdd:cd12117   239 QLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELdEVAGSIPIGRPIANTRVY 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  795 LLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIR 874
Cdd:cd12117   319 VLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG--PGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  875 GFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPrfSELRKFLLQRLPDHMIPAAVVALDKLPLVP 954
Cdd:cd12117   397 GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLTA 474


                  ....*....
gi 260177242  955 SGKLDRRAL 963
Cdd:cd12117   475 NGKVDRRAL 483
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 499-898 4.43e-160

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: 501.03  E-value: 4.43e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   499 SYGELNRRADKLAHMLR-LKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAA 577
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   578 GAEERLGEGPWTVVRLDEDLGRPDER---DAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG-SSFATFGP 653
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDapaPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWlARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   654 DQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP--ESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLRGVRQL 731
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEdeERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   732 LAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGM--GTGSVPIGKPIANTHVYLLDEQMNPVPPNAVG 809
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDapRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   810 ELFTGGDGLARGYHERPDQTAERFVPDPFSGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQ 889
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 260177242   890 HPALREAVV 898
Cdd:TIGR01733  401 HPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
478-874 4.07e-104

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 340.83  E-value: 4.07e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   478 FEEEARRVPDAVALDAGSNV-VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   557 PSERLAFLAHDAGVQIVL--------SAAGAEERLGEGPWTVV---------RLDEDLGRPDERDAAPNDNVSAENLAYV 619
Cdd:pfam00501   81 PAEELAYILEDSGAKVLItddalkleELLEALGKLEVVKLVLVldrdpvlkeEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   620 MYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-----FGPDQVFLMMAPAAFDAS-TFEIWGALLHGARLVLFPPESPT-P 692
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfgLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALdP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   693 EEIGRVVREHGVTTLWLTAPLFHAVAD---RGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPAlRLINGYGPTENTTFTT 769
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagaPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   770 CHDVSRGMGTGSVPIGKPIANTHVYLLDEQ-MNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDpfsgvpgaRLYR 848
Cdd:pfam00501  320 TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED--------GWYR 391

                          410       420
                   ....*....|....*....|....*.
gi 260177242   849 TGDLARYLPNGDMEFLGRRDGQVKIR 874
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 976-1043 4.56e-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: 41.08  E-value: 4.56e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242    976 VAPEGHPEEVLARIWERVLRV------DAVGREDNFFELGGDSILAIQVVAG-AREVDLKLTVRQIFTHPTLSSL 1043
Cdd:smart00823    4 LPPAERRRLLLDLVREQVAAVlghaaaEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAAL 78
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 4-2433 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1865.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK12467 1116 PLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEE 1195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 --TDGSSWDEPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:PRK12467 1196 plLLAADKDEAQLKVYVEAEARQPFDLEQGPLlRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQS 1275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldvSTP-LDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRE 239
Cdd:PRK12467 1276 LQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGG---EQPvLELPTDRPRPAVQSHRGARLAFELPPALAEGLRA 1352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  240 SARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRV 319
Cdd:PRK12467 1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALE 1432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  320 TAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSFNEAirpegfghmlrwSRGPLGFEVEVPS--ELGSQLDLEVRC 397
Cdd:PRK12467 1433 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQA------------QAQLPGLSVESLSweSQTAQFDLTLDT 1500

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  398 YDFfSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHL 477
Cdd:PRK12467 1501 YES-SEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQL 1579

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERL--GEGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVT 635
Cdd:PRK12467 1660 RERLAYMIEDSGIELLLTQSHLQARLplPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNR 1739

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  636 HRNVVRLVRGSSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP-ESPTPEEIGRVVREHGVTTLWLTAPL 713
Cdd:PRK12467 1740 HGALVNRLCATQEAyQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPgAHRDPEQLIQLIERQQVTTLHFVPSM 1819

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FHAVA--DRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTG--SVPIGKPIA 789
Cdd:PRK12467 1820 LQQLLqmDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGrdSVPIGQPIA 1899

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  790 NTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDG 869
Cdd:PRK12467 1900 NLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF-GTVGSRLYRTGDLARYRADGVIEYLGRIDH 1978

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGdKRLVAYVVGREAEVPRF--------SELRKFLLQRLPDHMIP 941
Cdd:PRK12467 1979 QVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMVP 2057

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  942 AAVVALDKLPLVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAG 1021
Cdd:PRK12467 2058 AHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR 2137

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1022 AREVDLKLTVRQIFTHPTLSSLAAAAQATAVSGE-DQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKH 1100
Cdd:PRK12467 2138 ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSiDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAEL 2217

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1101 VDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSG---GPVPYE--VVDLSELpgeerraalEARAAEAQASLDLTDGPIL 1175
Cdd:PRK12467 2218 LEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEqerRPLLWQvvVADKEEL---------EALCEQAQRSLDLEEGPLL 2288

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1176 RVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWGERLLA-TVDEVVAAELPF 1254
Cdd:PRK12467 2289 RAVLATLPDGS-QRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTyAASAALADELGY 2367

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1255 WEALDGQGVRPLPRgcepaEDREGDAQT-----VEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAGGEAAY 1329
Cdd:PRK12467 2368 WQAQLQGASTELPC-----DHPQGGLQRrhaasVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTL 2442

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1330 VAVEGHGREELFPDIEVARTVGWFTTIHPVVLPGRPQSAGArLKAVKEAIRRVPKHGIGYGILRYLGSDEVVTRLARLPA 1409
Cdd:PRK12467 2443 IQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATS-IKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPV 2521

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1410 PEVAFNYLGRLDRALP--KDGPFVMAPEAAGPSVSPRGKRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQ 1487
Cdd:PRK12467 2522 PRITFNYLGQFDGSFDaeKQALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAE 2601

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1488 LLEELIAHAIDVGSEASwTPSDFPLARLEPHVLDALVDAdrARPLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALE 1567
Cdd:PRK12467 2602 ELRALIEHCCSNDQRGV-TPSDFPLAGLSQEQLDRLPVA--VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVE 2678

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1568 GaLDFDRLQQAWDETLGAHPALRASFLWEG-VPEPLQVVRRLVRIPTERIDARSMAVDGDAwIVERARDERRRGFALDAA 1646
Cdd:PRK12467 2679 G-LDVERFRTAWQAVIDRHEILRSGFLWDGeLEEPLQVVYKQARLPFSRLDWRDRADLEQA-LDALAAADRQQGFDLLSA 2756

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1647 PAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGgmqheaahRTAPRP---HRDYVAWLRGADAQSVERF 1723
Cdd:PRK12467 2757 PLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG--------QPPPARegrYRDYIAWLQAQDAEASEAF 2828

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1724 WRRELGGFREVTPLGIDRPPAGQRA-SSYRRFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGE 1802
Cdd:PRK12467 2829 WKEQLAALEEPTRLARALYPAPAEAvAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGA 2908

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1803 TVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAERTAYEHASLAQVQAWSEVPhGSALFESLIVVE 1882
Cdd:PRK12467 2909 TVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQG-GEALFDSILVFE 2987

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1883 NYPVAPAF--SGDE-LSVRLVGGDEQTNYPVTLVALPGRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTG 1959
Cdd:PRK12467 2988 NYPISEALkqGAPSgLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLG 3067

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1960 DLPLLSAHERRQVVADWNDTARAYARERCIHELFESSVERSPGSVALCYDGVpPLTYSDLNGRANRLGWLLRGLGAGPEE 2039
Cdd:PRK12467 3068 ELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQ-QLSYAELNRRANRLAHRLIAIGVGPDV 3146

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2040 RVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLgaveiaaRQLGIEHVV-SLDGDG 2118
Cdd:PRK12467 3147 LVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLL-------EQLPAPAGDtALTLDR 3219

                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2119 KDADGnvvihgrraladLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSP 2198
Cdd:PRK12467 3220 LDLNG------------YSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF 3287

                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2199 SFDLSVYDVFGMLAAGGSIHIASeDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRiEDGSQLRLAFLSGDWVPI 2278
Cdd:PRK12467 3288 SFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG-ADCASLDIYVFGGEAVPP 3365

                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2279 GMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDG-IDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCV 2357
Cdd:PRK12467 3366 AAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGdAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGL 3445

                        2410      2420      2430      2440      2450      2460      2470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 2358 SFGYYADPSQTAERFVPDPFSGEpGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:PRK12467 3446 ARGYHQRPSLTAERFVADPFSGS-GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
PRK12316 PRK12316
peptide synthase; Provisional
 4-2442 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1765.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLV-VRPDNEGLVQSLADvSAVDFG 82
Cdd:PRK12316   49 RDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVfPRGADDSLAQVPLD-RPLEVE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   83 VTDGSSWDEPTAAAWLQAEAAR----PFDLRAGA-LRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVE 157
Cdd:PRK12316  128 FEDCSGLPEAEQEARLRDEAQReslqPFDLCEGPlLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYAT 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  158 GRAATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldvSTP-LDLPTDLPRRAQQRYHVRQHFRDLGADLMDR 236
Cdd:PRK12316  208 GAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGE---EHPvLELPTDHPRPAVPSYRGSRYEFSIDPALAEA 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  237 VRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNA 316
Cdd:PRK12316  285 LRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDT 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  317 LRVTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEirsfneaiRPEGFGHMLRWSRGPLGFEVEVPSELGSQLDLEVR 396
Cdd:PRK12316  365 VLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNH--------QPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLD 436

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  397 CYDFfSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHH 476
Cdd:PRK12316  437 TYEK-GGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHR 515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:PRK12316  516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 PSERLAFLAHDAGVQIVLSAAGAEERLG-EGPWTVVRLDE-DLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAV 634
Cdd:PRK12316  596 PAERLAYMLEDSGVQLLLSQSHLGRKLPlAAGVQVLDLDRpAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGN 675

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  635 THRNVVRLVRGSSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPT-PEEIGRVVREHGVTTLWLTAP 712
Cdd:PRK12316  676 RHRALSNRLCWMQQAyGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRdPAKLVELINREGVDTLHFVPS 755

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  713 LFHA-VADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTEnTTFTTCHDVSRGMGTGSVPIGKPIANT 791
Cdd:PRK12316  756 MLQAfLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTE-AAIDVTHWTCVEEGGDSVPIGRPIANL 834

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  792 HVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQV 871
Cdd:PRK12316  835 ACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPF--VAGERMYRTGDLARYRADGVIEYAGRIDHQV 912

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  872 KIRGFRIELAEVEAALLQHPALREAVVIAREDrpgdKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLP 951
Cdd:PRK12316  913 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLP 988

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  952 LVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGAREVDLKLTV 1031
Cdd:PRK12316  989 LTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSP 1068

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1032 RQIFTHPTLSSLAAAAQATAVSGEDQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRH 1111
Cdd:PRK12316 1069 RDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAH 1148

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1112 HDALRLRFVAEDGMWRAR-GMPSGGPVPY--EVVDLSELpgeerraalEARAAEAQASLDLTDGPILRVVQFRLGPGEpD 1188
Cdd:PRK12316 1149 HDALRLRFREEDGGWQQAyAAPQAGEVLWqrQAASEEEL---------LALCEEAQRSLDLEQGPLLRALLVDMADGS-Q 1218

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1189 RLLVVVHHLAVDVVSWGILLADLATAHRQLVegeiVRLPSKTTSLRRWGERLLATVdEVVAAELPFWEALDGQGVRPLPr 1268
Cdd:PRK12316 1219 RLLLVIHHLVVDGVSWRILLEDLQRAYADLD----ADLPARTSSYQAWARRLHEHA-GARAEELDYWQAQLEDAPHELP- 1292

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1269 gCE-PAEDREGD-AQTVEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREELFPDIEV 1346
Cdd:PRK12316 1293 -CEnPDGALENRhERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDL 1371

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1347 ARTVGWFTTIHPVVLPGRpQSAGARLKAVKEAIRRVPKHGIGYGILRYLGSDEVVTRLARLPAPEVAFNYLGRLDRALPK 1426
Cdd:PRK12316 1372 SRTVGWFTSLFPVRLTPA-ADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNYLGQFDRQFDE 1450

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1427 DGPFVMAPEAAGPSVSPRGKRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAHAIDVGSEASwT 1506
Cdd:PRK12316 1451 AALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGV-T 1529

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1507 PSDFPLARLEPHVLDAL-VDADRarpLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGaLDFDRLQQAWDETLGA 1585
Cdd:PRK12316 1530 PSDFPLAGLSQAQLDALpLPAGE---IADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDR 1605

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1586 HPALRASFLWE-GVPEPLQVVRRLVRIPTERIDARSMAvDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLI 1664
Cdd:PRK12316 1606 HEILRSGFLWQdGLEQPLQVIHKQVELPFAELDWRGRE-DLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLI 1684

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1665 WTFHHILLDGWSVPLVLEEVFKRYSGGMQHEAAHRtaprpHRDYVAWLRGADAQSVERFWRRELGGFREVTPLG-IDRPP 1743
Cdd:PRK12316 1685 YTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGR-----YRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAqAARTE 1759

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1744 AGQraSSYRRFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFIN 1823
Cdd:PRK12316 1760 DGQ--VGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFIN 1837

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1824 TVPMRAVVDPERPIGEWLTELQGRRAERTAYEHASLAQVQAWSEVpHGSALFESLIVVENYPVAPAF-SGDELSVRL--V 1900
Cdd:PRK12316 1838 TLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQ-GGEALFDSLLVFENYPVAEALkQGAPAGLVFgrV 1916

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1901 GGDEQTNYPVTLVALPGRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVVADWNDTA 1980
Cdd:PRK12316 1917 SNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTP 1996

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1981 RAYARERCIHELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILK 2060
Cdd:PRK12316 1997 EAYPRGPGVHQRIAEQAARAPEAIAVVFGD-QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLK 2075

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2061 TGGAYVPLDPRWPLERVAAVLGTTRPVCIVTdERHLgaveiAARQLGIEHVVSLDGDGKDadgnvvihgrrALADLADGN 2140
Cdd:PRK12316 2076 AGGAYVPLDPNYPAERLAYMLEDSGAALLLT-QRHL-----LERLPLPAGVARLPLDRDA-----------EWADYPDTA 2138

                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2141 LPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIhIA 2220
Cdd:PRK12316 2139 PAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LI 2217

                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2221 SEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGAT 2300
Cdd:PRK12316 2218 RDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPT 2297

                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2301 EATVWSNYFEVDGIDPR-WTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSG 2379
Cdd:PRK12316 2298 EAVVTPLLWKCRPQDPCgAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSA 2377

                        2410      2420      2430      2440      2450      2460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 2380 ePGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQRG-----RGSGGPE 2442
Cdd:PRK12316 2378 -SGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAvvvaqDGASGKQ 2444
PRK12316 PRK12316
peptide synthase; Provisional
 4-2430 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1719.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK12316 2602 PLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVL 2681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSSWDEPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRAAT 162
Cdd:PRK12316 2682 EDCAGVADAAIRQRVAEEIQRPFDLARGPLlRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPT 2761

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  163 LTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLDvsTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRESAR 242
Cdd:PRK12316 2762 LPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQ--PVLELPLDRPRPALQSHRGARLDVALDVALSRELLALAR 2839

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  243 AEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRVTAK 322
Cdd:PRK12316 2840 REGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQA 2919

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  323 LQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSFNEAIRPEGfghmlrwsrgpLGFEVEVPSELGSQLDLEVRCYDFfS 402
Cdd:PRK12316 2920 HQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPG-----------LHIESFAWDGAATQFDLALDTWES-A 2987

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  403 SSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHLFEEEA 482
Cdd:PRK12316 2988 EGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQV 3067

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  483 RRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLA 562
Cdd:PRK12316 3068 ERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLA 3147

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  563 FLAHDAGVQIVLSAAGAEERLGEGpwtVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRL 642
Cdd:PRK12316 3148 YMLEDSGAQLLLSQSHLRLPLAQG---VQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNH 3224

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  643 VRGSSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPE-SPTPEEIGRVVREHGVTTLWLT-APLFHAVAD 719
Cdd:PRK12316 3225 LCWMQQAyGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEdWRDPALLVELINSEGVDVLHAYpSMLQAFLEE 3304

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  720 RGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPalrLINGYGPTENTTFTTCHDVSRGmGTGSVPIGKPIANTHVYLLDEQ 799
Cdd:PRK12316 3305 EDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEE-GKDAVPIGRPIANRACYILDGS 3380

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  800 MNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIE 879
Cdd:PRK12316 3381 LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFV--PGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIE 3458

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  880 LAEVEAALLQHPALREAVVIAREDRpgdkRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLD 959
Cdd:PRK12316 3459 LGEIEARLLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLD 3534

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  960 RRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGAREVDLKLTVRQIFTHPT 1039
Cdd:PRK12316 3535 RKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQT 3614

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1040 LSSLAAAAQATAVSGEDQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRF 1119
Cdd:PRK12316 3615 IQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRF 3694

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1120 VAEDGMWRARGMPS--GGPVPY--EVVDLSELpgeerraalEARAAEAQASLDLTDGPILRVVQFRLGPGEpDRLLVVVH 1195
Cdd:PRK12316 3695 VEDAGGWTAEHLPVelGGALLWraELDDAEEL---------ERLGEEAQRSLDLADGPLLRALLATLADGS-QRLLLVIH 3764

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1196 HLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWGERLLATV-DEVVAAELPFWEALDGQGVRPLPrgCE-PA 1273
Cdd:PRK12316 3765 HLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHArGEALKAELAYWQEQLQGVSSELP--CDhPQ 3842

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1274 EDREGD-AQTVEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREELFPDIEVARTVGW 1352
Cdd:PRK12316 3843 GALQNRhAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGW 3922

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1353 FTTIHPVVLPGRpQSAGARLKAVKEAIRRVPKHGIGYGILRYLGSDEVVTRLARLPAPEVAFNYLGRLDRALPKDGP-FV 1431
Cdd:PRK12316 3923 FTSLFPVRLSPV-EDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFDGSFDEEMAlFV 4001

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1432 MAPEAAGPSVSPRGKRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAHAIDVGSEASwTPSDFP 1511
Cdd:PRK12316 4002 PAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAERHGV-TPSDFP 4080

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1512 LARLEPHVLDALVDAdrARPLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGaLDFDRLQQAWDETLGAHPALRA 1591
Cdd:PRK12316 4081 LAGLDQARLDALPLP--LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRS 4157

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1592 SFLWEGVPE-PLQVVRRLVRIPTERIDARSMAvDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHI 1670
Cdd:PRK12316 4158 GFVWQGELGrPLQVVHKQVSLPFAELDWRGRA-DLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHI 4236

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1671 LLDGWSVPLVLEEVFKRYSGGMQHEAAHRtaprpHRDYVAWLRGADAQSVERFWRRELGGFREVTPLGID-RPPAGQRAS 1749
Cdd:PRK12316 4237 LMDGWSNSQLLGEVLERYSGRPPAQPGGR-----YRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAiARADLRSAN 4311

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1750 SYRRFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFINTVPMRA 1829
Cdd:PRK12316 4312 GYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIA 4391

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1830 VVDPERPIGEWLTELQGRRAERTAYEHASLAQVQAWSEVpHGSALFESLIVVENYPVAPAFS-GDELSVRL--VGGDEQT 1906
Cdd:PRK12316 4392 TPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQ-GGEALFDSLLVFENYPVSEALQqGAPGGLRFgeVTNHEQT 4470

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1907 NYPVTLVALPGRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVVADWNDTARAYARE 1986
Cdd:PRK12316 4471 NYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPAT 4550

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1987 RCIHELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYV 2066
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDE-EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2067 PLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAArqlGIeHVVSLDGDGKdadgnvvihgrraLADLADGNLPRAAG 2146
Cdd:PRK12316 4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPD---GL-ASLALDRDED-------------WEGFPAHDPAVRLH 4692

                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2147 PHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIAsEDDLR 2226
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLW 4771

                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2227 SPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWS 2306
Cdd:PRK12316 4772 DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTV 4851

                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2307 NYFEV-DGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEPGARL 2385
Cdd:PRK12316 4852 LLWKArDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGGRL 4930

                        2410      2420      2430      2440
                  ....*....|....*....|....*....|....*....|....*
gi 260177242 2386 YRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK12316 4931 YRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHP 4975
PRK05691 PRK05691
peptide synthase; Validated
 4-2431 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1514.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK05691 1728 PVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDW 1807

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSSWD----EPTAAAWLQAEAARPFDLRAGALRVRALRRAPDQWQIL-FAFHHIVCDGWSAMIVAAEFAELCAADVEG 158
Cdd:PRK05691 1808 QDFSALPadarQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFvLTLHHIVTEGWAMDIFARELGALYEAFLDD 1887

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  159 RAATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldvSTP-LDLPTDLPRRAQQRyHVRQHFR-DLGADLMDR 236
Cdd:PRK05691 1888 RESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGN---EHPlLELPADRPRPPVQS-HRGELYRfDLSPELAAR 1963

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  237 VRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNA 316
Cdd:PRK05691 1964 VRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQT 2043

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  317 LRVTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFqeirsfneairpegfgHMLRW----SRGPLGFEVE--VPSELGSQ 390
Cdd:PRK05691 2044 VIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMC----------------NVQRWefqqSRQLAGMTVEylVNDARATK 2107

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  391 LDLEVRCYDFfSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPR 470
Cdd:PRK05691 2108 FDLNLEVTDL-DGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARL 2186

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  471 ERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYV 550
Cdd:PRK05691 2187 DQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYV 2266

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  551 PLDPAYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVR--LDEDLGRPDERDAAPNDNVS-AENLAYVMYTSGSTG 627
Cdd:PRK05691 2267 PLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARwcLEDDAAALAAYSDAPLPFLSlPQHQAYLIYTSGSTG 2346

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  628 KPKGVAVTHRNVVRLVRgSSFATFG--PDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTPEEIGRVVREHGVT 705
Cdd:PRK05691 2347 KPKGVVVSHGEIAMHCQ-AVIERFGmrADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVS 2425

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  706 TLWLT----APLFHAVADRGldQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGM--GT 779
Cdd:PRK05691 2426 ILGFTpsygSQLAQWLAGQG--EQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLeeGA 2503

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  780 GSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSgVPGARLYRTGDLARYLPNG 859
Cdd:PRK05691 2504 ASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFA-ADGGRLYRTGDLVRLRADG 2582

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  860 DMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAReDRPGDKRLVAYVVGR-----EAEVPRFSE-LRKFLLQ 933
Cdd:PRK05691 2583 LVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAvagqdDEAQAALREaLKAHLKQ 2661

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  934 RLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSI 1013
Cdd:PRK05691 2662 QLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSI 2741

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1014 LAIQVVAGAREVDLKLTVRQIFTHPTLSSLAAAAQATAVSGEDQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALR 1093
Cdd:PRK05691 2742 LSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPR 2821

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1094 DAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSGGPVPYEVVDLSELpgeerrAALEARAAEAQASLDLTDGP 1173
Cdd:PRK05691 2822 QALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELLWQVTVADF------AECAALFADAQRSLDLQQGP 2895

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1174 ILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWGERLLATV-DEVVAAEL 1252
Cdd:PRK05691 2896 LLRALLVDGPQGQ-QRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAgSESLREEL 2974

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1253 PFWEALDGQGVRPLPRGCEPAEDREGDAQTVEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAGGEAAYVAV 1332
Cdd:PRK05691 2975 GWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQL 3054

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1333 EGHGREELFPDIEVARTVGWFTTIHPVVL---PGRPQSAGARLKAVKEAIRRVPKHGIGYGILRYLGSDEVVTRLARLPA 1409
Cdd:PRK05691 3055 EGHGREALFDDIDLTRSVGWFTSAYPLRLtpaPGDDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQ 3134

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1410 PEVAFNYLGRLDRALPKDGPFVMAPEAAGPSVSPRGKRSHALQtmVVAEPQG--LRTRFAFQPKRHSHEEIARLAARYGQ 1487
Cdd:PRK05691 3135 APITFNYLGQFDQSFASDALFRPLDEPAGPAHDPDAPLPNELS--VDGQVYGgeLVLRWTYSAERYDEQTIAELAEAYLA 3212

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1488 LLEELIAHAIDVGSeASWTPSDFPLARLEPHVLDALvdADRARPLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALE 1567
Cdd:PRK05691 3213 ELQALIAHCLADGA-GGLTPSDFPLAQLTQAQLDAL--PVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRIN 3289

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1568 GALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPTERIDARSMAVDG-DAWIVERARDERRRGFALDAA 1646
Cdd:PRK05691 3290 SALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGqEQRLQALHKQEREAGFDLLNQ 3369

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1647 PAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSG-GMQHEAAHRTAPRpHRDYVAWLRGADAQSVERFWR 1725
Cdd:PRK05691 3370 PPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTAlGEGREAQLPVPPR-YRDYIGWLQRQDLAQARQWWQ 3448

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1726 RELGGFREVTPLGIDRPPAGQRASS---------YRRferaLDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRR 1796
Cdd:PRK05691 3449 DNLRGFERPTPIPSDRPFLREHAGDsggmvvgdcYTR----LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDR 3524

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1797 DVVFGETVSGRSAPLEGIERMVGLFINTVPMRA---VVDPERPIGEWLTELQGRRAERTAYEHASLAQVQAWSEVPHGSA 1873
Cdd:PRK05691 3525 DVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVqlpAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQP 3604

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1874 LFESLIVVENYPVAPAF--SGDELSVRLVGGDEQTNYPVTLVALPGRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIA 1951
Cdd:PRK05691 3605 LFDSLFVFENAPVEVSVldRAQSLNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALV 3684

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1952 DDPDLPTGDLPLLSAHERRQVVADWNDTARAYARERCIHELFESSVERSPGS-VALCYDGvpPLTYSDLNGRANRLGWLL 2030
Cdd:PRK05691 3685 QGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRiAASCLDQ--QWSYAELNRAANRLGHAL 3762

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2031 RGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTR-PVCIVTDerhlgaveiAARQLGIE 2109
Cdd:PRK05691 3763 RAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRtPVLVCSA---------ACREQARA 3833

                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2110 HVVSLDGDGKDadgNVVIHGRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGV-VERHSQVINLIEWVnrTYL-VG 2187
Cdd:PRK05691 3834 LLDELGCANRP---RLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVmVEQRGMLNNQLSKV--PYLaLS 3908

                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2188 PSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEDGsqLR 2267
Cdd:PRK05691 3909 EADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDG--LR 3986

                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2268 LAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVT 2347
Cdd:PRK05691 3987 WMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAV 4066

                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2348 GDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALA 2427
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFVPHPF-GAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLH 4145


                  ....
gi 260177242 2428 QHPG 2431
Cdd:PRK05691 4146 EQAE 4149
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 3-1324 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: 895.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    3 TPLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSL-----ADVS 77
Cdd:COG1020    16 APLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIqpvvaAPLP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   78 AVDFGVTDGSSWDEPTAAAWLQAEAARPFDLRAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVE 157
Cdd:COG1020    96 VVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  158 GRAATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLDvsTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRV 237
Cdd:COG1020   176 GAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLP--PLLELPTDRPRPAVQSYRGARVSFRLPAELTAAL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  238 RESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNAL 317
Cdd:COG1020   254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETL 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  318 RVTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFqeirSFNEAIRPEGFGHMLRWSRGPLGFEVevpselgSQLDLEVRC 397
Cdd:COG1020   334 LAAYAHQDLPFERLVEELQPERDLSRNPLFQVMF----VLQNAPADELELPGLTLEPLELDSGT-------AKFDLTLTV 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  398 YDFfSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHL 477
Cdd:COG1020   403 VET-GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHEL 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:COG1020   482 FEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYP 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDeDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHR 637
Cdd:COG1020   562 AERLAYMLEDAGARLVLTQSALAARLPELGVPVLALD-ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHR 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  638 NVVRLVRG-SSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPES-PTPEEIGRVVREHGVTTLWLTAPLFH 715
Cdd:COG1020   641 ALVNLLAWmQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEArRDPAALAELLARHRVTVLNLTPSLLR 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  716 AVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRG-MGTGSVPIGKPIANTHVY 794
Cdd:COG1020   721 ALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPdADGGSVPIGRPIANTRVY 800

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  795 LLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIR 874
Cdd:COG1020   801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-GFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIR 879

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  875 GFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVP 954
Cdd:COG1020   880 GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTG 959

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  955 SGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGAREVDLKLTVRQI 1034
Cdd:COG1020   960 NGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1035 FTHPTLSSLAAAAQATAVSGEDQGEITGEMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDA 1114
Cdd:COG1020  1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1115 LRLRFVAEDGMWRARGMPSGGPVPYEVVDLSELPGEERRAALEARAAEAQASLDLTDGPILRVVQFRLGPGEPDRLLVVV 1194
Cdd:COG1020  1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1195 HHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWgERLLATVDEVVAAELPFWEALDGQGVRPLPRGCEPAE 1274
Cdd:COG1020  1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALL-ALAALLALAALAALAAALLALALALLALALLLLALAL 1278

                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242 1275 DREGDAQTVEVWLGGPETEALLGRVGEAYRTRADEVILAALAGALTEWAG 1324
Cdd:COG1020  1279 LLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
PRK12467 PRK12467
peptide synthase; Provisional
 5-1227 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 813.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    5 LPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGVT 84
Cdd:PRK12467   50 IPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   85 DGSSWD----EPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGR 159
Cdd:PRK12467  130 DLANEQgrarESQIEAYINEEVARPFDLANGPLlRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGR 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  160 AATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldVSTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRE 239
Cdd:PRK12467  210 EPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGG--EHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKA 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  240 SARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRV 319
Cdd:PRK12467  288 LAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALG 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  320 TAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFqeirsfNEAIRPEGFGHMLRWSRGPLGFEVEVPSELGSQLDLEVrcyD 399
Cdd:PRK12467  368 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMF------NHQNTATGGRDREGAQLPGLTVEELSWARHTAQFDLAL---D 438

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  400 FFSSS--VRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPReRCLHHL 477
Cdd:PRK12467  439 TYESAqgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAP-DCVHQL 517

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:PRK12467  518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERLG-EGPWTVVRLDEDLGRPDERDAA-PNDNVSAENLAYVMYTSGSTGKPKGVAVT 635
Cdd:PRK12467  598 QDRLAYMLDDSGVRLLLTQSHLLAQLPvPAGLRSLCLDEPADLLCGYSGHnPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  636 HRNVVRLVRG-SSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESP-TPEEIGRVVREHGVTTLWLTAPL 713
Cdd:PRK12467  678 HGALANYVCViAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCArDAEAFAALMADQGVTVLKIVPSH 757

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FHAVADRGL-DQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSR-GMGTGSVPIGKPIANT 791
Cdd:PRK12467  758 LQALLQASRvALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDeERDFGNVPIGQPLANL 837

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  792 HVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQV 871
Cdd:PRK12467  838 GLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPF-GADGGRLYRTGDLARYRADGVIEYLGRMDHQV 916

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  872 KIRGFRIELAEVEAALLQHPALREAVVIArEDRPGDKRLVAYVV---GREAEVP--RFSELRKFLLQRLPDHMIPAAVVA 946
Cdd:PRK12467  917 KIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVpaaVADGAEHqaTRDELKAQLRQVLPDYMVPAHLLL 995

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  947 LDKLPLVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGAREV- 1025
Cdd:PRK12467  996 LDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRl 1075

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1026 DLKLTVRQIFTHPTLSSLaaaaqATAVSGEDQGEITG--------EMPLTPIQ--RWFL-SGEP-AAPHHFNQAvlLALR 1093
Cdd:PRK12467 1076 GIQVPLRTLFEHQTLAGF-----AQAVAAQQQGAQPAlpdvdrdqPLPLSYAQerQWFLwQLEPgSAAYHIPQA--LRLK 1148

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1094 DAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSgGPVPYEvVDLSELPGEERRAALEARAAEAQASLDLTDGP 1173
Cdd:PRK12467 1149 GPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPV-GSLTLE-EPLLLAADKDEAQLKVYVEAEARQPFDLEQGP 1226

                        1210      1220      1230      1240      1250
                  ....*....|....*....|....*....|....*....|....*....|....
gi 260177242 1174 ILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIVRLP 1227
Cdd:PRK12467 1227 LLRVGLLRLAADE-HVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLP 1279
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1520-2431 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: 727.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1520 LDALVDADRARPLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVP 1599
Cdd:COG1020     2 AAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1600 EPLQVVRRLVRIPTERIDARSMAVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPL 1679
Cdd:COG1020    82 PVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1680 VLEEVFKRYSGGMQHEAAHR-----TAPRPHRDYVAWLRGADAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRF 1754
Cdd:COG1020   162 LLAELLRLYLAAYAGAPLPLpplpiQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1755 ERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPleGIERMVGLFINTVPMRAVVDPE 1834
Cdd:COG1020   242 SFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGD 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1835 RPIGEWLTELQGRRAERTAYEHASLAQVQ---AWSEVPHGSALFESLIVVENYPVaPAFSGDELSVRLVGGDEQT-NYPV 1910
Cdd:COG1020   320 PSFAELLARVRETLLAAYAHQDLPFERLVeelQPERDLSRNPLFQVMFVLQNAPA-DELELPGLTLEPLELDSGTaKFDL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1911 TLVALP-GRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVVADWNDTARAYARERCI 1989
Cdd:COG1020   399 TLTVVEtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATL 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1990 HELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLD 2069
Cdd:COG1020   479 HELFEAQAARTPDAVAVVFGDQS-LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2070 PRWPLERVAAVLGTTRPVCIVTDERHlgAVEIAARQLgieHVVSLDGDgkdadgnvvihgrrALADLADGNLPRAAGPHN 2149
Cdd:COG1020   558 PAYPAERLAYMLEDAGARLVLTQSAL--AARLPELGV---PVLALDAL--------------ALAAEPATNPPVPVTPDD 618

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2150 MAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPE 2229
Cdd:COG1020   619 LAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPA 698

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLAAELGRGTITFWDSAPAALQQLVPYfdRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYF 2309
Cdd:COG1020   699 ALAELLARHRVTVLNLTPSLLRALLDA--APEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYY 776

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2310 EVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEPGARLYRTG 2389
Cdd:COG1020   777 EVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-GFPGARLYRTG 855

                         890       900       910       920
                  ....*....|....*....|....*....|....*....|..
gi 260177242 2390 DLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:COG1020   856 DLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPG 897
PRK12316 PRK12316
peptide synthase; Provisional
 39-1496 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 713.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   39 LSEAAIRRSMEAVLERRDALR--LVVRPDNEGLVQSLADVSAVDFGVTDGSSWDEPTAAAWLQAEAARP--FDL-RAGAL 113
Cdd:PRK12316 1590 LDPDRFRAAWQATVDRHEILRsgFLWQDGLEQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAERQkgFDLtRAPLL 1669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  114 RVRALRRAPDQWQILFAFHHIVCDGWSAmivaaefAELCAADVEGRAATLTPISRG-FRDYLVWhrdlLASDDASALVRE 192
Cdd:PRK12316 1670 RLVLVRTGEGRHHLIYTNHHILMDGWSN-------AQLLGEVLQRYAGQPVAAPGGrYRDYIAW----LQRQDAAASEAF 1738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  193 WAAMVGDLDVSTPLdlpTDLPRRAQQRYHVRQHFRDLGADLMDRVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVG 272
Cdd:PRK12316 1739 WKEQLAALEEPTRL---AQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFG 1815

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  273 CGVSGRTRTWQlGV---VGHMAGIVPVparidaAATPRAiirelrnALRVTAKLQSVPLSRLA--EQCRVPkspgrMPLV 347
Cdd:PRK12316 1816 ATVAGRPAELP-GIeqqIGLFINTLPV------IAAPRP-------DQSVADWLQEVQALNLAlrEHEHTP-----LYDI 1876

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  348 Q--------AVFQEIRSFN-----EAIR---PEG--FG--HMLRWSRGPLGFEVEvpseLGSQLDLEvrcydffsssvrt 407
Cdd:PRK12316 1877 QrwagqggeALFDSLLVFEnypvaEALKqgaPAGlvFGrvSNHEQTNYPLTLAVT----LGETLSLQ------------- 1939

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  408 cWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHLFEEEARRVPD 487
Cdd:PRK12316 1940 -YSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPE 2018

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  488 AVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHD 567
Cdd:PRK12316 2019 AIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLED 2098

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  568 AGVQIVLSAAGAEERLgEGPWTVVRL--DEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV-RLVR 644
Cdd:PRK12316 2099 SGAALLLTQRHLLERL-PLPAGVARLplDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVaHCQA 2177

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  645 GSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQ 724
Cdd:PRK12316 2178 AGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERD 2257

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  725 LR--GVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSR--GMGTGSVPIGKPIANTHVYLLDEQM 800
Cdd:PRK12316 2258 GRppAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPqdPCGAAYVPIGRALGNRRAYILDADL 2337

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  801 NPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIEL 880
Cdd:PRK12316 2338 NLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSA-SGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIEL 2416

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  881 AEVEAALLQHPALREAVVIAReDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:PRK12316 2417 GEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDR 2495

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  961 RALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGARE-VDLKLTVRQIFTHPT 1039
Cdd:PRK12316 2496 KALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQdLGLEVPLRILFERPT 2575

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1040 LSSLAAAAQATAVS-GEDQGEITGEMPL----TPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDA 1114
Cdd:PRK12316 2576 LAAFAASLESGQTSrAPVLQKVTRVQPLplshAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHET 2655

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1115 LRLRFVAEDGMWRARGMPSGG--PVPYEVVDLSElpgeerRAALEARAAEAQASLDLTDGPILRVVQFRLgPGEPDRLLV 1192
Cdd:PRK12316 2656 LRTRFVEVGEQTRQVILPNMSlrIVLEDCAGVAD------AAIRQRVAEEIQRPFDLARGPLLRVRLLAL-DGQEHVLVI 2728

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1193 VVHHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLRRWGERLLATVDE-VVAAELPFWEALDG--QGVRPLPRG 1269
Cdd:PRK12316 2729 TQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSgEGARQLDYWRERLGgeQPVLELPLD 2808

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1270 CEPAEDREGDAQTVEVWLGGPETEALLgRVGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREELfpdiEVART 1349
Cdd:PRK12316 2809 RPRPALQSHRGARLDVALDVALSRELL-ALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA----ETERL 2883

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1350 VGWFTTIHPVVLPGRPQSA-GARLKAVKEAIRRVPKHgigygilrylgSDEVVTRLARLPAPEVAFNYLGRLDRALPKDG 1428
Cdd:PRK12316 2884 IGFFVNTQVLRAQVDAQLAfRDLLGQVKEQALGAQAH-----------QDLPFEQLVEALQPERSLSHSPLFQVMYNHQS 2952

                        1450      1460      1470      1480      1490      1500      1510
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242 1429 PFVMAPEAAGPSVSPRGKRSHALQTMVVAE----PQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAHA 1496
Cdd:PRK12316 2953 GERAAAQLPGLHIESFAWDGAATQFDLALDtwesAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENP 3024
PRK05691 PRK05691
peptide synthase; Validated
 4-1197 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 677.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK05691  675 ALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQR 754

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSswDEPTAAAWLQAEAAR------PFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADV 156
Cdd:PRK05691  755 IDLS--DLPEAEREARAAQIReeearqPFDLEKGPLlRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAC 832

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  157 EGRAATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldVSTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDR 236
Cdd:PRK05691  833 QGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGD--EQPVLELATDHPRSARQAHSAARYSLRVDASLSEA 910

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  237 VRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNA 316
Cdd:PRK05691  911 LRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQA 990

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  317 LRVTAKLQSVPLSRLAEQCRVPKSPGrmpLVQAVFQEIRSFNEAIR--PEGFGHMLRWSRGPLGFEVEVPSELGSQLDLe 394
Cdd:PRK05691  991 TLGAQAHQDLPFEQLVEALPQAREQG---LFQVMFNHQQRDLSALRrlPGLLAEELPWHSREAKFDLQLHSEEDRNGRL- 1066

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  395 vrcydffsssvRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRvLVEWNQTASDyPRERCL 474
Cdd:PRK05691 1067 -----------TLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCA-PAQAWL 1133

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  475 HHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDP 554
Cdd:PRK05691 1134 PELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDP 1213

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  555 AYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAV 634
Cdd:PRK05691 1214 DYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGN 1293

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  635 THRNVV-RLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP-ESPTPEEIGRVVREHGVTTLWLTAP 712
Cdd:PRK05691 1294 THAALAeRLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPgEHRDPQRIAELVQQYGVTTLHFVPP 1373

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  713 LFHAVADR-GLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTEnTTFTTCHDVSRGMGTGSVPIGKPIANT 791
Cdd:PRK05691 1374 LLQLFIDEpLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTE-TAINVTHWQCQAEDGERSPIGRPLGNV 1452

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  792 HVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQV 871
Cdd:PRK05691 1453 LCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPL-GEDGARLYRTGDRARWNADGALEYLGRLDQQV 1531

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  872 KIRGFRIELAEVEAALLQHPALREAVVIAREDRPGdKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLP 951
Cdd:PRK05691 1532 KLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMP 1610

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  952 LVPSGKLDRRALPAPTLSGRSgpFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGAREV-DLKLT 1030
Cdd:PRK05691 1611 LGPSGKLDRRALPEPVWQQRE--HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELP 1688

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1031 VRQIFTHPTLSSLAAAAQATAVSGE--DQGEIT-----GEMPLTPIQR--WFL-SGEPAAPhHFNQAVLLALRDAWVPKH 1100
Cdd:PRK05691 1689 LRALFEASELGAFAEQVARIQAAGErnSQGAIArvdrsQPVPLSYSQQrmWFLwQMEPDSP-AYNVGGMARLSGVLDVDR 1767

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1101 VDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSGGpVPYEVVDLSELPGEERRAALEARAAEAQ-ASLDLTDGPILRVVQ 1179
Cdd:PRK05691 1768 FEAALQALILRHETLRTTFPSVDGVPVQQVAEDSG-LRMDWQDFSALPADARQQRLQQLADSEAhQPFDLERGPLLRACL 1846

                        1210
                  ....*....|....*...
gi 260177242 1180 FRLGPGEpDRLLVVVHHL 1197
Cdd:PRK05691 1847 VKAAERE-HYFVLTLHHI 1863
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 477-963 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: 670.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:cd12117     2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 PSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDnvsAENLAYVMYTSGSTGKPKGVAVTH 636
Cdd:cd12117    82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVS---PDDLAYVMYTSGSTGRPKGVAVTH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  637 RNVVRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESP-TPEEIGRVVREHGVTTLWLTAPLFH 715
Cdd:cd12117   159 RGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAALFN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  716 AVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRG-MGTGSVPIGKPIANTHVY 794
Cdd:cd12117   239 QLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELdEVAGSIPIGRPIANTRVY 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  795 LLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIR 874
Cdd:cd12117   319 VLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG--PGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  875 GFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPrfSELRKFLLQRLPDHMIPAAVVALDKLPLVP 954
Cdd:cd12117   397 GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLTA 474


                  ....*....
gi 260177242  955 SGKLDRRAL 963
Cdd:cd12117   475 NGKVDRRAL 483
PRK12316 PRK12316
peptide synthase; Provisional
 6-1043 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 661.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    6 PLSEGQRSLWLAQELAGDvpvYTLPLVFRVTGpLSEAAIRRSMEAVLERRDALRL--VVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK12316 4107 PMQQGMLFHSLYEQEAGD---YINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSgfVWQGELGRPLQVVHKQVSLPFAE 4182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TD--GSSWDEPTAAAWLQAEAARPFDL-RAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAElcaadvEGRA 160
Cdd:PRK12316 4183 LDwrGRADLQAALDALAAAERERGFDLqRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLE------RYSG 4256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWhrdlLASDDASALVREWAAMVGDLDVSTPLdlpTDLPRRAQQR--YHVRQHFRDLGADLMDRVR 238
Cdd:PRK12316 4257 RPPAQPGGRYRDYIAW----LQRQDAAASEAFWREQLAALDEPTRL---AQAIARADLRsaNGYGEHVRELDATATARLR 4329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  239 ESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQ--LGVVGHMAGIVPVparidaAATPRAiirelrnA 316
Cdd:PRK12316 4330 EFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPgiEGQIGLFINTLPV------IATPRA-------Q 4396

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  317 LRVTAKLQSVPLSRLA--EQCRVP---KSPGRMPLVQAVFQEIRSFNEAIRPEgfgHMLRWSRGPLGF-EVEVPSELGSQ 390
Cdd:PRK12316 4397 QSVVEWLQQVQRQNLAlrEHEHTPlyeIQRWAGQGGEALFDSLLVFENYPVSE---ALQQGAPGGLRFgEVTNHEQTNYP 4473

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  391 LDLEVRCYDffssSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPR 470
Cdd:PRK12316 4474 LTLAVGLGE----TLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  471 ERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYV 550
Cdd:PRK12316 4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  551 PLDPAYPSERLAFLAHDAGVQIVLSAAGAEERL----GEGPWTVVRLDEDLGRPDErdaAPNDNVSAENLAYVMYTSGST 626
Cdd:PRK12316 4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpipdGLASLALDRDEDWEGFPAH---DPAVRLHPDNLAYVIYTSGST 4706

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  627 GKPKGVAVTHRNVV-RLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTPEEIGRVVREHGVT 705
Cdd:PRK12316 4707 GRPKGVAVSHGSLVnHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVT 4786

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  706 TLWLTAPLFHAVA--DRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGS-- 781
Cdd:PRK12316 4787 VLVFPPVYLQQLAehAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAay 4866

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  782 VPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsGVPGARLYRTGDLARYLPNGDM 861
Cdd:PRK12316 4867 MPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGGRLYRTGDLARYRADGVI 4945

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  862 EFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDrPGDKRLVAYVVGREAEVPRFSE--------LRKFLLQ 933
Cdd:PRK12316 4946 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYVVPQDPALADADEaqaelrdeLKAALRE 5024

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  934 RLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSI 1013
Cdd:PRK12316 5025 RLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSL 5104

                        1050      1060      1070
                  ....*....|....*....|....*....|.
gi 260177242 1014 LAIQVVAGAR-EVDLKLTVRQIFTHPTLSSL 1043
Cdd:PRK12316 5105 LAIQVTSRIQlELGLELPLRELFQTPTLAAF 5135
PRK12467 PRK12467
peptide synthase; Provisional
 6-1071 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 629.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    6 PLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGpLSEAAIRRSMEAVLERRDALR--LVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:PRK12467 2648 PLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRsgFLWDGELEEPLQVVYKQARLPFSR 2726

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSSWD--EPTAAAWLQAEAARPFDL-RAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRa 160
Cdd:PRK12467 2727 LDWRDRAdlEQALDALAAADRQQGFDLlSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQPPPA- 2805

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 atltPISRgFRDYLVWhrdlLASDDASALVREWAAMVGDLDVSTPLdLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRES 240
Cdd:PRK12467 2806 ----REGR-YRDYIAW----LQAQDAEASEAFWKEQLAALEEPTRL-ARALYPAPAEAVAGHGAHYLHLDATQTRQLIEF 2875

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  241 ARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRtwQL----GVVGHMAGIVPVPARIDAAATPRAIIRELRN- 315
Cdd:PRK12467 2876 ARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPA--QLrgaeQQLGLFINTLPVIASPRAEQTVSDWLQQVQAq 2953

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  316 --ALRvtaKLQSVPLsrlAEQCRVPKSPGrmplvQAVFQEIRSF-----NEAIRPEG-----FGHMLrwSRGPLGFEVEV 383
Cdd:PRK12467 2954 nlALR---EFEHTPL---ADIQRWAGQGG-----EALFDSILVFenypiSEALKQGApsglrFGAVS--SREQTNYPLTL 3020

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  384 PSELGSQLDLEvrcydffsssvrtcWRYDPDLFLPETVERWADYYAALLRELVGD----LGRLALQIdfipEPERRRVLV 459
Cdd:PRK12467 3021 AVGLGDTLELE--------------FSYDRQHFDAAAIERLAESFDRLLQAMLNNpaarLGELPTLA----AHERRQVLH 3082

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  460 EWNQTASDYPRERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGI 539
Cdd:PRK12467 3083 AWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVAL 3162

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  540 LGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAGAEERLGEgPWTVVRLDEDLGRPD-ERDAAPNDNVSAENLAY 618
Cdd:PRK12467 3163 LAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPA-PAGDTALTLDRLDLNgYSENNPSTRVMGENLAY 3241

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNVVRLVRGSSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTPEEIGR 697
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIAEAyELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQ 3321

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  698 VVREHGVTTLWLTAPLFHAVA-DRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTEnTTFTTCH---DV 773
Cdd:PRK12467 3322 AIHAHRISIACFPPAYLQQFAeDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTE-AVVTVTLwkcGG 3400

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  774 SRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGVpGARLYRTGDLA 853
Cdd:PRK12467 3401 DAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGS-GGRLYRTGDLA 3479

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  854 RYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAReDRPGDKRLVAYVVGREAEVPRFSELRKFLLQ 933
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAA 3558

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  934 RLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGrSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSI 1013
Cdd:PRK12467 3559 SLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKG-SREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSL 3637

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 1014 LAIQVVAGAREV-DLKLTVRQIFTHPTLSSLaaaaqatavSGEDQGEITGEMPLTPIQR 1071
Cdd:PRK12467 3638 LALQVLSRIRQSlGLKLSLRDLMSAPTIAEL---------AGYSPLGDVPVNLLLDLNR 3687
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 486-963 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: 594.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLsaagaeerlgegpwtvvrldedlgrpderdaapndnVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG 645
Cdd:cd05930    81 EDSGAKLVL------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 SSFAT-FGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPT-PEEIGRVVREHGVTTLWLTAPLFHA-VADRGL 722
Cdd:cd05930   125 MQEAYpLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdPEALADLLAEEGITVLHLTPSLLRLlLQELEL 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  723 DQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGM-GTGSVPIGKPIANTHVYLLDEQMN 801
Cdd:cd05930   205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDeEDGRVPIGRPIPNTRVYVLDENLR 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  802 PVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELA 881
Cdd:cd05930   285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF--GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  882 EVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRR 961
Cdd:cd05930   363 EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442


                  ..
gi 260177242  962 AL 963
Cdd:cd05930   443 AL 444
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 478-964 8.72e-166

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: 520.75  E-value: 8.72e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDeDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHR 637
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLD-QPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  638 NVVRLVRG-SSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPE-SPTPEEIGRVVREHGVTTLWLTAPLFH 715
Cdd:cd17651   160 SLANLVAWqARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvRTDPPALAAWLDEQRISRVFLPTVALR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  716 AVA---DRGLDQLRGVRQLLAGGDVLSPKHVARVLL-GLPALRLINGYGPTEnTTFTTCHDVSRGMGT--GSVPIGKPIA 789
Cdd:cd17651   240 ALAehgRPLGVRLAALRYLLTGGEQLVLTEDLREFCaGLPGLRLHNHYGPTE-THVVTALSLPGDPAAwpAPPPIGRPID 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  790 NTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDG 869
Cdd:cd17651   319 NTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF--VPGARMYRTGDLARWLPDGELEFLGRADD 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDK 949
Cdd:cd17651   397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDA 476

                         490
                  ....*....|....*
gi 260177242  950 LPLVPSGKLDRRALP 964
Cdd:cd17651   477 LPLTPNGKLDRRALP 491
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 473-964 3.31e-165

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: 517.76  E-value: 3.31e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  473 CLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPL 552
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  553 DPAYPSERLAFLAHDAGVQIVLSaagaeerlgegpwtvvrldedlgrpderdaapndnvSAENLAYVMYTSGSTGKPKGV 632
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLT------------------------------------QPENLAYVIYTSGSTGKPKGV 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  633 AVTHRNVVRLVRGSSFATF--GPDQVfLMMAPAAFDASTFEIWGALLHGARLVLFPPES-PTPEEIGRVVREHGVTTLWL 709
Cdd:cd17644   125 MIEHQSLVNLSHGLIKEYGitSSDRV-LQFASIAFDVAAEEIYVTLLSGATLVLRPEEMrSSLEDFVQYIQQWQLTVLSL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  710 TAPLFHAVADRGL----DQLRGVRQLLAGGDVLSPKHVAR-VLLGLPALRLINGYGPTENTTFTTCHDVS--RGMGTGSV 782
Cdd:cd17644   204 PPAYWHLLVLELLlstiDLPSSLRLVIVGGEAVQPELVRQwQKNVGNFIQLINVYGPTEATIAATVCRLTqlTERNITSV 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  783 PIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGVPGARLYRTGDLARYLPNGDME 862
Cdd:cd17644   284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGNIE 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  863 FLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPA 942
Cdd:cd17644   364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443

                         490       500
                  ....*....|....*....|..
gi 260177242  943 AVVALDKLPLVPSGKLDRRALP 964
Cdd:cd17644   444 AFVVLEELPLTPNGKIDRRALP 465
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 486-963 1.38e-164

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: 515.32  E-value: 1.38e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLsaagaeerlgegpwtvvrldedlgrpderdaapndnVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG 645
Cdd:cd17643    81 ADSGPSLLL------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 SSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPE-SPTPEEIGRVVREHGVTTLWLTAPLFHA---VADR 720
Cdd:cd17643   125 TQRWfGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEvARSPEDFARLLRDEGVTVLNQTPSAFYQlveAADR 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  721 GLDQLRGVRQLLAGGDVLSPKHVAR--VLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGS--VPIGKPIANTHVYLL 796
Cdd:cd17643   205 DGRDPLALRYVIFGGEALEAAMLRPwaGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAaaSPIGRPLPGLRVYVL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  797 DEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGF 876
Cdd:cd17643   285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGG-PGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  877 RIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSG 956
Cdd:cd17643   364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443


                  ....*..
gi 260177242  957 KLDRRAL 963
Cdd:cd17643   444 KLDRAAL 450
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 477-966 4.01e-164

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: 515.72  E-value: 4.01e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 PSERLAFLAHDAGVQIVLSAAGAEERL-GEGpwTVVRLDEDLGRPDERDAAPNDNvSAENLAYVMYTSGSTGKPKGVAVT 635
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIaFIG--LIDLLDEDTIYHEESENLEPVS-KSDDLAYVIYTSGSTGKPKGVMIE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  636 HRNVVRLVRGSSFATFGPDQV-FLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTP-EEIGRVVREHGVTTLWLTAPL 713
Cdd:cd17655   159 HRGVVNLVEWANKVIYQGEHLrVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDgQALTQYIRQNRITIIDLTPAH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVL-LGLPALRLINGYGPTENTTFTTCHDVSRGMG-TGSVPIGKPIANT 791
Cdd:cd17655   239 LKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIeLFGTNPTITNAYGPTETTVDASIYQYEPETDqQVSVPIGKPLGNT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  792 HVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQV 871
Cdd:cd17655   319 RIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF--VPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  872 KIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREaEVPrFSELRKFLLQRLPDHMIPAAVVALDKLP 951
Cdd:cd17655   397 KIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK-ELP-VAQLREFLARELPDYMIPSYFIKLDEIP 474

                         490
                  ....*....|....*
gi 260177242  952 LVPSGKLDRRALPAP 966
Cdd:cd17655   475 LTPNGKVDRKALPEP 489
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 475-963 1.77e-161

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: 508.35  E-value: 1.77e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  475 HHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDP 554
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  555 AYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDerDAAPNDNVSAENLAYVMYTSGSTGKPKGVAV 634
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPP--ATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  635 THRNVV-RLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPT-PEEIGRVVREHGVTTLWLTAP 712
Cdd:cd17646   159 THAGIVnRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRdPAYLAALIREHGVTTCHFVPS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  713 LFHA-VADRGLDQLRGVRQLLAGGDVLSPKHVARvLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSVPIGKPIANT 791
Cdd:cd17646   239 MLRVfLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  792 HVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQV 871
Cdd:cd17646   318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF--GPGSRMYRTGDLARWRPDGALEFLGRSDDQV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  872 KIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGR-EAEVPRFSELRKFLLQRLPDHMIPAAVVALDKL 950
Cdd:cd17646   396 KIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAaGAAGPDTAALRAHLAERLPEYMVPAAFVVLDAL 475

                         490
                  ....*....|...
gi 260177242  951 PLVPSGKLDRRAL 963
Cdd:cd17646   476 PLTANGKLDRAAL 488
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 499-898 4.43e-160

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: 501.03  E-value: 4.43e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   499 SYGELNRRADKLAHMLR-LKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAA 577
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   578 GAEERLGEGPWTVVRLDEDLGRPDER---DAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG-SSFATFGP 653
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDapaPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWlARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   654 DQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP--ESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLRGVRQL 731
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEdeERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   732 LAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGM--GTGSVPIGKPIANTHVYLLDEQMNPVPPNAVG 809
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDapRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   810 ELFTGGDGLARGYHERPDQTAERFVPDPFSGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQ 889
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 260177242   890 HPALREAVV 898
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 486-964 2.41e-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: 500.24  E-value: 2.41e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLSaagaeerlgegpwtvvrldedlgrpderdaapndnvSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG 645
Cdd:cd17652    81 ADARPALLLT------------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 SS-FATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTP-EEIGRVVREHGVTTLWLTAPLFHAVADRGLD 723
Cdd:cd17652   125 QIaAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgEPLADLLREHRITHVTLPPAALAALPPDDLP 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  724 QLRGvrqLLAGGDVLSPKHVARvllGLPALRLINGYGPTENTTFTTCHDVSRGMGTgsVPIGKPIANTHVYLLDEQMNPV 803
Cdd:cd17652   205 DLRT---LVVAGEACPAELVDR---WAPGRRMINAYGPTETTVCATMAGPLPGGGV--PPIGRPVPGTRVYVLDARLRPV 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  804 PPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEV 883
Cdd:cd17652   277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGA-PGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  884 EAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd17652   356 EAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435


                  .
gi 260177242  964 P 964
Cdd:cd17652   436 P 436
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1536-1954 4.59e-159

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: 498.65  E-value: 4.59e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1536 YPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPTER 1615
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1616 IDARSMAVDG-DAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQH 1694
Cdd:cd19543    82 LDLSHLSEAEqEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1695 EAAHRTAPRPHRDYVAWLRGADAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEHTTARLEQVLRERQ 1774
Cdd:cd19543   162 QPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1775 LTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAERTAY 1854
Cdd:cd19543   242 VTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREH 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1855 EHASLAQVQAWSEVPHgsALFESLIVVENYPVAPAF----SGDELSVRLVGGDEQTNYPVTLVALPGRRLTLRLLYEAER 1930
Cdd:cd19543   322 EYVPLYEIQAWSEGKQ--ALFDHLLVFENYPVDESLeeeqDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAEV 399

                         410       420
                  ....*....|....*....|....
gi 260177242 1931 IPDGAAEGVLSHLESLLCAIADDP 1954
Cdd:cd19543   400 FDEATIERLLGHLRRVLEQVAANP 423
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1-1043 2.92e-157

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 524.61  E-value: 2.92e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    1 MWTPLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSL-ADVSAV 79
Cdd:PRK10252    4 MSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVdPALTFP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   80 DFGVTDGSSWDEPTAAAWLQAEAARPFDLRAG---ALRVRAL-RRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAAD 155
Cdd:PRK10252   84 LPEIIDLRTQPDPHAAAQALMQADLQQDLRVDsgkPLVFHQLiQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  156 VEGRAATLTPISrGFRDYLVWHRDLLASDDASALVREWAAMVGDLDVSTPLDlPTDLPRRAQQryhVRQHFRDLGADLMD 235
Cdd:PRK10252  164 LRGEPTPASPFT-PFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLS-PAPLPGRSAS---ADILRLKLEFTDGA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  236 RVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRN 315
Cdd:PRK10252  239 FRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  316 ALRVTAKLQSVPlsrlAEQCR--VPKSPGRMPLVQAVFQeIRSFNEAIR---PEGFGHMLrwSRGPLG-FEVEVPSELGS 389
Cdd:PRK10252  319 QLKKMRRHQRYD----AEQIVrdSGRAAGDEPLFGPVLN-IKVFDYQLDfpgVQAQTHTL--ATGPVNdLELALFPDEHG 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  390 QLDLEVRCydffsssvrtcwryDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRvLVEWNQTASDYP 469
Cdd:PRK10252  392 GLSIEILA--------------NPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIP 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  470 rERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAY 549
Cdd:PRK10252  457 -ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  550 VPLDPAYPSERLAFLAHDAGVQIVLSAAGAEERLGEGP-WTVVRLDEDLGRPDERDAAPNdnvSAENLAYVMYTSGSTGK 628
Cdd:PRK10252  536 LPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPdLTSLCYNAPLAPQGAAPLQLS---QPHHTAYIIFTSGSTGR 612

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  629 PKGVAVTHRNVV-RLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPES-PTPEEIGRVVREHGVTT 706
Cdd:PRK10252  613 PKGVMVGQTAIVnRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAhRDPLAMQQFFAEYGVTT 692

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  707 L-----WLTAPLFHAVADRGLDQLRGVRQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTEN----TTFTTCHDVSRGM 777
Cdd:PRK10252  693 ThfvpsMLAAFVASLTPEGARQSCASLRQVFCSGEAL-PADLCREWQQLTGAPLHNLYGPTEAavdvSWYPAFGEELAAV 771

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  778 GTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLP 857
Cdd:PRK10252  772 RGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF--APGERMYRTGDVARWLD 849

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  858 NGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAR-----EDRPGD-KRLVAYVVGREAEVPRFSELRKFL 931
Cdd:PRK10252  850 DGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDaRQLVGYLVSQSGLPLDTSALQAQL 929

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  932 LQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGRSGPfVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGD 1011
Cdd:PRK10252  930 RERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPG-RAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGH 1008

                        1050      1060      1070
                  ....*....|....*....|....*....|...
gi 260177242 1012 SILAIQVVAG-AREVDLKLTVRQIFTHPTLSSL 1043
Cdd:PRK10252 1009 SLLAMKLAAQlSRQFARQVTPGQVMVASTVAKL 1041
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 486-963 1.20e-150

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: 476.78  E-value: 1.20e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLSAAGAEERLgegPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRg 645
Cdd:cd12116    81 EDAEPALVLTDDALPDRL---PAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 sSFA---TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPE-SPTPEEIGRVVREHGVTTLWLTAPLFHAVADRG 721
Cdd:cd12116   157 -SMRerlGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMLLDAG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  722 LDQLRGVRqLLAGGDVLSPKhVARVLLGLPAlRLINGYGPTENTTFTTCHDVSrgMGTGSVPIGKPIANTHVYLLDEQMN 801
Cdd:cd12116   236 WQGRAGLT-ALCGGEALPPD-LAARLLSRVG-SLWNLYGPTETTIWSTAARVT--AAAGPIPIGRPLANTQVYVLDAALR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  802 PVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELA 881
Cdd:cd12116   311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAG-PGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELG 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  882 EVEAALLQHPALREAVVIAREDRpGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRR 961
Cdd:cd12116   390 EIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468


                  ..
gi 260177242  962 AL 963
Cdd:cd12116   469 AL 470
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 474-963 2.30e-150

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: 474.88  E-value: 2.30e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 PAYPSERLAFLAHDAGVQIVLsaagaeerlgegpwtvvrldedlgrpderdaapndnVSAENLAYVMYTSGSTGKPKGVA 633
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVL------------------------------------TDPDDLAYVIYTSGSTGRPKGVA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  634 VTHRNVVRLVRGSSfATFGPDQVFLMMA--PAAFDASTFEIWGALLHGARLVL-----FPPESPTPEEIgrvvrehgvtT 706
Cdd:cd12115   125 IEHRNAAAFLQWAA-AAFSAEELAGVLAstSICFDLSVFELFGPLATGGKVVLadnvlALPDLPAAAEV----------T 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  707 LWLTAPlfhAVADRGLDQ---LRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGmGTGSVP 783
Cdd:cd12115   194 LINTVP---SAAAELLRHdalPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPG-ASGEVS 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  784 IGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEF 863
Cdd:cd12115   270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG--PGARLYRTGDLVRWRPDGLLEF 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  864 LGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAA 943
Cdd:cd12115   348 LGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSR 427

                         490       500
                  ....*....|....*....|
gi 260177242  944 VVALDKLPLVPSGKLDRRAL 963
Cdd:cd12115   428 FVRLDALPLTPNGKIDRSAL 447
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 486-964 1.59e-149

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: 472.62  E-value: 1.59e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLSAAGaeerlgegpwtvvrldedlgrpderdaapndnvsaENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG 645
Cdd:cd17649    81 EDSGAGLLLTHHP-----------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 SS-FATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPES-PTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLD 723
Cdd:cd17649   126 TAeRYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELwASADELAEMVRELGVTVLDLPPAYLQQLAEEADR 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  724 QLRG----VRQLLAGGDVLSPKHVARVLLGlpALRLINGYGPTENTTFTTCHDVSRGMGTG--SVPIGKPIANTHVYLLD 797
Cdd:cd17649   206 TGDGrppsLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWKCEAGAARAgaSMPIGRPLGGRSAYILD 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  798 EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFR 877
Cdd:cd17649   284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGA-PGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFR 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  878 IELAEVEAALLQHPALREAVVIAReDRPGDKRLVAYVVGREAEVPR--FSELRKFLLQRLPDHMIPAAVVALDKLPLVPS 955
Cdd:cd17649   363 IELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPelRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441


                  ....*....
gi 260177242  956 GKLDRRALP 964
Cdd:cd17649   442 GKLDRKALP 450
PRK12467 PRK12467
peptide synthase; Provisional
 1537-2433 1.27e-147

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 517.02  E-value: 1.27e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1537 PLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGvPEPLQVVRRLVRIPTERI 1616
Cdd:PRK12467   51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDE-EGFRQVIDASLSLTIPLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1617 DARSMA-VDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQ-H 1694
Cdd:PRK12467  130 DLANEQgRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQgR 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1695 EAAHRTAPRPHRDYVAWLRG-ADAQSVER---FWRRELGGFREVTPLGIDRP-PAGQrasSYR--RFERALDEHTTARLE 1767
Cdd:PRK12467  210 EPSLPALPIQYADYAIWQRSwLEAGERERqlaYWQEQLGGEHTVLELPTDRPrPAVP---SYRgaRLRVDLPQALSAGLK 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1768 QVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAplEGIERMVGLFINTVPMRAVVDPERPIGEWLtelqgR 1847
Cdd:PRK12467  287 ALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELL-----Q 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1848 RAERTAYEhaslaqVQAWSEVPhgsalFESLIVV----ENYPVAPAFSGDELSVRLVGGDEQTNYPvTLVAL------PG 1917
Cdd:PRK12467  360 QVKRTALG------AQAHQDLP-----FEQLVEAlqpeRSLSHSPLFQVMFNHQNTATGGRDREGA-QLPGLtveelsWA 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1918 RR-----LTL-----------RLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVVADWNDTAR 1981
Cdd:PRK12467  428 RHtaqfdLALdtyesaqglwaAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPAT 507

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1982 AYAReRCIHELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKT 2061
Cdd:PRK12467  508 EYAP-DCVHQLIEAQARQHPERPALVFGE-QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKA 585

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2062 GGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAArqlGIEHVVsLDGDGkdadgnvvihgrRALADLADGNL 2141
Cdd:PRK12467  586 GGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPA---GLRSLC-LDEPA------------DLLCGYSGHNP 649

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2142 PRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIAS 2221
Cdd:PRK12467  650 EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLP 729

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2222 EDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATE 2301
Cdd:PRK12467  730 PDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA-SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTE 808

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2302 ATVWSNYFEVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEP 2381
Cdd:PRK12467  809 TTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPF-GAD 887

                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242 2382 GARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:PRK12467  888 GGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVR 939
PRK12316 PRK12316
peptide synthase; Provisional
 1533-2431 2.41e-146

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 513.35  E-value: 2.41e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1533 DDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLwEGVPEPLQVVRRLVRIP 1612
Cdd:PRK12316   47 AERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFP-RGADDSLAQVPLDRPLE 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1613 TERIDARSMAvdgDAWIVERARDERRRG----FALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEvFKRY 1688
Cdd:PRK12316  126 VEFEDCSGLP---EAEQEARLRDEAQREslqpFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEE-FSRF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1689 SGGMQHEAAHRTAPRP--HRDYVAWLR-----GADAQSVErFWRRELGGFREVTPLGIDRP-PAGQrasSYR--RFERAL 1758
Cdd:PRK12316  202 YSAYATGAEPGLPALPiqYADYALWQRswleaGEQERQLE-YWRAQLGEEHPVLELPTDHPrPAVP---SYRgsRYEFSI 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1759 DEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAplEGIERMVGLFINTVPMRAVVDPERPIG 1838
Cdd:PRK12316  278 DPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVA 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1839 EWLTELQgrraertayEHASLAqvQAWSEVPHgSALFESLIVVENYPVAPAFS---------GDELSVRLVGG------- 1902
Cdd:PRK12316  356 TLLAGVK---------DTVLGA--QAHQDLPF-ERLVEALKVERSLSHSPLFQvmynhqplvADIEALDTVAGlefgqle 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1903 --DEQTNYPVTLVAL-PGRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVVADWNDT 1979
Cdd:PRK12316  424 wkSRTTQFDLTLDTYeKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNAT 503

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1980 ARAYARERCIHELFESSVERSPGSVALCYdGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGIL 2059
Cdd:PRK12316  504 AAEYPLQRGVHRLFEEQVERTPEAPALAF-GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAIL 582

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2060 KTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTdERHLGAVEIAARQLgieHVVSLDGDGKDADGNvvihgrraladlADG 2139
Cdd:PRK12316  583 KAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS-QSHLGRKLPLAAGV---QVLDLDRPAAWLEGY------------SEE 646

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2140 NLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHI 2219
Cdd:PRK12316  647 NPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVV 726

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2220 ASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPyFDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGA 2299
Cdd:PRK12316  727 AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGP 805

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2300 TEATVWSNYFEVdgIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSG 2379
Cdd:PRK12316  806 TEAAIDVTHWTC--VEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA 883

                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242 2380 epGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK12316  884 --GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 933
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 486-963 1.09e-139

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: 444.60  E-value: 1.09e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLsaagaeerlgegpwtvvrldedlgrpderdaapndnVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLV-- 643
Cdd:cd17650    81 EDSGAKLLL------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAha 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  644 --RGSSFATFGPDqvFLMMAPAAFDASTFEIWGALLHGARLVLFPPESP-TPEEIGRVVREHGVT----TLWLTAPLFHA 716
Cdd:cd17650   125 wrREYELDSFPVR--LLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKlDPAALYDLILKSRITlmesTPALIRPVMAY 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  717 VADRGLDqLRGVRQLLAGGDVLSPKH----VARVLLGLpalRLINGYGPTENTTFTTCHDVSRG--MGTGSVPIGKPIAN 790
Cdd:cd17650   203 VYRNGLD-LSAMRLLIVGSDGCKAQDfktlAARFGQGM---RIINSYGVTEATIDSTYYEEGRDplGDSANVPIGRPLPN 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  791 THVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQ 870
Cdd:cd17650   279 TAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--APGERMYRTGDLARWRADGNVELLGRVDHQ 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  871 VKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGreAEVPRFSELRKFLLQRLPDHMIPAAVVALDKL 950
Cdd:cd17650   357 VKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVA--AATLNTAELRAFLAKELPSYMIPSYYVQLDAL 434

                         490
                  ....*....|...
gi 260177242  951 PLVPSGKLDRRAL 963
Cdd:cd17650   435 PLTPNGKVDRRAL 447
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 2015-2431 1.34e-139

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: 442.47  E-value: 1.34e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2015 TYSDLNGRANRLGWLLRGL-GAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2094 RHLgaveIAARQLGIEHVVSLDGDGKDADgnvvihgrralADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:TIGR01733   81 ALA----SRLAGLVLPVILLDPLELAALD-----------DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSL 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2174 INLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGR-GTITFWDSAPAALQQ 2252
Cdd:TIGR01733  146 VNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAeHPVTVLNLTPSLLAL 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2253 LVPyfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDGIDPRWTS-IPYGRPIQNAR 2331
Cdd:TIGR01733  226 LAA--ALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTR 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2332 YYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSGEPGARLYRTGDLARFFRDGNIEFLGRADSQVK 2411
Cdd:TIGR01733  304 LYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVK 383

                          410       420
                   ....*....|....*....|
gi 260177242  2412 IRGYRIECGEVEVALAQHPG 2431
Cdd:TIGR01733  384 IRGYRIELGEIEAALLRHPG 403
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 2001-2434 5.26e-139

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: 443.64  E-value: 5.26e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:cd12114     1 PDATAVICGD-GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTTRPVCIVTDERHLGAVEIAARqlgiehvvsldgdgkdadgnvVIHGRRALADLADGNLPRAAGPHNMAYVIFTSGST 2160
Cdd:cd12114    80 LADAGARLVLTDGPDAQLDVAVFD---------------------VLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGST 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTI 2240
Cdd:cd12114   139 GTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGV 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 TFWDSAPAALQQLVPYF-DRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDGIDPRWT 2319
Cdd:cd12114   219 TLWNSVPALLEMLLDVLeAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWR 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2320 SIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPfsgePGARLYRTGDLARFFRDGN 2399
Cdd:cd12114   299 SIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP----DGERLYRTGDLGRYRPDGT 374

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 260177242 2400 IEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd12114   375 LEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVAR 409
PRK12316 PRK12316
peptide synthase; Provisional
 1401-2431 2.17e-138

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 487.93  E-value: 2.17e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1401 VTRLARLPapevaFNYLGRLDR-ALPKdgPFVMAPEAAG-PSVSPRGKRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEI 1478
Cdd:PRK12316 2479 WVVLERLP-----LNPNGKLDRkALPK--PDVSQLRQAYvAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLAT 2551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1479 aRLAARYGQLLEeLIAHAIDVGSEASWTPSDFPLARLEPHVLDALVDADRARPLddlyPLTPLQEGILFHALLEPGGSHY 1558
Cdd:PRK12316 2552 -QVVSRVRQDLG-LEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPL----PLSHAQQRQWFLWQLEPESAAY 2625

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1559 CVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGvPEPLQVVRRLVRIPTERIDARSMAvdgDAWIVERARDERR 1638
Cdd:PRK12316 2626 HLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVG-EQTRQVILPNMSLRIVLEDCAGVA---DAAIRQRVAEEIQ 2701

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1639 RGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQHEAAH-RTAPRPHRDYVAWLRGADA 1717
Cdd:PRK12316 2702 RPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTlPPLPLQYADYAAWQRAWMD 2781

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1718 QSVER----FWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYG 1793
Cdd:PRK12316 2782 SGEGArqldYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYS 2861

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1794 GRRDVVFGETVSGRSAPleGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAERTAYEHASLAQ----VQAWSEVP 1869
Cdd:PRK12316 2862 GQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQlveaLQPERSLS 2939

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1870 HgSALFESLIVVENYPVAPAFSG--DELSVRLVGGDEQTNYPVTLVALPgRRLTLRLLYEAERIPDGAAEGVLSHLESLL 1947
Cdd:PRK12316 2940 H-SPLFQVMYNHQSGERAAAQLPglHIESFAWDGAATQFDLALDTWESA-EGLGASLTYATDLFDARTVERLARHWQNLL 3017

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1948 CAIADDPDLPTGDLPLLSAHERRQVVADWNDTARAYARERCIHELFESSVERSPGSVALcYDGVPPLTYSDLNGRANRLG 2027
Cdd:PRK12316 3018 RGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVAL-AFGEQRLSYAELNRRANRLA 3096

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2028 WLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDErHLGAVEiaarqlg 2107
Cdd:PRK12316 3097 HRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-HLRLPL------- 3168

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2108 iehvvsldgdgkdADGNVVIHGRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVG 2187
Cdd:PRK12316 3169 -------------AQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLG 3235

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2188 PSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYfDRIEDGSQLR 2267
Cdd:PRK12316 3236 VGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEE-EDAHRCTSLK 3314

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2268 LAFLSGDWVPIgmlDELRRAFPNVKLVGLGGATEATVWSNYFEVdgIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVT 2347
Cdd:PRK12316 3315 RIVCGGEALPA---DLQQQVFAGLPLYNLYGPTEATITVTHWQC--VEEGKDAVPIGRPIANRACYILDGSLEPVPVGAL 3389

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2348 GDLYIGGTCVSFGYYADPSQTAERFVPDPFSgePGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALA 2427
Cdd:PRK12316 3390 GELYLGGEGLARGYHNRPGLTAERFVPDPFV--PGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLL 3467


                  ....
gi 260177242 2428 QHPG 2431
Cdd:PRK12316 3468 EHPW 3471
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 2001-2431 2.33e-136

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: 434.65  E-value: 2.33e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:cd05930     1 PDAVAVVDGDQS-LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTTRPVCIVTDerhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagPHNMAYVIFTSGST 2160
Cdd:cd05930    80 LEDSGAKLVLTD------------------------------------------------------PDDLAYVIYTSGST 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTI 2240
Cdd:cd05930   106 GKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGI 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 TFWDSAPAALQQLVPYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDGIDPRWTS 2320
Cdd:cd05930   186 TVLHLTPSLLRLLLQELEL-AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGR 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2321 IPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGARLYRTGDLARFFRDGNI 2400
Cdd:cd05930   265 VPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF--GPGERMYRTGDLVRWLPDGNL 342

                         410       420       430
                  ....*....|....*....|....*....|.
gi 260177242 2401 EFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05930   343 EFLGRIDDQVKIRGYRIELGEIEAALLAHPG 373
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 474-963 6.89e-130

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: 417.71  E-value: 6.89e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 PAYPSERLAFLAHDAGVQIVLSAagaeerlgegpwtvvrldedlgrpderdaapndnvSAENLAYVMYTSGSTGKPKGVA 633
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTS-----------------------------------SPSDAAYVIFTSGSTGKPKGVV 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  634 VTHRNVVRLVRGSSFAT-FGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLfPPESPTPEEIGRVVREHGVTTLWLTaP 712
Cdd:cd05918   126 IEHRALSTSALAHGRALgLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI-PSEEDRLNDLAGFINRLRVTWAFLT-P 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  713 lfhAVAdRGLD--QLRGVRQLLAGGDVLSPKHVA----RVllglpalRLINGYGPTENTTFTTCHDVSRGMGTGSvpIGK 786
Cdd:cd05918   204 ---SVA-RLLDpeDVPSLRTLVLGGEALTQSDVDtwadRV-------RLINAYGPAECTIAATVSPVVPSTDPRN--IGR 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  787 PI-ANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDP-----FSGVPGARLYRTGDLARYLPNGD 860
Cdd:cd05918   271 PLgATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqEGSGRGRRLYRTGDLVRYNPDGS 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  861 MEFLGRRDGQVKIRGFRIELAEVEAALLQH-PALREAVV--IAREDRPGDKRLVAYVVGREAE----------------- 920
Cdd:cd05918   351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVevVKPKDGSSSPQLVAFVVLDGSSsgsgdgdslflepsdef 430

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 260177242  921 VPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05918   431 RALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1063-1496 2.03e-129

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: 414.34  E-value: 2.03e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1063 EMPLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMW--RARGmPSGGPVPYE 1140
Cdd:cd19534     1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWqqRIRG-DVEELFRLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1141 VVDLSELPGEERRAALEARAAEaqaSLDLTDGPILRVVQFRlGPGEPDRLLVVVHHLAVDVVSWGILLADLATAHRQLVE 1220
Cdd:cd19534    80 VVDLSSLAQAAAIEALAAEAQS---SLDLEEGPLLAAALFD-GTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1221 GEIVRLPSKTtSLRRWGERLL-ATVDEVVAAELPFWEALDGQGVRPLPRGCEpaeDREGDAQTVEVWLGGPETEALLGRV 1299
Cdd:cd19534   156 GEPIPLPSKT-SFQTWAELLAeYAQSPALLEELAYWRELPAADYWGLPKDPE---QTYGDARTVSFTLDEEETEALLQEA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1300 GEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREELFPDIEVARTVGWFTTIHPVVLP-GRPQSAGARLKAVKEA 1378
Cdd:cd19534   232 NAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDlEASEDLGDTLKRVKEQ 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1379 IRRVPKHGIGYGILRYLgSDEVVTRLARLPAPEVAFNYLGRLDRALPKDGPFVMAPEAAGPSVSPRGKRSHALQ-TMVVA 1457
Cdd:cd19534   312 LRRIPNKGIGYGILRYL-TPEGTKRLAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDiNAVVE 390

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 260177242 1458 EPQgLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAHA 1496
Cdd:cd19534   391 GGQ-LVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 486-964 2.54e-128

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: 413.02  E-value: 2.54e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDerDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLV-- 643
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQED--TSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLhf 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  644 -RGSSFATFGPDqvFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTP-EEIGRVVREHGVTTLWLTAPLFHAVA-DR 720
Cdd:cd17656   160 eREKTNINFSDK--VLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDvEQLFDLVKRHNIEVVFLPVAFLKFIFsER 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  721 GL--DQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTChDVSRGMGTGSVP-IGKPIANTHVYLLD 797
Cdd:cd17656   238 EFinRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTY-TINPEAEIPELPpIGKPISNTWIYILD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  798 EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFR 877
Cdd:cd17656   317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFD--PNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  878 IELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGrEAEVPrFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGK 957
Cdd:cd17656   395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-EQELN-ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472


                  ....*..
gi 260177242  958 LDRRALP 964
Cdd:cd17656   473 VDRKALP 479
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 475-964 2.57e-127

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: 408.48  E-value: 2.57e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  475 HHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDP 554
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  555 AYPSERLAFLAHDAGVQIVLSaagaeerlgegpwtvvrldedlgrpderdaapndnvSAENLAYVMYTSGSTGKPKGVAV 634
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLT------------------------------------NPDDLAYVIYTSGSTGLPKGVMI 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  635 THRNVVRLVR-GSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTP-EEIGRVVREHGVTTLWLTAP 712
Cdd:cd17645   125 EHHNLVNLCEwHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDlDALNDYFNQEGITISFLPTG 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  713 L---FHAVADRGLdqlrgvRQLLAGGDVLspKHVARvllglPALRLINGYGPTENTTFTTCHDVSRGmgTGSVPIGKPIA 789
Cdd:cd17645   205 AaeqFMQLDNQSL------RVLLTGGDKL--KKIER-----KGYKLVNNYGPTENTVVATSFEIDKP--YANIPIGKPID 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  790 NTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDG 869
Cdd:cd17645   270 NTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF--VPGERMYRTGDLAKFLPDGNIEFLGRLDQ 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREaEVPrFSELRKFLLQRLPDHMIPAAVVALDK 949
Cdd:cd17645   348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE-EIP-HEELREWLKNDLPDYMIPTYFVHLKA 425

                         490
                  ....*....|....*
gi 260177242  950 LPLVPSGKLDRRALP 964
Cdd:cd17645   426 LPLTANGKVDRKALP 440
PRK05691 PRK05691
peptide synthase; Validated
 1531-2431 1.79e-125

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 445.77  E-value: 1.79e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1531 PLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLwEGVPEPLQVVRRLVR 1610
Cdd:PRK05691  671 PRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFY-ERDGVALQRIDAQGE 749

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1611 IPTERIDARSMAVDG-DAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYS 1689
Cdd:PRK05691  750 FALQRIDLSDLPEAErEARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYA 829

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1690 GGMQHEAAHrTAPRPHR--DYVAWLR----GADAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEHTT 1763
Cdd:PRK05691  830 AACQGQTAE-LAPLPLGyaDYGAWQRqwlaQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLS 908

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1764 ARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGetVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTe 1843
Cdd:PRK05691  909 EALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIG--VPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLA- 985

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1844 lQGRRAERTAyehaslaqvQAWSEVPhgsalFESLivVENYPVAPafsgdELSVRLVGGDEQTNYPVTLVALPGR----- 1918
Cdd:PRK05691  986 -QVRQATLGA---------QAHQDLP-----FEQL--VEALPQAR-----EQGLFQVMFNHQQRDLSALRRLPGLlaeel 1043

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1919 ---------------------RLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVvADWN 1977
Cdd:PRK05691 1044 pwhsreakfdlqlhseedrngRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQL-AQWG 1122

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1978 dTARAYARERCIHELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLG 2057
Cdd:PRK05691 1123 -QAPCAPAQAWLPELLNEQARQTPERIALVWDG-GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLA 1200

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2058 ILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEiaarqlgiehvvsldgdgkDADGNVVIhgrrALADLA 2137
Cdd:PRK05691 1201 ILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLP-------------------QAEGVSAI----ALDSLH 1257

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2138 DGNLP-RAAGPH----NMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLA 2212
Cdd:PRK05691 1258 LDSWPsQAPGLHlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLI 1337

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2213 AGGSIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEDGSqLRLAFLSGDWVPIGMLDELRRAFPNVK 2292
Cdd:PRK05691 1338 TGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTS-LRRLFSGGEALPAELRNRVLQRLPQVQ 1416

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2293 LVGLGGATEATVWSNYFEVDGIDPRWTsiPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERF 2372
Cdd:PRK05691 1417 LHNRYGPTETAINVTHWQCQAEDGERS--PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERF 1494

                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2373 VPDPFsGEPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK05691 1495 VPDPL-GEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG 1552
PRK05691 PRK05691
peptide synthase; Validated
 6-1043 1.82e-124

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 442.30  E-value: 1.82e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    6 PLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPD-NEGLVQSLADVSAVDFGVT 84
Cdd:PRK05691 3259 PLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNaGETMLQVIHKPGRTPIDYL 3338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   85 DGSSWDEPTAAAWLQAEAARP----FDL-RAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGR 159
Cdd:PRK05691 3339 DWRGLPEDGQEQRLQALHKQEreagFDLlNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGR 3418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  160 AATLTPISRgFRDYLVWhrdlLASDDASALVREWAAMVGDLDVSTPLdlPTDLPRRaqqryhvRQHFRDLGA-------- 231
Cdd:PRK05691 3419 EAQLPVPPR-YRDYIGW----LQRQDLAQARQWWQDNLRGFERPTPI--PSDRPFL-------REHAGDSGGmvvgdcyt 3484

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  232 --DLMD--RVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGR-------TRTwqlgvVGHMAGIVPVPARI 300
Cdd:PRK05691 3485 rlDAADgaRLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvsmpqmQRT-----VGLFINSIALRVQL 3559

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  301 DAAATPRAIIRELRNALRVTAKLQS---VPLSRLAEQCRVPKSP---------GRMPLVQAVFQEIRSFNeAIRPEGFGH 368
Cdd:PRK05691 3560 PAAGQRCSVRQWLQGLLDSNMELREyeyLPLVAIQECSELPKGQplfdslfvfENAPVEVSVLDRAQSLN-ASSDSGRTH 3638

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  369 MlrwsrgplGFEVEVPSELGSQLDLEVRcydffsssvrtcwrYDPDLFLPETVERWADYYAALLRELV----GDLGRLAL 444
Cdd:PRK05691 3639 T--------NFPLTAVCYPGDDLGLHLS--------------YDQRYFDAPTVERLLGEFKRLLLALVqgfhGDLSELPL 3696

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  445 qidfIPEPERRRVLVEWNQTASDYPRERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETR 524
Cdd:PRK05691 3697 ----LGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQP 3772

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  525 VGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQI-VLSAAGAE------ERLGEGPWTVVRLDEDL 597
Cdd:PRK05691 3773 VALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVlVCSAACREqarallDELGCANRPRLLVWEEV 3852

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  598 GRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV--RLVRGSSFATFGPDqVFLMMAPAAFDASTFEIWGA 675
Cdd:PRK05691 3853 QAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLnnQLSKVPYLALSEAD-VIAQTASQSFDISVWQFLAA 3931

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  676 LLHGARLVLFPPE-SPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALR 754
Cdd:PRK05691 3932 PLFGARVEIVPNAiAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQIG 4011

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  755 LINGYGPTENTTFTTCHDVSRGMGTGS-VPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERF 833
Cdd:PRK05691 4012 LVNAYGPAECSDDVAFFRVDLASTRGSyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAF 4091

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  834 VPDPFsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREdRPGDKRLVAY 913
Cdd:PRK05691 4092 VPHPF-GAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQE-GVNGKHLVGY 4169

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  914 VVGREAEV---PRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSG-RSGPFVAPEGHPEEVLARI 989
Cdd:PRK05691 4170 LVPHQTVLaqgALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQlQSQAYLAPRNELEQTLATI 4249

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  990 WERVLRVDAVGREDNFFELGGDSILAIQVVAGAREV-DLKLTVRQIFTHPTLSSL 1043
Cdd:PRK05691 4250 WADVLKVERVGVHDNFFELGGHSLLATQIASRVQKAlQRNVPLRAMFECSTVEEL 4304
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 486-963 3.82e-119

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: 386.63  E-value: 3.82e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDE---RDAAPNDnvsaenLAYVMYTSGSTGKPKGVAVTHRNVVRL 642
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPpppVDVAPDD------LAYVIFTSGSTGTPKGVMISHRAALNT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  643 VR--GSSFAtFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP-ESPTPEEIGRVVREHGVTtLWLTAP------L 713
Cdd:cd12114   155 ILdiNRRFA-VGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEaRRRDPAHWAELIERHGVT-LWNSVPallemlL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FHAVADRGLdqLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSR-GMGTGSVPIGKPIANTH 792
Cdd:cd12114   233 DVLEAAQAL--LPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEvPPDWRSIPYGRPLANQR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  793 VYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPfsgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVK 872
Cdd:cd12114   311 YRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP----DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  873 IRGFRIELAEVEAALLQHPALREAVVIAReDRPGDKRLVAYVVGREAEVPRFSE-LRKFLLQRLPDHMIPAAVVALDKLP 951
Cdd:cd12114   387 VRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIAPDaLRAFLAQTLPAYMIPSRVIALEALP 465

                         490
                  ....*....|..
gi 260177242  952 LVPSGKLDRRAL 963
Cdd:cd12114   466 LTANGKVDRAAL 477
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 486-964 1.11e-117

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: 381.36  E-value: 1.11e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVG-TETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFL 564
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  565 AHDAGVQIVLSaagaeerlgegpwtvvrldedlgrpderdaapndnvSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVR 644
Cdd:cd17648    81 LEDTGARVVIT------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  645 GSSFATFGP---DQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPE-SPTPEEIGRVVREHGVTTLWLTAPLFHAVADR 720
Cdd:cd17648   125 SLSERYFGRdngDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEmRFDPDRFYAYINREKVTYLSGTPSVLQQYDLA 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  721 GLDQLRgvrQLLAGGDVLSPKHVARVLLGLPAlRLINGYGPTENTTFTTCHDVSRGMGTGSvPIGKPIANTHVYLLDEQM 800
Cdd:cd17648   205 RLPHLK---RVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQRFDK-SLGRPVRNTKCYVLNDAM 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  801 NPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPF-------SGVPgARLYRTGDLARYLPNGDMEFLGRRDGQVKI 873
Cdd:cd17648   280 KRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqeraRGRN-ARLYKTGDLVRWLPSGELEYLGRNDFQVKI 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  874 RGFRIELAEVEAALLQHPALREAVVIARED-----RPGDKRLVAYVVGREAEVPRfSELRKFLLQRLPDHMIPAAVVALD 948
Cdd:cd17648   359 RGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLPEPGHVPE-SDLLSFLRAKLPRYMVPARLVRLE 437

                         490
                  ....*....|....*.
gi 260177242  949 KLPLVPSGKLDRRALP 964
Cdd:cd17648   438 GIPVTINGKLDVRALP 453
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1990-2431 1.41e-117

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: 382.39  E-value: 1.41e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1990 HELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLD 2069
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRT-LTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2070 PRWPLERVAAVLGTTRPVCIVTDERhlgaveiaarqlgiehvvslDGDGKDADGNVVIHGRRALADLADGNLPRAAGPHN 2149
Cdd:cd17646    80 PGYPADRLAYMLADAGPAVVLTTAD--------------------LAARLPAGGDVALLGDEALAAPPATPPLVPPRPDN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2150 MAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPE 2229
Cdd:cd17646   140 LAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPA 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLAAELGRGTITFWDSAPAALQQLVPYfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAfPNVKLVGLGGATEATVWSNYF 2309
Cdd:cd17646   220 YLAALIREHGVTTCHFVPSMLRVFLAE-PAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHW 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2310 EVDGIDPRwTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGARLYRTG 2389
Cdd:cd17646   298 PVRGPAET-PSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF--GPGSRMYRTG 374

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 260177242 2390 DLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17646   375 DLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPA 416
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1993-2431 6.26e-115

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: 375.14  E-value: 6.26e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1993 FESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRW 2072
Cdd:cd17651     1 FERQAARTPDAPALVAEGRR-LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2073 PLERVAAVLGTTRPVCIVTDERHLGaveiaaRQLGIEHVVSLDGDGKDADGnvvihgrraladlADGNLPRAAGPHNMAY 2152
Cdd:cd17651    80 PAERLAFMLADAGPVLVLTHPALAG------ELAVELVAVTLLDQPGAAAG-------------ADAEPDPALDADDLAY 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2153 VIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLA 2232
Cdd:cd17651   141 VIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALA 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2233 AELGRGTITFWDSAPAALQQLVPYFDRIEDGSQ-LRLAFLSGDWVPIG-MLDELRRAFPNVKLVGLGGATEATVWSNYfE 2310
Cdd:cd17651   221 AWLDEQRISRVFLPTVALRALAEHGRPLGVRLAaLRYLLTGGEQLVLTeDLREFCAGLPGLRLHNHYGPTETHVVTAL-S 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2311 VDGIDPRWTSIP-YGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSgePGARLYRTG 2389
Cdd:cd17651   300 LPGDPAAWPAPPpIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV--PGARMYRTG 377

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 260177242 2390 DLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17651   378 DLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPG 419
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1991-2431 9.10e-115

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: 374.23  E-value: 9.10e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP 2070
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRS-LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 RWPLERVAAVLGTTRPVCIVTDErhlgavEIAARQLGIEHVVSLDGDGKDADGnvvihgrraladladGNLPRAAGPHNM 2150
Cdd:cd12117    80 ELPAERLAFMLADAGAKVLLTDR------SLAGRAGGLEVAVVIDEALDAGPA---------------GNPAVPVSPDDL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 AYVIFTSGSTGTPKGVVERHSQVINLIEwvNRTYL-VGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPE 2229
Cdd:cd12117   139 AYVMYTSGSTGRPKGVAVTHRGVVRLVK--NTNYVtLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPD 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLAAELGRGTIT-FWDSApAALQQLVPyfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNY 2308
Cdd:cd12117   217 ALGALIAEEGVTvLWLTA-ALFNQLAD--EDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTS 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2309 FEVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGARLYRT 2388
Cdd:cd12117   294 HVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF--GPGERLYRT 371

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 260177242 2389 GDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd12117   372 GDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPG 414
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 482-963 2.51e-114

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: 371.58  E-value: 2.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLsaagaeerlgegpwtvvrldedlgrpderdAAPNDNvsaenlAYVMYTSGSTGKPKGVAVTHRNVVR 641
Cdd:cd05945    81 REILDAAKPALLI------------------------------ADGDDN------AYIIFTSGSTGRPKGVQISHDNLVS 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  642 LVRGS-SFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPE-SPTPEEIGRVVREHGVTTlWLTAPLFHAVA- 718
Cdd:cd05945   125 FTNWMlSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDaTADPKQLFRFLAEHGITV-WVSTPSFAAMCl 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  719 -DRGLDQ--LRGVRQLLAGGDVLsPKHVARVLLG-LPALRLINGYGPTENTTFTTCHDVSRGM--GTGSVPIGKPIANTH 792
Cdd:cd05945   204 lSPTFTPesLPSLRHFLFCGEVL-PHKTARALQQrFPDARIYNTYGPTEATVAVTYIEVTPEVldGYDRLPIGYAKPGAK 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  793 VYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPfsgvpGARLYRTGDLARYLPNGDMEFLGRRDGQVK 872
Cdd:cd05945   283 LVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-----GQRAYRTGDLVRLEADGLLFYRGRLDFQVK 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  873 IRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGRE-AEVPRFSELRKFLLQRLPDHMIPAAVVALDKLP 951
Cdd:cd05945   358 LNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgAEAGLTKAIKAELAERLPPYMIPRRFVYLDELP 437

                         490
                  ....*....|..
gi 260177242  952 LVPSGKLDRRAL 963
Cdd:cd05945   438 LNANGKIDRKAL 449
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1529-2435 3.70e-114

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 397.11  E-value: 3.70e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1529 ARPLDDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLwEGVPEPLQVVRRL 1608
Cdd:PRK10252    1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFT-EDNGEVWQWVDPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1609 VRIPT-ERIDARSMAvDGDAWIVERARDERRRGFALDAA-PAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFK 1686
Cdd:PRK10252   80 LTFPLpEIIDLRTQP-DPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1687 RYSGGMQHEAAhRTAPRPH-----RDYVAWLRGADAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEH 1761
Cdd:PRK10252  159 IYCAWLRGEPT-PASPFTPfadvvEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1762 TTARLEQVLRERQLTigTLIAGAWAILLERYGGRRDVVFGETVSGR--SAPLegieRMVGLFINTVPMRAVVDPERPIGE 1839
Cdd:PRK10252  238 AFRQLAAQASGVQRP--DLALALVALWLGRLCGRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLRVHIAAQETLPE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1840 WLTEL-----QGRRAERTAYEhaslaQVQAWSEVPHGS-ALFESLIVVENYPVAPAFSGDE-LSVRLVGGdeqtnyPVTL 1912
Cdd:PRK10252  312 LATRLaaqlkKMRRHQRYDAE-----QIVRDSGRAAGDePLFGPVLNIKVFDYQLDFPGVQaQTHTLATG------PVND 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1913 VALPGRR-----LTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQvVADWNDTARAYArER 1987
Cdd:PRK10252  381 LELALFPdehggLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIP-ET 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1988 CIHELFESSVERSPGSVALCYDGVpPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVP 2067
Cdd:PRK10252  459 TLSALVAQQAAKTPDAPALADARY-QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2068 LDPRWPLERVAAVLGTTRPVCIVTderhlgAVEIAARQLGIEHVVSLDGDGKDADgnvvihgrraladlADGNLPRAAGP 2147
Cdd:PRK10252  538 LDTGYPDDRLKMMLEDARPSLLIT------TADQLPRFADVPDLTSLCYNAPLAP--------------QGAAPLQLSQP 597

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2148 HNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRS 2227
Cdd:PRK10252  598 HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRD 677

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 PERLAAELGRGTIT---FWDSAPAA-LQQLVPYfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEAT 2303
Cdd:PRK10252  678 PLAMQQFFAEYGVTtthFVPSMLAAfVASLTPE-GARQSCASLRQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAA 755

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2304 V---WSNYFEVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSge 2380
Cdd:PRK10252  756 VdvsWYPAFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-- 833

                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260177242 2381 PGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQRG 2435
Cdd:PRK10252  834 PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQA 888
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1991-2430 7.61e-114

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: 372.05  E-value: 7.61e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP 2070
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFED-QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 RWPLERVAAVLGTTRPVCIVTDErhlgavEIAARQLGIEHVVSLDGDGkdadgnvVIHGRRAladladgNLPRAAGPHNM 2150
Cdd:cd17655    80 DYPEERIQYILEDSGADILLTQS------HLQPPIAFIGLIDLLDEDT-------IYHEESE-------NLEPVSKSDDL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 AYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPER 2230
Cdd:cd17655   140 AYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQA 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2231 LAAELGRGTITFWDSAPAALQQLVPyfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAF-PNVKLVGLGGATEATVWSNYF 2309
Cdd:cd17655   220 LTQYIRQNRITIIDLTPAHLKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIY 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2310 EVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGARLYRTG 2389
Cdd:cd17655   298 QYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF--VPGERMYRTG 375

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 260177242 2390 DLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd17655   376 DLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP 416
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 2001-2434 2.74e-107

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: 351.98  E-value: 2.74e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:cd12116     1 PDATAVRDDDRS-LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTTRPVCIVTDErhlgavEIAARQLGIEHVVSLDGDGkdadgnvvihgrralADLADGNLPRAAGPHNMAYVIFTSGST 2160
Cdd:cd12116    80 LEDAEPALVLTDD------ALPDRLPAGLPVLLLALAA---------------AAAAPAAPRTPVSPDDLAYVIYTSGST 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTI 2240
Cdd:cd12116   139 GRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSI 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 TFWDSAPAALQQLVpyfdrieDGSQLRLAFLS----GDWVPIGMLDELrrAFPNVKLVGLGGATEATVWSNYFEVDGIDP 2316
Cdd:cd12116   219 TVMQATPATWRMLL-------DAGWQGRAGLTalcgGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAARVTAAAG 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2317 rwtSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEPGARLYRTGDLARFFR 2396
Cdd:cd12116   290 ---PIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-AGPGSRLYRTGDLVRRRA 365

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 260177242 2397 DGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd12116   366 DGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQ 403
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 476-963 1.20e-106

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: 348.92  E-value: 1.20e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  476 HLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPA 555
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  556 YPSERLAFLAHDAGVQIVLSAAgaeerlgegpwtvvrldedlgrpderdaAPNDnvsaenLAYVMYTSGSTGKPKGVAVT 635
Cdd:cd17653    81 LPSARIQAILRTSGATLLLTTD----------------------------SPDD------LAYIIFTSGSTGIPKGVMVP 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  636 HRNVVRLVRGSSFATF-GPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPtpeeIGRVVREhgVTTLWLTAPLF 714
Cdd:cd17653   127 HRGVLNYVSQPPARLDvGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDP----FAHVART--VDALMSTPSIL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  715 HAVADRGLDQLRGVrqlLAGGDVLSPKHVARVLLGLpalRLINGYGPTEnttfTTCHDVSRGMGTGS-VPIGKPIANTHV 793
Cdd:cd17653   201 STLSPQDFPNLKTI---FLGGEAVPPSLLDRWSPGR---RLYNAYGPTE----CTISSTMTELLPGQpVTIGKPIPNSTC 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  794 YLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKI 873
Cdd:cd17653   271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF--WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKV 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  874 RGFRIELAEVEA-ALLQHPALREAVVIAREDrpgdkRLVAYVVGREAEVPRfseLRKFLLQRLPDHMIPAAVVALDKLPL 952
Cdd:cd17653   349 RGFRINLEEIEEvVLQSQPEVTQAAAIVVNG-----RLVAFVTPETVDVDG---LRSELAKHLPSYAVPDRIIALDSFPL 420

                         490
                  ....*....|.
gi 260177242  953 VPSGKLDRRAL 963
Cdd:cd17653   421 TANGKVDRKAL 431
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 474-971 1.40e-105

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: 346.41  E-value: 1.40e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 PAYPSERLAFLAHDAGVQIVLSAagaeerlgegpwtvvrldedlgrpderdaapndnvsaenlaYVMYTSGSTGKPKGVA 633
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVTA-----------------------------------------LILYTSGTTGRPKGVM 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  634 VTHRNVVRLVRGSSFAT-FGPDQVFLMMAPAAFDAS-TFEIWGALLHGARLVLFPpeSPTPEEIGRVVREHGVTTLWLTA 711
Cdd:COG0318   120 LTHRNLLANAAAIAAALgLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLP--RFDPERVLELIERERVTVLFGVP 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  712 PLFHAVADRGLDQ---LRGVRQLLAGGDVLSPKHVARV--LLGLpalRLINGYGPTENTTFTTCHDVSRGmGTGSVPIGK 786
Cdd:COG0318   198 TMLARLLRHPEFArydLSSLRLVVSGGAPLPPELLERFeeRFGV---RIVEGYGLTETSPVVTVNPEDPG-ERRPGSVGR 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  787 PIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFvPDPFsgvpgarlYRTGDLARYLPNGDMEFLGR 866
Cdd:COG0318   274 PLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW--------LRTGDLGRLDEDGYLYIVGR 344

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  867 RDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVA 946
Cdd:COG0318   345 KKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEF 424

                         490       500
                  ....*....|....*....|....*
gi 260177242  947 LDKLPLVPSGKLDRRALPAPTLSGR 971
Cdd:COG0318   425 VDELPRTASGKIDRRALRERYAAGA 449
AMP-binding pfam00501
AMP-binding enzyme;
478-874 4.07e-104

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 340.83  E-value: 4.07e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   478 FEEEARRVPDAVALDAGSNV-VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   557 PSERLAFLAHDAGVQIVL--------SAAGAEERLGEGPWTVV---------RLDEDLGRPDERDAAPNDNVSAENLAYV 619
Cdd:pfam00501   81 PAEELAYILEDSGAKVLItddalkleELLEALGKLEVVKLVLVldrdpvlkeEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   620 MYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-----FGPDQVFLMMAPAAFDAS-TFEIWGALLHGARLVLFPPESPT-P 692
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfgLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALdP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   693 EEIGRVVREHGVTTLWLTAPLFHAVAD---RGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPAlRLINGYGPTENTTFTT 769
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagaPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   770 CHDVSRGMGTGSVPIGKPIANTHVYLLDEQ-MNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDpfsgvpgaRLYR 848
Cdd:pfam00501  320 TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED--------GWYR 391

                          410       420
                   ....*....|....*....|....*.
gi 260177242   849 TGDLARYLPNGDMEFLGRRDGQVKIR 874
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1989-2431 1.11e-103

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: 340.83  E-value: 1.11e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVAL-CYDGvpPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVP 2067
Cdd:cd12115     1 LHDLVEAQAARTPDAIALvCGDE--SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2068 LDPRWPLERVAAVLGTTRPVCIVTDerhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagP 2147
Cdd:cd12115    79 LDPAYPPERLRFILEDAQARLVLTD------------------------------------------------------P 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2148 HNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYlvgPSDRL---LFVTSPSFDLSVYDVFGMLAAGGSIHIAseDD 2224
Cdd:cd12115   105 DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAF---SAEELagvLASTSICFDLSVFELFGPLATGGKVVLA--DN 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2225 LRSPERLAAelgRGTITFWDSAPAALQQLVpyfdRIED-GSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEAT 2303
Cdd:cd12115   180 VLALPDLPA---AAEVTLINTVPSAAAELL----RHDAlPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDT 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2304 VWSNYFEVDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGA 2383
Cdd:cd12115   253 TYSTVAPVPPGASGEVSI--GRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--GPGA 328

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 260177242 2384 RLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd12115   329 RLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPG 376
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 2001-2431 2.82e-101

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: 333.89  E-value: 2.82e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:cd17643     1 PEAVAVVDED-RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTTRPVCIVTDerhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagPHNMAYVIFTSGST 2160
Cdd:cd17643    80 LADSGPSLLLTD------------------------------------------------------PDDLAYVIYTSGST 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTI 2240
Cdd:cd17643   106 GRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 TFWDSAPAALQQLVPYFDR-IEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVK--LVGLGGATEATVWSNYFEVDGID-P 2316
Cdd:cd17643   186 TVLNQTPSAFYQLVEAADRdGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTVHVTFRPLDAADlP 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2317 RWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEPGARLYRTGDLARFFR 2396
Cdd:cd17643   266 AAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-GGPGSRMYRTGDLARRLP 344

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 260177242 2397 DGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17643   345 DGELEYLGRADEQVKIRGFRIELGEIEAALATHPS 379
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 2001-2434 8.30e-101

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: 332.30  E-value: 8.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:cd17652     1 PDAPAVVFGDET-LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTTRPVCIVTDerhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagPHNMAYVIFTSGST 2160
Cdd:cd17652    80 LADARPALLLTT------------------------------------------------------PDNLAYVIYTSGST 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTI 2240
Cdd:cd17652   106 GRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRI 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 TFWDSAPAALQQLVPyfdriEDGSQLRLAFLSGDWVPIGMLdelRRAFPNVKLVGLGGATEATVWSNYFEVDGIDprwTS 2320
Cdd:cd17652   186 THVTLPPAALAALPP-----DDLPDLRTLVVAGEACPAELV---DRWAPGRRMINAYGPTETTVCATMAGPLPGG---GV 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2321 IPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEPGARLYRTGDLARFFRDGNI 2400
Cdd:cd17652   255 PPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPF-GAPGSRMYRTGDLARWRADGQL 333

                         410       420       430
                  ....*....|....*....|....*....|....
gi 260177242 2401 EFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd17652   334 EFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE 367
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1988-2430 2.11e-100

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: 332.09  E-value: 2.11e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1988 CIHELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVP 2067
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFED-QQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2068 LDPRWPLERVAAVLGTTRPVCIVTDerhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagP 2147
Cdd:cd17644    80 LDPNYPQERLTYILEDAQISVLLTQ------------------------------------------------------P 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2148 HNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRS 2227
Cdd:cd17644   106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSS 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 PERLAAELGRGTITFWDSAPAALQQLVPYF--DRIEDGSQLRLAFLSGDWVPIGMLDELRRAF-PNVKLVGLGGATEATV 2304
Cdd:cd17644   186 LEDFVQYIQQWQLTVLSLPPAYWHLLVLELllSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEATI 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2305 WSNYFEVDGIDPRW-TSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSGEPGA 2383
Cdd:cd17644   266 AATVCRLTQLTERNiTSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESE 345

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 260177242 2384 RLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd17644   346 RLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHN 392
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 2001-2431 1.67e-98

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: 325.86  E-value: 1.67e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:cd17649     1 PDAVALVFGDQS-LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LgttrpvcivtderhlgaveiaarqlgiehvvsldgdgKDADGNVVIhgrraladladgnlprAAGPHNMAYVIFTSGST 2160
Cdd:cd17649    80 L-------------------------------------EDSGAGLLL----------------THHPRQLAYVIYTSGST 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTI 2240
Cdd:cd17649   107 GTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGV 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 TFWDSAPAALQQLVPYFDRIEDGSQ--LRLAFLSGDWVPIgmlDELRRAFPN-VKLVGLGGATEATVWSNYFEVDGIDPR 2317
Cdd:cd17649   187 TVLDLPPAYLQQLAEEADRTGDGRPpsLRLYIFGGEALSP---ELLRRWLKApVRLFNAYGPTEATVTPLVWKCEAGAAR 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2318 -WTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsGEPGARLYRTGDLARFFR 2396
Cdd:cd17649   264 aGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF-GAPGSRLYRTGDLARWRD 342

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 260177242 2397 DGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17649   343 DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
AMP-binding pfam00501
AMP-binding enzyme;
1993-2413 1.44e-92

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 307.70  E-value: 1.44e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1993 FESSVERSPGSVALCYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRW 2072
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2073 PLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLG--IEHVVSLDGDGKDADGNVVIHGRRALADLADgnlPRAAGPHNM 2150
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLevVKLVLVLDRDPVLKEEPLPEEAKPADVPPPP---PPPPDPDDL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2151 AYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYL----VGPSDRLLFVTSPSFDLSV-YDVFGMLAAGGSIHIASEDDL 2225
Cdd:pfam00501  158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2226 RSPERLAAELGRGTITFWDSAPAALQQLV--PYFDRIEDGSqLRLAFLSGDWVPIGMLDELRRAFPNVkLVGLGGATEAT 2303
Cdd:pfam00501  238 LDPAALLELIERYKVTVLYGVPTLLNMLLeaGAPKRALLSS-LRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2304 VWSNYfeVDGIDPRWTSIP-YGRPIQNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDpfsgep 2381
Cdd:pfam00501  316 GVVTT--PLPLDEDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------ 387

                          410       420       430
                   ....*....|....*....|....*....|..
gi 260177242  2382 gaRLYRTGDLARFFRDGNIEFLGRADSQVKIR 2413
Cdd:pfam00501  388 --GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 2014-2431 1.48e-89

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: 300.15  E-value: 1.48e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDe 2093
Cdd:cd17650    13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagPHNMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd17650    92 -----------------------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNV 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLI-EWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQ 2252
Cdd:cd17650   119 AHAAhAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRP 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2253 LVPYFDRIE-DGSQLRLAFLSGDWVPIG-MLDELRRAFPNVKLVGLGGATEATVWSNYFEVD-GIDPRWTSIPYGRPIQN 2329
Cdd:cd17650   199 VMAYVYRNGlDLSAMRLLIVGSDGCKAQdFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGrDPLGDSANVPIGRPLPN 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2330 ARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGARLYRTGDLARFFRDGNIEFLGRADSQ 2409
Cdd:cd17650   279 TAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--APGERMYRTGDLARWRADGNVELLGRVDHQ 356

                         410       420
                  ....*....|....*....|..
gi 260177242 2410 VKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17650   357 VKIRGFRIELGEIESQLARHPA 378
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1990-2430 3.88e-88

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: 295.62  E-value: 3.88e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1990 HELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLD 2069
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRG-QSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2070 PRWPLERVAAVLGTTRPVCIVTDerhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagPHN 2149
Cdd:cd17645    80 PDYPGERIAYMLADSSAKILLTN------------------------------------------------------PDD 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2150 MAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPE 2229
Cdd:cd17645   106 LAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLD 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLA--AELGRGTITFWDSaPAALQqlvpyFDRIEDGSqLRLAFLSGDwvpigmldELRRAFPN-VKLVGLGGATEATVWS 2306
Cdd:cd17645   186 ALNdyFNQEGITISFLPT-GAAEQ-----FMQLDNQS-LRVLLTGGD--------KLKKIERKgYKLVNNYGPTENTVVA 250

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2307 NYFEvdgIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSgePGARLY 2386
Cdd:cd17645   251 TSFE---IDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV--PGERMY 325

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 260177242 2387 RTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd17645   326 RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHP 369
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1997-2433 9.40e-86

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: 289.15  E-value: 9.40e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1997 VERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLER 2076
Cdd:cd05945     1 AAANPDRPAVVEGGRT-LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2077 VAAVLGTTRPVCIVTDerhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagPHNMAYVIFT 2156
Cdd:cd05945    80 IREILDAAKPALLIAD------------------------------------------------------GDDNAYIIFT 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2157 SGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELG 2236
Cdd:cd05945   106 SGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLA 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2237 RGTITFWDSAPAALQQLV--PYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDGI 2314
Cdd:cd05945   186 EHGITVWVSTPSFAAMCLlsPTFTP-ESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPE 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2315 DP-RWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDpfsgePGARLYRTGDLAR 2393
Cdd:cd05945   265 VLdGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD-----EGQRAYRTGDLVR 339

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 260177242 2394 FFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:cd05945   340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVK 379
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1534-1973 6.59e-85

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: 286.92  E-value: 6.59e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1534 DLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPT 1613
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFEL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1614 ERIDARSM-AVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGM 1692
Cdd:pfam00668   83 EIIDISDLsESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1693 QHEAAHRTAPRPHRDYVAWLR----GADAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEHTTARLEQ 1768
Cdd:pfam00668  163 KGEPLPLPPKTPYKDYAEWLQqylqSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRK 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1769 VLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRsaPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQgrR 1848
Cdd:pfam00668  243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR--PSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQ--E 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1849 AERTAYEHAS--LAQVQAWSEVPH---GSALFESLIVVENYPV------APAFSGDELSVRLVgGDEQTNYPVTLVALP- 1916
Cdd:pfam00668  319 DLLSAEPHQGypFGDLVNDLRLPRdlsRHPLFDPMFSFQNYLGqdsqeeEFQLSELDLSVSSV-IEEEAKYDLSLTASEr 397

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  1917 GRRLTLRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVV 1973
Cdd:pfam00668  398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1991-2435 2.16e-84

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: 284.59  E-value: 2.16e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP 2070
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGS-LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 RWPLERVAAVLGTTRPVCIVTderhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlprAAGPHNM 2150
Cdd:cd17653    80 KLPSARIQAILRTSGATLLLT----------------------------------------------------TDSPDDL 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 AYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHiaseddLRSPER 2230
Cdd:cd17653   108 AYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLV------LADPSD 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2231 LAAELGRgTITFWDSAPAALQQLVPyfdriEDGSQLRLAFLSGDWVPIGMLDELRrafPNVKLVGLGGATEATVWSNYFE 2310
Cdd:cd17653   182 PFAHVAR-TVDALMSTPSILSTLSP-----QDFPNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTECTISSTMTE 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2311 VDGIDPrwtsIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGARLYRTGD 2390
Cdd:cd17653   253 LLPGQP----VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF--WPGSRMYRTGD 326

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 260177242 2391 LARFFRDGNIEFLGRADSQVKIRGYRIECGEVE-VALAQHPGAQRG 2435
Cdd:cd17653   327 YGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEeVVLQSQPEVTQA 372
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 2000-2433 7.46e-82

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: 278.97  E-value: 7.46e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2000 SPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAA 2079
Cdd:cd17656     1 TPDAVAVVFEN-QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2080 VLGTTRPVCIVTDERHLGAVEiaarQLGIEHVVSLDGDGKDADGNVvihgrralaDLADGNlpraagpHNMAYVIFTSGS 2159
Cdd:cd17656    80 IMLDSGVRVVLTQRHLKSKLS----FNKSTILLEDPSISQEDTSNI---------DYINNS-------DDLLYIIYTSGT 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2160 TGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGT 2239
Cdd:cd17656   140 TGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHN 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2240 I-------TFWDSApAALQQLVPYFDR-----IEDGSQLRlaflsgdwvpigMLDELRRAF--PNVKLVGLGGATEATVW 2305
Cdd:cd17656   220 IevvflpvAFLKFI-FSEREFINRFPTcvkhiITAGEQLV------------ITNEFKEMLheHNVHLHNHYGPSETHVV 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2306 SNYfEVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgEPGARL 2385
Cdd:cd17656   287 TTY-TINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF--DPNERM 363

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 260177242 2386 YRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:cd17656   364 YRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVS 411
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1989-2434 1.42e-81

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: 278.27  E-value: 1.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALC-YDGvpPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVP 2067
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCaWDG--SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2068 LDPRWPLERVAAVLGTTRPVCIVTDErhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagP 2147
Cdd:cd05918    79 LDPSHPLQRLQEILQDTGAKVVLTSS-----------------------------------------------------P 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2148 HNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRs 2227
Cdd:cd05918   106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRL- 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 pERLAAELGRGTITFWDSAPAALQQLVPyfdriEDGSQLRLAFLSGDWVPIGMLDELRrafPNVKLVGLGGATEATVWSN 2307
Cdd:cd05918   185 -NDLAGFINRLRVTWAFLTPSVARLLDP-----EDVPSLRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAECTIAAT 255

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2308 YFEV-DGIDPRwtSIpyGRPIqNARYYVLDRSGN--PCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDP-----FSG 2379
Cdd:cd05918   256 VSPVvPSTDPR--NI--GRPL-GATCWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqEGS 330

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260177242 2380 EPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd05918   331 GRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAK 385
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1535-1927 9.05e-78

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: 265.33  E-value: 9.05e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1535 LYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPTE 1614
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1615 RIDARSMAVDGDAWIVERA-RDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQ 1693
Cdd:cd19547    81 LLDWSGEDPDRRAELLERLlADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1694 HEAAHRTAPRPHRDYVAWLRGADAQS--VERFWRRELggfREVTPLGIDRPPAgQRASSYRRFERALDEHTTARLEQVLR 1771
Cdd:cd19547   161 GREPQLSPCRPYRDYVRWIRARTAQSeeSERFWREYL---RDLTPSPFSTAPA-DREGEFDTVVHEFPEQLTRLVNEAAR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1772 ERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAER 1851
Cdd:cd19547   237 GYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1852 TAYEHASLAQVQAWS--EVPHGSALFESLIVVENYPvAPAFSGDELSVRLVG--GDEQTNYPVTLVALPGRRLTLRLLYE 1927
Cdd:cd19547   317 AAHGHVPLAQIKSWAsgERLSGGRVFDNLVAFENYP-EDNLPGDDLSIQIIDlhAQEKTEYPIGLIVLPLQKLAFHFNYD 395
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 4-438 7.59e-77

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: 262.68  E-value: 7.59e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSSWDEPTAAAWLQAE----AARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEG 158
Cdd:cd19531    81 VDLSGLPEAEREAEAQRLareeARRPFDLARGPLlRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  159 RAATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDldVSTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVR 238
Cdd:cd19531   161 RPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAG--APPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  239 ESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTwQL-GVVGHMAGIVPVPARIDAAATPRAIIRELRNAL 317
Cdd:cd19531   239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRA-ELeGLIGFFVNTLVLRTDLSGDPTFRELLARVRETA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  318 rvtakL-----QSVPLSRLAEQCRVPKSPGRMPLVQAVFqeirSFNEAIRPEgfghmlrWSRGPLGFEVEVPSELGSQLD 392
Cdd:cd19531   318 -----LeayahQDLPFEKLVEALQPERDLSRSPLFQVMF----VLQNAPAAA-------LELPGLTVEPLEVDSGTAKFD 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 260177242  393 LEVRCYDfFSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19531   382 LTLSLTE-TDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVAD 426
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1535-1954 1.62e-76

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: 261.23  E-value: 1.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1535 LYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPTE 1614
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1615 RIDARSMAvDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSH-RLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQ 1693
Cdd:cd19536    81 ELDLTPLE-EQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQLLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1694 HEAAHRTAPRPHRDYVAWLRGADAQS-VERFWRRELGGFREVTplgidrPPAGQRAS---SYRRFERALDEHTTARLEQV 1769
Cdd:cd19536   160 YKPLSLPPAQPYRDFVAHERASIQQAaSERYWREYLAGATLAT------LPALSEAVgggPEQDSELLVSVPLPVRSRSL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1770 LRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFINTVPMRaVVDPERPIGEWLTELQGRRA 1849
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLR-VTLSEETVEDLLKRAQEQEL 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1850 ERTAYEHASLAQVQAWSEvphGSALFESLIVVENYPV---APAFSGDELSVR-LVGGDEQTNYPVTLVALP-GRRLTLRL 1924
Cdd:cd19536   313 ESLSHEQVPLADIQRCSE---GEPLFDSIVNFRHFDLdfgLPEWGSDEGMRRgLLFSEFKSNYDVNLSVLPkQDRLELKL 389

                         410       420       430
                  ....*....|....*....|....*....|
gi 260177242 1925 LYEAERIPDGAAEGVLSHLESLLCAIADDP 1954
Cdd:cd19536   390 AYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 2001-2434 1.78e-75

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: 259.64  E-value: 1.78e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYdGVPPLTYSDLNGRANRLGWLLRGLGAG-PEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAA 2079
Cdd:cd17648     1 PDRVAVVY-GDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2080 VLGTTrpvcivtderhlgaveiAARqlgiehvvsldgdgkdadgnVVIhgrraladladgnlpraAGPHNMAYVIFTSGS 2159
Cdd:cd17648    80 ILEDT-----------------GAR--------------------VVI-----------------TNSTDLAYAIYTSGT 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2160 TGTPKGVVERHSQVINLIEWVNRTY-LVGPSD-RLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGR 2237
Cdd:cd17648   106 TGKPKGVLVEHGSVVNLRTSLSERYfGRDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINR 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2238 GTITFWDSAPAALQQLvpYFDRIedgSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGgATEATVWSNYFEVDGIDPR 2317
Cdd:cd17648   186 EKVTYLSGTPSVLQQY--DLARL---PHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYG-PTETTVTNHKRFFPGDQRF 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2318 WTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPF-------SGEPgARLYRTGD 2390
Cdd:cd17648   260 DKSL--GRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqeraRGRN-ARLYKTGD 336

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 260177242 2391 LARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd17648   337 LVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRE 380
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1536-1954 4.73e-74

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: 253.77  E-value: 4.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1536 YPLTPLQEGILFHALLEPGgsHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPL-QVVRRLVRIPTE 1614
Cdd:cd19542     2 YPCTPMQEGMLLSQLRSPG--LYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFlQVVLKSLDPPIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1615 RIDARSMAVDGDAWIVERARDerrrgfaLDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGgmqh 1694
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPT-------LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG---- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1695 eaAHRTAPRPHRDYVAWLRGADAQSVERFWRRELGGFREVTPlgidrpPAgqrASSYRRFERALD--EHTTARLEQVLRE 1772
Cdd:cd19542   149 --QLLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPCAF------PS---LSPKRPAERSLSstRRSLAKLEAFCAS 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1773 RQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAERT 1852
Cdd:cd19542   218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSL 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1853 AYEHASLAQVQAWSEVPHGSALFESLIVVENYPVAPAFSGD-ELSVRLVGGDEQTNYPVTLVALP-GRRLTLRLLYEAER 1930
Cdd:cd19542   298 PHQHLSLREIQRALGLWPSGTLFNTLVSYQNFEASPESELSgSSVFELSAAEDPTEYPVAVEVEPsGDSLKVSLAYSTSV 377

                         410       420
                  ....*....|....*....|....
gi 260177242 1931 IPDGAAEGVLSHLESLLCAIADDP 1954
Cdd:cd19542   378 LSEEQAEELLEQFDDILEALLANP 401
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 200-1043 8.36e-74

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: 273.48  E-value: 8.36e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   200 LDVSTPLDLPTDLPRRAQQRYHVRQHFRDLGADlmdrvrESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGcgVSGRT 279
Cdd:TIGR03443    6 LDNPTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLG--TSSNK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   280 RTWQLgvvghmagIVPVParIDAAATPRAIIRELRNALRVTAKLQSVPLSRLAEQCRVPKSPGRMP-LVQAVFQEIRSFN 358
Cdd:TIGR03443   78 SGRPF--------VLRLN--ITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAFQDAPDNQ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   359 EAIRPEGFghmlrwsrgPLGFEVEVPselGSQLDLEVRCYdffsssvrtcwrYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:TIGR03443  148 QTTYSTGS---------TTDLTVFLT---PSSPELELSIY------------YNSLLFSSDRITIVADQLAQLLSAASSN 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   439 ----LGRLAL----QIDFIPEPERRrvlVEWnqtaSDYprERCLHHLFEEEARRVPD---------AVALDAGSNVVSYG 501
Cdd:TIGR03443  204 pdepIGKVSLitpsQKSLLPDPTKD---LDW----SGF--RGAIHDIFADNAEKHPDrtcvvetpsFLDPSSKTRSFTYK 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   502 ELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAF---LAHDAGVqIVLSAAG 578
Cdd:TIGR03443  275 QINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIylsVAKPRAL-IVIEKAG 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   579 AEERL------------GEGPWTVVRLDEDL--GRPDERDA---APNDNVSAENLAYVM---------YTSGSTGKPKGV 632
Cdd:TIGR03443  354 TLDQLvrdyidkelelrTEIPALALQDDGSLvgGSLEGGETdvlAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGV 433

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   633 avthrnvvrLVRGSSFA--------TFG--PDQVFLMMAPAAFDASTFEIWGALLHGARLVLfppesPTPEEIGRVVR-- 700
Cdd:TIGR03443  434 ---------LGRHFSLAyyfpwmakRFGlsENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLV-----PTADDIGTPGRla 499

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   701 ----EHGVTTLWLTAPLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTE------------- 763
Cdd:TIGR03443  500 ewmaKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTEtqravsyfeipsr 579

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   764 --NTTF-TTCHDVsrgmgtgsVPIGKPIANthVYLL----DEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPD 836
Cdd:TIGR03443  580 ssDSTFlKNLKDV--------MPAGKGMKN--VQLLvvnrNDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNN 649

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   837 --------------------PFSGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREA 896
Cdd:TIGR03443  650 wfvdpshwidldkennkperEFWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 729

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   897 VVIAREDRPGDKRLVAYVVGRE---------AEVP-------------RFSELRK----FLLQRLPDHMIPAAVVALDKL 950
Cdd:TIGR03443  730 VTLVRRDKDEEPTLVSYIVPQDksdeleefkSEVDdeessdpvvkgliKYRKLIKdireYLKKKLPSYAIPTVIVPLKKL 809

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   951 PLVPSGKLDRRALPAPTLSGRSGpfVAPEGHP----------EEVLARIWERVL--RVDAVGREDNFFELGGDSILAIQV 1018
Cdd:TIGR03443  810 PLNPNGKVDKPALPFPDTAQLAA--VAKNRSAsaadeeftetEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRM 887

                          970       980
                   ....*....|....*....|....*...
gi 260177242  1019 VAGAR---EVDLKLTVrqIFTHPTLSSL 1043
Cdd:TIGR03443  888 IFELRkklNVELPLGL--IFKSPTIKGF 913
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1536-1912 9.90e-69

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: 238.49  E-value: 9.90e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1536 YPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPTER 1615
Cdd:cd19544     2 YPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1616 IDarsmaVDGDAWIVERAR---DERRRGFALDAAPAMRLLLVRTGDR-SHRLIWTFHHILLDGWSVPLVLEEVfKRYsgg 1691
Cdd:cd19544    82 LT-----LDPGDDALAQLRarfDPRRYRLDLRQAPLLRAHVAEDPANgRWLLLLLFHHLISDHTSLELLLEEI-QAI--- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1692 MQHEAAHRTAPRPHRDYVAWLR-GADAQSVERFWRRELGGFREVT-PLGI-DRPPAGQRASSYRrfeRALDEHTTARLEQ 1768
Cdd:cd19544   153 LAGRAAALPPPVPYRNFVAQARlGASQAEHEAFFREMLGDVDEPTaPFGLlDVQGDGSDITEAR---LALDAELAQRLRA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1769 VLRERQLTIGTLIAGAWAILLERYGGRRDVVFGeTV-SGRSAPLEGIERMVGLFINTVPMRAVVDpERPIGEWLTELQGR 1847
Cdd:cd19544   230 QARRLGVSPASLFHLAWALVLARCSGRDDVVFG-TVlSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHAR 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1848 RAERTAYEHASLAQVQAWSEVPHGSALFESLIvveNY----PVAPAFSGDELS-VRLVGGDEQTNYPVTL 1912
Cdd:cd19544   308 LAELLRHEHASLALAQRCSGVPAPTPLFSALL---NYrhsaAAAAAAALAAWEgIELLGGEERTNYPLTL 374
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 616-959 2.10e-68

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: 234.87  E-value: 2.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  616 LAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPesPTPEE 694
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGgLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK--FDPEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  695 IGRVVREHGVTTLWLTAPLFHAVADRGLDQ---LRGVRQLLAGGDVLSPkHVARVLLGLPALRLINGYGPTEnTTFTTCH 771
Cdd:cd04433    80 ALELIEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPP-ELLERFEEAPGIKLVNGYGLTE-TGGTVAT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  772 DVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFvpdpfsgvpGARLYRTGD 851
Cdd:cd04433   158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD---------EDGWYRTGD 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  852 LARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFL 931
Cdd:cd04433   229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHV 308

                         330       340
                  ....*....|....*....|....*...
gi 260177242  932 LQRLPDHMIPAAVVALDKLPLVPSGKLD 959
Cdd:cd04433   309 RERLAPYKVPRRVVFVDALPRTASGKID 336
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1536-1954 2.10e-68

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: 237.20  E-value: 2.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1536 YPLTPLQEGILfhALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPTER 1615
Cdd:cd19545     2 YPCTPLQEGLM--ALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1616 IDARSMAVDGDawiverardeRRRGFALDAaPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGmqhe 1695
Cdd:cd19545    80 STSLDEYLEED----------RAAPMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGE---- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1696 aaHRTAPRPHRDYVAWLRGADAQSVERFWRRELGGFREV--TPLgidrPPAGQRASSYRRFERALDEHTTARleqvlreR 1773
Cdd:cd19545   145 --PVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfPPL----PSSRYQPRPDATLEHSISLPSSAS-------S 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1774 QLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTELQGRRAERTA 1853
Cdd:cd19545   212 GVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIP 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1854 YEHASLAQVQAWSEVPHGSALFESLIVVE--NYPVAPAFSGDELSVRLVGGDEQTNYPVTL-VALPGRRLTLRLLYEAER 1930
Cdd:cd19545   292 FEHTGLQNIRRLGPDARAACNFQTLLVVQpaLPSSTSESLELGIEEESEDLEDFSSYGLTLeCQLSGSGLRVRARYDSSV 371

                         410       420
                  ....*....|....*....|....
gi 260177242 1931 IPDGAAEGVLSHLESLLCAIADDP 1954
Cdd:cd19545   372 ISEEQVERLLDQFEHVLQQLASAP 395
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
478-963 2.72e-68

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 240.57  E-value: 2.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAgaEERLGEGPWTVVRLDE--DLGRPDErDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVT 635
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATE--ELPLEILGIPVITLDElkDIFATGN-PYDFDHAVKGDDNYYIIFTSGTTGKPKGVQIS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  636 HRNVVrlvrgsSFA-------TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPT-PEEIGRVVREHGVTTl 707
Cdd:PRK04813  165 HDNLV------SFTnwmledfALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTAnFKQLFETLPQLPINV- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  708 WLTAPLFHAVA--DRGLDQ--LRGVRQLLAGGDVLsPKHVARVLLG-LPALRLINGYGPTENTTFTTCHDVSRGMGT--G 780
Cdd:PRK04813  238 WVSTPSFADMCllDPSFNEehLPNLTHFLFCGEEL-PHKTAKKLLErFPSATIYNTYGPTEATVAVTSIEITDEMLDqyK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  781 SVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPdpFSGVPGarlYRTGDLArYLPNGD 860
Cdd:PRK04813  317 RLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT--FDGQPA---YHTGDAG-YLEDGL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  861 MEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIaredrPGDK-----RLVAYVV----GREAEVPRFSELRKFL 931
Cdd:PRK04813  391 LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-----PYNKdhkvqYLIAYVVpkeeDFEREFELTKAIKKEL 465

                         490       500       510
                  ....*....|....*....|....*....|..
gi 260177242  932 LQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK04813  466 KERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 474-963 1.40e-67

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: 237.08  E-value: 1.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 PAYPSERLAFLAHDAGVQIVLSAAGAEerlgegpwTVVRLDEDLGRPDERDaapndnvsAENLAYVMYTSGSTGKPKGVA 633
Cdd:cd05936    81 PLYTPRELEHILNDSGAKALIVAVSFT--------DLLAAGAPLGERVALT--------PEDVAVLQYTSGTTGVPKGAM 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  634 VTHRNVV---RLVRGSSFATFGPDQVFLMMAPaafdasTFEIWG-------ALLHGARLVLFPpeSPTPEEIGRVVREHG 703
Cdd:cd05936   145 LTHRNLVanaLQIKAWLEDLLEGDDVVLAALP------LFHVFGltvalllPLALGATIVLIP--RFRPIGVLKEIRKHR 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  704 VT------TLWLTapLFHAVADRGLDqLRGVRQLLAGGDVLSPKHVARV--LLGLPalrLINGYGPTENTTFTTCHDVSR 775
Cdd:cd05936   217 VTifpgvpTMYIA--LLNAPEFKKRD-FSSLRLCISGGAPLPVEVAERFeeLTGVP---IVEGYGLTETSPVVAVNPLDG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  776 GMGTGSvpIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLARY 855
Cdd:cd05936   291 PRKPGS--IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL---------RTGDIGYM 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  856 LPNGDMeFLGRRDGQVKIR-GFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQR 934
Cdd:cd05936   360 DEDGYF-FIVDRKKDMIIVgGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQ 438

                         490       500
                  ....*....|....*....|....*....
gi 260177242  935 LPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05936   439 LAGYKVPRQVEFRDELPKSAVGKILRREL 467
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1989-2431 7.49e-67

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: 234.32  E-value: 7.49e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPL 2068
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRR-LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2069 DPRWPLERVAAVLGTTRPVCIVTderhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagph 2148
Cdd:COG0318    80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2149 nmAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLS-VYDVFGMLAAGGSIHIASEddlRS 2227
Cdd:COG0318   103 --ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FD 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 PERLAAELGRGTITFWDSAPAALQQLV--PYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEATVW 2305
Cdd:COG0318   178 PERVLELIERERVTVLFGVPTMLARLLrhPEFAR-YDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPV 255

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2306 SNYFEVDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFvPDPFsgepgarl 2385
Cdd:COG0318   256 VTVNPEDPGERRPGSV--GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------- 324

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 260177242 2386 YRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:COG0318   325 LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPG 370
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
475-963 8.74e-67

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 237.70  E-value: 8.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  475 HHLFEEEARRVPDAVAL-----DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAY 549
Cdd:COG0365    12 YNCLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  550 VPLDPAYPSERLAFLAHDAGVQIVLSAAG----------------AEERLgEGPWTVV---RLDEDLGRPDERD-----A 605
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidlkekvdeALEEL-PSLEHVIvvgRTGADVPMEGDLDwdellA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  606 APNDN-----VSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFATFG--PDQVFLMMAPAAFdasTFEIW----G 674
Cdd:COG0365   171 AASAEfepepTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDlkPGDVFWCTADIGW---ATGHSyivyG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  675 ALLHGARLVLFP--PESPTPEEIGRVVREHGVTTLWlTAP----LFHAVADRGLDQ--LRGVRQLLAGGDVLSPKHVARV 746
Cdd:COG0365   248 PLLNGATVVLYEgrPDFPDPGRLWELIEKYGVTVFF-TAPtairALMKAGDEPLKKydLSSLRLLGSAGEPLNPEVWEWW 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  747 --LLGLPalrLINGYGPTEnttfTTCHDVSRGMGTGSVP--IGKPIANTHVYLLDEQMNPVPPNAVGEL-FTGGD-GLAR 820
Cdd:COG0365   327 yeAVGVP---IVDGWGQTE----TGGIFISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELvIKGPWpGMFR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  821 GYHERPDQTAERFvpdpFSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIA 900
Cdd:COG0365   400 GYWNDPERYRETY----FGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242  901 REDRPGDKRLVAYVVGREAEVPRF---SELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:COG0365   474 VPDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 474-965 2.50e-66

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: 235.06  E-value: 2.50e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   554 PAYPSERLAFLAHDAGVQIVLSAAGAEERLGEGP------WTVVRLDE----DLGRPDER-----------DAAPNDNVS 612
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTSSERLDLLHPALpgchdlRTLIIVGDpahaSEGHPGEEpaswpkllalgDADPPHPVI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   613 AENLAYVMYTSGSTGKPKGVAVTHRNVVR-LVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFppESPT 691
Cdd:TIGR03098  162 DSDMAAILYTSGSTGRPKGVVLSHRNLVAgAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH--DYLL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   692 PEEIGRVVREHGVTTLWLTAPLFHAVA--DRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTE--NTTF 767
Cdd:TIGR03098  240 PRDVLKALEKHGITGLAAVPPLWAQLAqlDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEafRSTY 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   768 TTCHDVSRGMGTgsvpIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDP-FSG---VPG 843
Cdd:TIGR03098  320 LPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpFPGelhLPE 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   844 ARLYrTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPR 923
Cdd:TIGR03098  396 LAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELD 474

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 260177242   924 FSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:TIGR03098  475 RAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 488-963 4.70e-62

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: 220.42  E-value: 4.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  488 AVALDAGS--NVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd17654     5 ALIIDQTTsdTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLsaagAEERLGEGPWTVVRLDEDLGRPderdaapndnvSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG 645
Cdd:cd17654    85 KKCHVSYLL----QNKELDNAPLSFTPEHRHFNIR-----------TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQH 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 SS--FATFgPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPT-PEEIGRVVRE-HGVTTLWLTAPLFH-----A 716
Cdd:cd17654   150 FRslFNIT-SEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVlPSKLADILFKrHRITVLQATPTLFRrfgsqS 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  717 VADRGLDQLRGVRQLLAGGDVLSPKHVARVLLG-LPALRLINGYGPTENTTFTTCHDVSRGMGTgsVPIGKPIANTHVYL 795
Cdd:cd17654   229 IKSTVLSATSSLRVLALGGEPFPSLVILSSWRGkGNRTRIFNIYGITEVSCWALAYKVPEEDSP--VQLGSPLLGTVIEV 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  796 LDEQMNPVPpnavGELFTGgdGLARGYherpdqtaerFVPDPFsGVPGARLYRTGDLARyLPNGDMEFLGRRDGQVKIRG 875
Cdd:cd17654   307 RDQNGSEGT----GQVFLG--GLNRVC----------ILDDEV-TVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRG 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  876 FRIELAEVEAALLQHPALrEAVVIAREDrpgDKRLVAYVVGREAEVPRFSELRKFLlqrLPDHMIPAAVVALDKLPLVPS 955
Cdd:cd17654   369 KRINLDLIQQVIESCLGV-ESCAVTLSD---QQRLIAFIVGESSSSRIHKELQLTL---LSSHAIPDTFVQIDKLPLTSH 441


                  ....*...
gi 260177242  956 GKLDRRAL 963
Cdd:cd17654   442 GKVDKSEL 449
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 474-971 2.91e-61

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 220.44  E-value: 2.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:PRK06187    8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 PAYPSERLAFLAHDAGVQIVL-------SAAGAEERL---------GEGP-----WTVVRLDEDL-GRPDERDAAPNDnv 611
Cdd:PRK06187   88 IRLKPEEIAYILNDAEDRVVLvdsefvpLLAAILPQLptvrtviveGDGPaaplaPEVGEYEELLaAASDTFDFPDID-- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  612 saENLAYVM-YTSGSTGKPKGVAVTHRNVVRLVRGS-SFATFGPDQVFLMMAPAaFDASTfeiWG----ALLHGARLVLf 685
Cdd:PRK06187  166 --ENDAAAMlYTSGTTGHPKGVVLSHRNLFLHSLAVcAWLKLSRDDVYLVIVPM-FHVHA---WGlpylALMAGAKQVI- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  686 pPESPTPEEIGRVVREHGVTTLwLTAP-----LFHAVADRGLDqLRGVRQLLAGGDVLsPKHVARVLLGLPALRLINGYG 760
Cdd:PRK06187  239 -PRRFDPENLLDLIETERVTFF-FAVPtiwqmLLKAPRAYFVD-FSSLRLVIYGGAAL-PPALLREFKEKFGIDLVQGYG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  761 PTENTTFTTC-----HDVSRGMGTGSVpiGKPIANTHVYLLDEQMNPVPPN--AVGELFTGGDGLARGYHERPDQTAERF 833
Cdd:PRK06187  315 MTETSPVVSVlppedQLPGQWTKRRSA--GRPLPGVEARIVDDDGDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETI 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  834 VPDpfsgvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAY 913
Cdd:PRK06187  393 DGG---------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAV 463

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242  914 VVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGR 971
Cdd:PRK06187  464 VVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 6-438 1.98e-60

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: 214.94  E-value: 1.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    6 PLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALR-LVVRPDNEGLVQSLADVSAVDFGVT 84
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRtLLVRDDGGVPRQEILPPGPAPLEVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   85 DGSSWD---EPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:cd19539    83 DLSDPDsdrERRLEELLRERESRGFDLDEEPPiRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLDvstPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRES 240
Cdd:cd19539   163 APLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAE---PTALPTDRPRPAGFPYPGADLRFELDAELVAALREL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  241 ARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRVT 320
Cdd:cd19539   240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  321 AKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSFNEAIRPEGfghmlrwsrgplGFEVEVPSEL--GSQLDLEVRcY 398
Cdd:cd19539   320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAG------------GLSYTEGSDIpdGAKFDLNLT-V 386

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 260177242  399 DFFSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19539   387 TEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLAN 426
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 482-960 9.64e-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: 213.24  E-value: 9.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:cd17631     5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLsaagaeerlgegpwtvvrldedlgrpderdaapndnvsaENLAYVMYTSGSTGKPKGVAVTHRNVVR 641
Cdd:cd17631    85 AYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLW 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  642 LVRGSSFA-TFGPDQVFLMMAP----AAFDASTFEIwgaLLHGARLVLfpPESPTPEEIGRVVREHGVTTLWLTAPLFHA 716
Cdd:cd17631   126 NAVNALAAlDLGPDDVLLVVAPlfhiGGLGVFTLPT---LLRGGTVVI--LRKFDPETVLDLIERHRVTSFFLVPTMIQA 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  717 VAD----RGLDqLRGVRQLLAGGdvlSPkHVARVLLGLPA--LRLINGYGPTE---NTTFTTCHDVSRGMGTgsvpIGKP 787
Cdd:cd17631   201 LLQhprfATTD-LSSLRAVIYGG---AP-MPERLLRALQArgVKFVQGYGMTEtspGVTFLSPEDHRRKLGS----AGRP 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  788 IANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLARYLPNGDMEFLGRR 867
Cdd:cd17631   272 VFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF---------HTGDLGRLDEDGYLYIVDRK 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  868 DGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVAL 947
Cdd:cd17631   343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFV 422

                         490
                  ....*....|...
gi 260177242  948 DKLPLVPSGKLDR 960
Cdd:cd17631   423 DALPRNATGKILK 435
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 492-958 1.62e-59

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: 214.38  E-value: 1.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  492 DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQ 571
Cdd:cd05911     5 ADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  572 IVLSAAG-------AEERLGEGP--WTV-VRLDEDLGRPD---------ERDAAPNDNVSAENLAYVMYTSGSTGKPKGV 632
Cdd:cd05911    85 VIFTDPDglekvkeAAKELGPKDkiIVLdDKPDGVLSIEDllsptlgeeDEDLPPPLKDGKDDTAAILYSSGTTGLPKGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  633 AVTHRNVV---RLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPpeSPTPEEIGRVVREHGVTTLWL 709
Cdd:cd05911   165 CLSHRNLIanlSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP--KFDSELFLDLIEKYKITFLYL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  710 TAPLFHAVADRGL---DQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTEnTTFTTCHDVSRGMGTGSVpiGK 786
Cdd:cd05911   243 VPPIAAALAKSPLldkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE-TGGILTVNPDGDDKPGSV--GR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  787 PIANTHVYLLDEQ-MNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLG 865
Cdd:cd05911   320 LLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW--------LHTGDIGYFDEDGYLYIVD 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  866 RRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDH-MIPAAV 944
Cdd:cd05911   392 RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYkQLRGGV 471

                         490
                  ....*....|....
gi 260177242  945 VALDKLPLVPSGKL 958
Cdd:cd05911   472 VFVDEIPKSASGKI 485
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 485-966 2.26e-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: 206.21  E-value: 2.26e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  485 VPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAF- 563
Cdd:cd17647     8 VETPSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIy 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  564 --LAHDAGVqIVLSAAGaeerLGEGPwtvvrldedlgrpderDAAPNdnvsaenlayVMYTSGSTGKPKGVAVTHRNVVR 641
Cdd:cd17647    88 lgVAKPRGL-IVIRAAG----VVVGP----------------DSNPT----------LSFTSGSEGIPKGVLGRHFSLAY 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  642 LVRGSSfATFG--PDQVFLMMAPAAFDASTFEIWGALLHGARLvLFPPESP--TPEEIGRVVREHGVTTLWLTAPLFHAV 717
Cdd:cd17647   137 YFPWMA-KRFNlsENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQLL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  718 ADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDV-SRGMGTGSVPIGKPIANTHVYLL 796
Cdd:cd17647   215 TAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVpSRSSDPTFLKNLKDVMPAGRGML 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  797 DEQMNPVPPN---------AVGELFTGGDGLARGYHERPDQTAERFV------PD--------------PFSGVPGARLY 847
Cdd:cd17647   295 NVQLLVVNRNdrtqicgigEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvePDhwnyldkdnnepwrQFWLGPRDRLY 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  848 RTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSE- 926
Cdd:cd17647   375 RTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFa 454

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242  927 --------------------------LRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAP 966
Cdd:cd17647   455 qedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 1989-2428 2.98e-56

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: 205.38  E-value: 2.98e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1989 IHELFESSvERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPL 2068
Cdd:TIGR01734    3 IEAIQAFA-ETYPQTIAYRYQG-QELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2069 DPRWPLERVAAVLGTTRPVCIVTderhlgAVEIAARQLGIEhVVSLDGDgkdadgnvvihgRRALADLADGNLPRAAGPH 2148
Cdd:TIGR01734   81 DTSIPSERIEMIIEAAGPELVIH------TAELSIDAVGTQ-IITLSAL------------EQAETSGGPVSFDHAVKGD 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2149 NMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSP 2228
Cdd:TIGR01734  142 DNYYIIYTSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNF 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2229 ERLAAELGRGTITFWDSAPAALQQ--LVPYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWS 2306
Cdd:TIGR01734  222 KLLFEELPKTGLNVWVSTPSFVDMclLDPNFNQ-ENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAV 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2307 NYFEV-DGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFvpdpFSGEpGARL 2385
Cdd:TIGR01734  301 TSVKItQEILDQYPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHE-GQPA 375

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 260177242  2386 YRTGDLArFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQ 2428
Cdd:TIGR01734  376 YRTGDAG-TITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQ 417
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1535-1951 3.97e-56

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: 202.64  E-value: 3.97e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1535 LYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLwEGVPEPLQVVR-RLVRIPT 1613
Cdd:cd19066     1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFC-EEAGRYEQVVLdKTVRFRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1614 ERIDARSMAvDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQ 1693
Cdd:cd19066    80 EIIDLRNLA-DPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1694 HEAAHRTAPRPHRDYVAWLRGA----DAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEHTTARLEQV 1769
Cdd:cd19066   159 QKPTLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1770 LRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRsaPLEGIERMVGLFINTVPMRAVVDPERPIGEWLTEL--QGR 1847
Cdd:cd19066   239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR--PDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTkeQSR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1848 RAERTAYEHASLAQVQAWSEVPHG-SALFESLIVVENYP----VAPAFSGDELSVRLVGGdeqTNYPVTLVALPGRR--L 1920
Cdd:cd19066   317 EAIEHQRVPFIELVRHLGVVPEAPkHPLFEPVFTFKNNQqqlgKTGGFIFTTPVYTSSEG---TVFDLDLEASEDPDgdL 393

                         410       420       430
                  ....*....|....*....|....*....|.
gi 260177242 1921 TLRLLYEAERIPDgaaEGVLSHLESLLCAIA 1951
Cdd:cd19066   394 LLRLEYSRGVYDE---RTIDRFAERYMTALR 421
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 505-963 2.55e-55

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: 201.13  E-value: 2.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  505 RRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGA----YVPLDPAYPSERLAFLAHDAGVQIVLSAAGAE 580
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  581 ERLGEG------PWTVVRLDEDLGRPDERDAAPndnVSAENLAYVMYTSGSTGKPKGVAVTHRNVvrLVRGSSFATF--- 651
Cdd:cd05922    81 DRLRDAlpaspdPGTVLDADGIRAARASAPAHE---VSHEDLALLLYTSGSTGSPKLVRLSHQNL--LANARSIAEYlgi 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  652 -GPDQVFLMMaPAAFDASTFEIWGALLHGARLVLfPPESPTPEEIGRVVREHGVTTLWLTAPLFH-----AVADRGLDQL 725
Cdd:cd05922   156 tADDRALTVL-PLSYDYGLSVLNTHLLRGATLVL-TNDGVLDDAFWEDLREHGATGLAGVPSTYAmltrlGFDPAKLPSL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  726 RGVRQllAGGDvLSPKHVARVLLGLPALRLINGYGPTENT---TFTTCHDVSRGMGTgsvpIGKPIANTHVYLLDEQMNP 802
Cdd:cd05922   234 RYLTQ--AGGR-LPQETIARLRELLPGAQVYVMYGQTEATrrmTYLPPERILEKPGS----IGLAIPGGEFEILDDDGTP 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  803 VPPNAVGELFTGGDGLARGYHERPdqtaerfvPDPFSGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAE 882
Cdd:cd05922   307 TPPGEPGEIVHRGPNVMKGYWNDP--------PYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTE 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  883 VEAALLQHPALREAVVIAREDRPGDkRLVAYVVGREAEVPrfSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRA 962
Cdd:cd05922   379 IEAAARSIGLIIEAAAVGLPDPLGE-KLALFVTAPDKIDP--KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAA 455


                  .
gi 260177242  963 L 963
Cdd:cd05922   456 L 456
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 6-458 5.46e-55

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: 199.87  E-value: 5.46e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242     6 PLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEG-LVQSLADVSAVDFGVT 84
Cdd:pfam00668    6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGePVQVILEERPFELEII 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    85 DGSSWD----EPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGR 159
Cdd:pfam00668   86 DISDLSeseeEEAIEAFIQRDLQSPFDLEKGPLfRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   160 AATLTPISRgFRDYLVWHRDLLASDDASALVREWAamvGDLDVSTP-LDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVR 238
Cdd:pfam00668  166 PLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWL---EQLEGELPvLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   239 ESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALR 318
Cdd:pfam00668  242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   319 VTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFqeirSFNEAIRPEGFGHMLRWSRGPLGFEVEVPSELGSQLDLEVRCY 398
Cdd:pfam00668  322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMF----SFQNYLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASER 397

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   399 DffsSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVL 458
Cdd:pfam00668  398 G---GGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 468-963 2.78e-54

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: 200.37  E-value: 2.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  468 YPRERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGG 547
Cdd:COG1021    21 YWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  548 ayVPLDpAYPSERLAFLAH-----DAGVQIVLSAAG-------AEERLGEGPW--TVVRLDE--------DLGRPDERDA 605
Cdd:COG1021   101 --IPVF-ALPAHRRAEISHfaeqsEAVAYIIPDRHRgfdyralARELQAEVPSlrHVLVVGDageftsldALLAAPADLS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  606 APNdnVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVFLMMAPAA--FDASTFEIWGALLHGARL 682
Cdd:COG1021   178 EPR--PDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICgLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTV 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  683 VLFPpeSPTPEEIGRVVREHGVT---------TLWLTAplfhavADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPAl 753
Cdd:COG1021   256 VLAP--DPSPDTAFPLIERERVTvtalvpplaLLWLDA------AERSRYDLSSLRVLQVGGAKLSPELARRVRPALGC- 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  754 RLINGYGPTE---NTT---------FTTChdvsrgmgtgsvpiGKPI-ANTHVYLLDEQMNPVPPNAVGELFTGGDGLAR 820
Cdd:COG1021   327 TLQQVFGMAEglvNYTrlddpeeviLTTQ--------------GRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIR 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  821 GYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVkIR-GFRIELAEVEAALLQHPALREAVVI 899
Cdd:COG1021   393 GYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVV 463

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  900 AREDRPGDKRLVAYVVGREAEvPRFSELRKFLLQR-LPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:COG1021   464 AMPDEYLGERSCAFVVPRGEP-LTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1536-1954 2.44e-53

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: 194.50  E-value: 2.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1536 YPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVpEPLQVVRRLVRIPTER 1615
Cdd:cd19531     2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPLPLPLPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1616 IDARSM-AVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGgmqh 1694
Cdd:cd19531    81 VDLSGLpEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAA---- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1695 EAAHRTAPRP-----HRDYVAW----LRGADAQSVERFWRRELGGFREVTPLGIDRP-PAGQrasSYR--RFERALDEHT 1762
Cdd:cd19531   157 FLAGRPSPLPplpiqYADYAVWqrewLQGEVLERQLAYWREQLAGAPPVLELPTDRPrPAVQ---SFRgaRVRFTLPAEL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1763 TARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPleGIERMVGLFINTVPMRAVVDPERPIGEWLT 1842
Cdd:cd19531   234 TAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLVLRTDLSGDPTFRELLA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1843 ELqgRRAERTAYEHAslaqvqawsEVP---------------HgSALFESLIVVENYPvAPAFSGDELSVRLVGGDEQT- 1906
Cdd:cd19531   312 RV--RETALEAYAHQ---------DLPfeklvealqperdlsR-SPLFQVMFVLQNAP-AAALELPGLTVEPLEVDSGTa 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 260177242 1907 NYPVTLVALP-GRRLTLRL-----LYEAERIpdgaaEGVLSHLESLLCAIADDP 1954
Cdd:cd19531   379 KFDLTLSLTEtDGGLRGSLeyntdLFDAATI-----ERMAGHFQTLLEAIVADP 427
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 485-963 5.92e-53

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: 195.22  E-value: 5.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  485 VPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFL 564
Cdd:cd05926     2 DAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  565 AHDAGVQIVL-------SAAGAEERLGegpWTVVRLDEDLGRPDERD--------------AAPNDNVSAENLAYVMYTS 623
Cdd:cd05926    82 LADLGSKLVLtpkgelgPASRAASKLG---LAILELALDVGVLIRAPsaeslsnlladkknAKSEGVPLPDDLALILHTS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  624 GSTGKPKGVAVTHRNVVRLVRG--SSFATFGPDQVFLMMaPaafdasTFEIWG-------ALLHGARLVLFPPESPT--- 691
Cdd:cd05926   159 GTTGRPKGVPLTHRNLAASATNitNTYKLTPDDRTLVVM-P------LFHVHGlvasllsTLAAGGSVVLPPRFSAStfw 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  692 PEeigrvVREHGVTtlWLTA-PLFHAV--------ADRGLDQLRGVRqllAGGDVLSPKHVARV--LLGLPalrLINGYG 760
Cdd:cd05926   232 PD-----VRDYNAT--WYTAvPTIHQIllnrpepnPESPPPKLRFIR---SCSASLPPAVLEALeaTFGAP---VLEAYG 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  761 PTEnttftTCHDVS------RGMGTGSVPIGkpiANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFV 834
Cdd:cd05926   299 MTE-----AAHQMTsnplppGPRKPGSVGKP---VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  835 PDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYV 914
Cdd:cd05926   371 KDGW--------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAV 442

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 260177242  915 VGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05926   443 VLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 464-963 1.12e-52

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: 194.08  E-value: 1.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  464 TASDYPRERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVL 543
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  544 KAGGAYVPldpAYPSERLAFLAHdagvqiVLSAAGAeerlgegpwTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTS 623
Cdd:cd05920    87 RLGAVPVL---ALPSHRRSELSA------FCAHAEA---------VAYIVPDRHAGFDHRALARELAESIPEVALFLLSG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  624 GSTGKPKGVAVTHRNVVRLVRGSS-FATFGPDQVFLMMAPAA--FDASTFEIWGALLHGARLVLFPpeSPTPEEIGRVVR 700
Cdd:cd05920   149 GTTGTPKLIPRTHNDYAYNVRASAeVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAP--DPSPDAAFPLIE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  701 EHGVTTLWLT---APLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLlglPAL--RLINGYGPTEN----TTFTTCH 771
Cdd:cd05920   227 REGVTVTALVpalVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVP---PVLgcTLQQVFGMAEGllnyTRLDDPD 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  772 DVSrgMGTGsvpiGKPI-ANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTG 850
Cdd:cd05920   304 EVI--IHTQ----GRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTG 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  851 DLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEvPRFSELRKF 930
Cdd:cd05920   370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPP-PSAAQLRRF 448

                         490       500       510
                  ....*....|....*....|....*....|....
gi 260177242  931 LLQR-LPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05920   449 LRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1538-1777 3.28e-52

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 184.86  E-value: 3.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1538 LTPLQEGILFhalLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGvPEPLQVVRRLVRIPTERID 1617
Cdd:COG4908     1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1618 ARSM-AVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQHEA 1696
Cdd:COG4908    77 LSALpEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1697 AHRTA-PRPHRDYVAWLR----GADAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEHTTARLEQVLR 1771
Cdd:COG4908   157 PPLPElPIQYADYAAWQRawlqSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236


                  ....*.
gi 260177242 1772 ERQLTI 1777
Cdd:COG4908   237 AHGATV 242
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1991-2428 5.34e-52

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 192.80  E-value: 5.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP 2070
Cdd:PRK04813    6 ETIEEFAQTQPDFPAYDYLGEK-LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 RWPLERVAAVLGTTRP-VCIVTDERHLGAVEIaarqlgieHVVSLDgdgkdadgNVVihgrRALADLADGNLPRAAGPHN 2149
Cdd:PRK04813   85 SSPAERIEMIIEVAKPsLIIATEELPLEILGI--------PVITLD--------ELK----DIFATGNPYDFDHAVKGDD 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2150 MAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPE 2229
Cdd:PRK04813  145 NYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLAAELGRGTITFWDSAP--AALQQLVPYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSN 2307
Cdd:PRK04813  225 QLFETLPQLPINVWVSTPsfADMCLLDPSFNE-EHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2308 YFEV-DGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVpdPFSGEPGarlY 2386
Cdd:PRK04813  304 SIEItDEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF--TFDGQPA---Y 378

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 260177242 2387 RTGDLArFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQ 2428
Cdd:PRK04813  379 HTGDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQ 419
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 486-963 7.58e-52

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: 192.58  E-value: 7.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVL-----------SAAGAEERL-------GEGPWTVVRLDEDLgRPDERDAAPNDNVSAENLAYVMYTSGSTG 627
Cdd:cd05959    98 EDSRARVVVvsgelapvlaaALTKSEHTLvvlivsgGAGPEAGALLLAEL-VAAEAEQLKPAATHADDPAFWLYSSGSTG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  628 KPKGVAVTHRNVVRLVRGSSFATFG--PDQVFLMMAPAAF-----DASTFEIWgallHGARLVLFPpESPTPEEIGRVVR 700
Cdd:cd05959   177 RPKGVVHLHADIYWTAELYARNVLGirEDDVCFSAAKLFFayglgNSLTFPLS----VGATTVLMP-ERPTPAAVFKRIR 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  701 EH------GVTTLWLTAPLFHAVADRGLDQLRgvrQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTE-------NTTf 767
Cdd:cd05959   252 RYrptvffGVPTLYAAMLAAPNLPSRDLSSLR---LCVSAGEAL-PAEVGERWKARFGLDILDGIGSTEmlhiflsNRP- 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  768 ttcHDVSRGMGtgsvpiGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVpdpfsgvpgARLY 847
Cdd:cd05959   327 ---GRVRYGTT------GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ---------GEWT 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  848 RTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVV---GREAEVPRF 924
Cdd:cd05959   389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpGYEDSEALE 468

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 260177242  925 SELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05959   469 EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1784-2430 5.14e-51

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: 199.91  E-value: 5.14e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1784 AWAILLERYGGRRDVVFGEtvsgrSAPLEGIERMVGLFINtvpmravvdPERPIGEWLTELQGRRAERTAYEHASLAQVQ 1863
Cdd:TIGR03443   55 AFAALVYRLTGDEDIVLGT-----SSNKSGRPFVLRLNIT---------PELSFLQLYAKVSEEEKEGASDIGVPFDELS 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1864 AWSEVPHGSALFESLIVVENYPvAPAFSGDELSVRLVggdeqTNYPVTLV-ALPGRRLTL---RLLYEAERIpdgaaEGV 1939
Cdd:TIGR03443  121 EHIQAAKKLERTPPLFRLAFQD-APDNQQTTYSTGST-----TDLTVFLTpSSPELELSIyynSLLFSSDRI-----TIV 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1940 LSHLESLLCAIADDPDLPTGDLPLLSAHERR-----QVVADWNDTaRAyarerCIHELFESSVERSPG--------SVAL 2006
Cdd:TIGR03443  190 ADQLAQLLSAASSNPDEPIGKVSLITPSQKSllpdpTKDLDWSGF-RG-----AIHDIFADNAEKHPDrtcvvetpSFLD 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2007 CYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRP 2086
Cdd:TIGR03443  264 PSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKP 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2087 ---VCI-------------VTDErhlgaVEIAAR--QLGIEHVVSLDGDGKDADGNVVIHGRRALADLADGNLpraAGPH 2148
Cdd:TIGR03443  344 ralIVIekagtldqlvrdyIDKE-----LELRTEipALALQDDGSLVGGSLEGGETDVLAPYQALKDTPTGVV---VGPD 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2149 NMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSP 2228
Cdd:TIGR03443  416 SNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTP 495

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2229 ERLAAELGRGTITFWDSAPAALQQLVPYFDR-IedgSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSN 2307
Cdd:TIGR03443  496 GRLAEWMAKYGATVTHLTPAMGQLLSAQATTpI---PSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVS 572

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  2308 YFEVDGI--DPRWTS-----IPYGRPIQNARYYVLDRS--GNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVP---- 2374
Cdd:TIGR03443  573 YFEIPSRssDSTFLKnlkdvMPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNnwfv 652

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242  2375 --------DPFSGEPGA--------RLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:TIGR03443  653 dpshwidlDKENNKPERefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHP 724
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 487-963 8.82e-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: 187.50  E-value: 8.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  487 DAVALDAGSNVVSYGELNRRADKLAHML-RLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLsaagaeerlgegpwtvvrldedlgrpderdaapndnvsaeNLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG 645
Cdd:cd05941    81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 SSFA-TFGPDQVFLMMAPA-----AFDASTfeiwGALLHGARLVLFPPESPTPEEIGRVVRE----HGVTTLW---LTAP 712
Cdd:cd05941   121 LVDAwRWTEDDVLLHVLPLhhvhgLVNALL----CPLFAGASVEFLPKFDPKEVAISRLMPSitvfMGVPTIYtrlLQYY 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  713 LFHAVADRGL--DQLRGVRQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTENTTFTTC-HDVSRGMGTgsvpIGKPIA 789
Cdd:cd05941   197 EAHFTDPQFAraAAAERLRLMVSGSAAL-PVPTLEEWEAITGHTLLERYGMTEIGMALSNpLDGERRPGT----VGMPLP 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  790 NTHVYLLDEQMN-PVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGR-R 867
Cdd:cd05941   272 GVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDGYYWILGRsS 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  868 DGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGRE-AEVPRFSELRKFLLQRLPDHMIPAAVVA 946
Cdd:cd05941   344 VDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAgAAALSLEELKEWAKQRLAPYKRPRRLIL 423

                         490
                  ....*....|....*..
gi 260177242  947 LDKLPLVPSGKLDRRAL 963
Cdd:cd05941   424 VDELPRNAMGKVNKKEL 440
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 477-961 1.01e-50

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 189.71  E-value: 1.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 PSERLAFLAHDAGVQIVLSAAGAEERLGE------GPWTVVRLDEDLGRPDERDAAPNDNV-------------SAENLa 617
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYEREFAPRVAEvlprlpKLRTLVVVEDGSGNDLLPGAVDYEDAlaagsperdfgerSPDDL- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  618 YVMYTSGSTGKPKGVAVTHRNVVR----------------LVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGAR 681
Cdd:PRK07798  167 YLLYTGGTTGMPKGVMWRQEDIFRvllggrdfatgepiedEEELAKRAAAGPGMRRFPAPPLMHGAGQWAAFAALFSGQT 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  682 LVLFPPESPTPEEIGRVVREHGVTTLWLT-----APLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLI 756
Cdd:PRK07798  247 VVLLPDVRFDADEVWRTIEREKVNVITIVgdamaRPLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLT 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  757 NGYGPTEnTTFTTCHDVSRGMGTGSVPIGKPIANTHVylLDEQMNPVPPnavGElftGGDG-LAR------GYHERPDQT 829
Cdd:PRK07798  327 DSIGSSE-TGFGGSGTVAKGAVHTGGPRFTIGPRTVV--LDEDGNPVEP---GS---GEIGwIARrghiplGYYKDPEKT 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  830 AERFVPdpfsgVPGARLYRTGDLARYLPNGDMEFLGRrdGQVKIR--GFRIELAEVEAALLQHPALREAVVIAREDRPGD 907
Cdd:PRK07798  398 AETFPT-----IDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADALVVGVPDERWG 470

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 260177242  908 KRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRR 961
Cdd:PRK07798  471 QEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 499-964 3.93e-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. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 184.80  E-value: 3.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  499 SYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYpseRLAFLAHdagvqiVLSAAG 578
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTAL---RGDELAY------IIDHSG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  579 AEerlgegpWTVVrldedlgrpderdaapndnvsaeNLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVF 657
Cdd:cd05934    76 AQ-------LVVV-----------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFgLGEDDVY 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  658 LMMAPaAF--DASTFEIWGALLHGARLVLFPPESPTpeEIGRVVREHGVT---TLWLTAPLFHAVADRGLDQLRGVRQLL 732
Cdd:cd05934   126 LTVLP-LFhiNAQAVSVLAALSVGATLVLLPRFSAS--RFWSDVRRYGATvtnYLGAMLSYLLAQPPSPDDRAHRLRAAY 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  733 AGGDVLSPKHVARVLLGLPalrLINGYGPTEnTTFTTCHDVSRGMGTGSvpIGKPIANTHVYLLDEQMNPVPPNAVGELF 812
Cdd:cd05934   203 GAPNPPELHEEFEERFGVR---LLEGYGMTE-TIVGVIGPRDEPRRPGS--IGRPAPGYEVRIVDDDGQELPAGEPGELV 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  813 ---TGGDGLARGYHERPDQTAERFvPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQ 889
Cdd:cd05934   277 irgLRGWGFFKGYYNMPEATAEAM-RNGW--------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  890 HPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALP 964
Cdd:cd05934   348 HPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 469-963 1.12e-49

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 186.26  E-value: 1.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  469 PRERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGA 548
Cdd:PRK07656    2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  549 YVPLDPAYPSERLAFLAHDAGVQIVLSAAG-------AEERL-----------GEGPWTVVRL---DEDLGRPDERDAAP 607
Cdd:PRK07656   82 VVPLNTRYTADEAAYILARGDAKALFVLGLflgvdysATTRLpalehvvicetEEDDPHTEKMktfTDFLAAGDPAERAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  608 ndNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG-SSFATFGPDQVFLMMAP--------AAFDAStfeiwgaLLH 678
Cdd:PRK07656  162 --EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADwAEYLGLTEGDRYLAANPffhvfgykAGVNAP-------LMR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  679 GARLVLFPPESptPEEIGRVVREHGVT------TLWLTaplFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPA 752
Cdd:PRK07656  233 GATILPLPVFD--PDEVFRLIETERITvlpgppTMYNS---LLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGV 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  753 LRLINGYGPTENTTFTTCHDVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAER 832
Cdd:PRK07656  308 DIVLTGYGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  833 FVPDPFsgvpgarLYrTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIaredrpG--DKRL 910
Cdd:PRK07656  388 IDADGW-------LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI------GvpDERL 453

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  911 ----VAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK07656  454 gevgKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 498-963 2.71e-49

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: 182.68  E-value: 2.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAA 577
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 gaeerlgegpwtvvrldedlgrpderdaapndnvSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFATFG-PDQV 656
Cdd:cd05935    82 ----------------------------------ELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLtPSDV 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  657 FLMMAPAaFDASTFE--IWGALLHGARLVLFPPESPtpEEIGRVVREHGVTTLWLTAPLFHAV------ADRGLDQLRgv 728
Cdd:cd05935   128 ILACLPL-FHVTGFVgsLNTAVYVGGTYVLMARWDR--ETALELIEKYKVTFWTNIPTMLVDLlatpefKTRDLSSLK-- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  729 rqLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRgmgTGSVPIGKPIANTHVYLLD-EQMNPVPPNA 807
Cdd:cd05935   203 --VLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLR---PKLQCLGIP*FGVDARVIDiETGRELPPNE 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  808 VGELFTGGDGLARGYHERPDQTAERFVPDPfsgvpGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAAL 887
Cdd:cd05935   278 VGEIVVRGPQIFKGYWNRPEETEESFIEIK-----GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242  888 LQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSE--LRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05935   353 YKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEedIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1062-1495 7.05e-49

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: 182.15  E-value: 7.05e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1062 GEMPLTPIQ--RWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFV-AEDG-----MWRARgmps 1133
Cdd:pfam00668    3 DEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGepvqvILEER---- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1134 ggPVPYEVVDLSELPGEERRAALEARAAEAQAS-LDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLA 1212
Cdd:pfam00668   79 --PFELEIIDISDLSESEEEEAIEAFIQRDLQSpFDLEKGPLFRAGLFRIAENR-HHLLLSMHHIIVDGVSLGILLRDLA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1213 TAHRQLVEGEIVRLPSKtTSLRRWGERLLATVD-EVVAAELPFW-EALDG-QGVRPLPRGCEPAEDREGDAQTVEVWLgG 1289
Cdd:pfam00668  156 DLYQQLLKGEPLPLPPK-TPYKDYAEWLQQYLQsEDYQKDAAYWlEQLEGeLPVLQLPKDYARPADRSFKGDRLSFTL-D 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1290 PETEALLGRVGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREElfPDIEvaRTVGWFTTIHPVVL-PGRPQSA 1368
Cdd:pfam00668  234 EDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIE--RMVGMFVNTLPLRIdPKGGKTF 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1369 GARLKAVKEAIRRVPKH-GIGYGILRYLGSDEVVTRLARLPAPEVAF-NYLGRLDRALPKDgpfvmaPEAAGPSVSP--R 1444
Cdd:pfam00668  310 SELIKRVQEDLLSAEPHqGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQDSQEEEFQ------LSELDLSVSSviE 383

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 260177242  1445 GKRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAH 1495
Cdd:pfam00668  384 EEAKYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAH 434
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 499-965 4.49e-48

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: 179.62  E-value: 4.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  499 SYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLsaag 578
Cdd:cd05969     2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  579 AEERLGEgpwtvvrldedlgrpderdaapndNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV-RLVRGSSFATFGPDQVF 657
Cdd:cd05969    78 TTEELYE------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIfYYFTGKYVLDLHPDDIY 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  658 LMMAPAAFDASTFE-IWGALLHGARLVLFPPESpTPEEIGRVVREHGVtTLWLTAPL-FHAVADRGLDQLR-----GVRQ 730
Cdd:cd05969   134 WCTADPGWVTGTVYgIWAPWLNGVTNVVYEGRF-DAESWYGIIERVKV-TVWYTAPTaIRMLMKEGDELARkydlsSLRF 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  731 LLAGGDVLSPKHVA--RVLLGLPALrliNGYGPTENTTFTTCHDVSRGMGTGSvpIGKPIANTHVYLLDEQMNPVPPNAV 808
Cdd:cd05969   212 IHSVGEPLNPEAIRwgMEVFGVPIH---DTWWQTETGSIMIANYPCMPIKPGS--MGKPLPGVKAAVVDENGNELPPGTK 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  809 GELFTGGD--GLARGYHERPDQTAERFVPDpfsgvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAA 886
Cdd:cd05969   287 GILALKPGwpSMFRGIWNDEERYKNSFIDG---------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  887 LLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFS---ELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05969   358 LMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437


                  ..
gi 260177242  964 PA 965
Cdd:cd05969   438 KA 439
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 497-958 6.67e-48

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: 178.73  E-value: 6.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  497 VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFlahdagvqiVLSA 576
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAF---------ILRR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  577 AGAEERLGEGPWTVVRLDEDlgrPDErdaapndnvsaenLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG-SSFATFGPDQ 655
Cdd:cd05903    72 AKAKVFVVPERFRQFDPAAM---PDA-------------VALLLFTSGTTGEPKGVMHSHNTLSASIRQyAERLGLGPGD 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  656 VFLMMAPAA-FDASTFEIWGALLHGARLVLFppESPTPEEIGRVVREHGVTTLwLTAPLFHA----VADRGLDQLRGVRQ 730
Cdd:cd05903   136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ--DIWDPDKALALMREHGVTFM-MGATPFLTdllnAVEEAGEPLSRLRT 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  731 LLAGGDVLsPKHVARVLLGLPALRLINGYGPTEN---TTFTTCHDVSRGMGTGsvpiGKPIANTHVYLLDEQMNPVPPNA 807
Cdd:cd05903   213 FVCGGATV-PRSLARRAAELLGAKVCSAYGSTECpgaVTSITPAPEDRRLYTD----GRPLPGVEIKVVDDTGATLAPGV 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  808 VGELFTGGDGLARGYHERPDQTAeRFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDgQVKIR-GFRIELAEVEAA 886
Cdd:cd05903   288 EGELLSRGPSVFLGYLDRPDLTA-DAAPEGW--------FRTGDLARLDEDGYLRITGRSK-DIIIRgGENIPVLEVEDL 357

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260177242  887 LLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLL-QRLPDHMIPAAVVALDKLPLVPSGKL 958
Cdd:cd05903   358 LLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 498-963 8.07e-48

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: 178.30  E-value: 8.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLsaa 577
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 gaeerlgegpwtvvrldedlgrpderdaapndnVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQV 656
Cdd:cd05972    78 ---------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLgLRPDDI 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  657 FLMMA-PAAFDASTFEIWGALLHGARLVLFPPESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLR--GVRQLLA 733
Cdd:cd05972   125 HWNIAdPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKfsHLRLVVS 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  734 GGDVLSPKHVARVL--LGLPalrLINGYGPTENT-TFTTCHDVSrgMGTGSvpIGKPIANTHVYLLDEQMNPVPPNAVGE 810
Cdd:cd05972   205 AGEPLNPEVIEWWRaaTGLP---IRDGYGQTETGlTVGNFPDMP--VKPGS--MGRPTPGYDVAIIDDDGRELPPGEEGD 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  811 LF--TGGDGLARGYHERPDQTAERFVPDpfsgvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALL 888
Cdd:cd05972   278 IAikLPPPGLFLGYVGDPEKTEASIRGD---------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALL 348

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  889 QHPALREAVVIAREDrPGDKRLV-AYVVGREAEVPRFS---ELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05972   349 EHPAVAEAAVVGSPD-PVRGEVVkAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 4-438 2.56e-47

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: 176.84  E-value: 2.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSL--ADVSAVDF 81
Cdd:cd19540     1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   82 GVTDGsswDEPTAAAWLQAEAARPFDLRAGA-LRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:cd19540    81 TVVDV---TEDELAARLAEAARRGFDLTAELpLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWHRDLLASDD-----ASALVREWAAMVGDLDvsTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMD 235
Cdd:cd19540   158 PDWAPLPVQYADYALWQRELLGDEDdpdslAARQLAYWRETLAGLP--EELELPTDRPRPAVASYRGGTVEFTIDAELHA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  236 RVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRN 315
Cdd:cd19540   236 RLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  316 A-LRVTAKlQSVPLSRLAEQCRVPKSPGRMPLVQAV--FQEirsfNEAIRPEGFGhmLRWSRGPLGFEVevpselgSQLD 392
Cdd:cd19540   316 TdLAAFAH-QDVPFERLVEALNPPRSTARHPLFQVMlaFQN----TAAATLELPG--LTVEPVPVDTGV-------AKFD 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 260177242  393 L-----EVRCYDFFSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19540   382 LsftltERRDADGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVAD 432
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 7-247 4.63e-47

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 169.83  E-value: 4.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    7 LSEGQRSLWlaqELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGVTDG 86
Cdd:COG4908     1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   87 SSWDEPTAAAWLQAE----AARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRAA 161
Cdd:COG4908    78 SALPEPEREAELEELvaeeASRPFDLARGPLlRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  162 TLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLdvSTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRESA 241
Cdd:COG4908   158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGA--PPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA 235


                  ....*.
gi 260177242  242 RAEGVT 247
Cdd:COG4908   236 KAHGAT 241
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 2015-2430 5.45e-47

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: 178.48  E-value: 5.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPvcivtder 2094
Cdd:cd17647    22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKP-------- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2095 hlgaveiaarqlgiehvvsldgdgkdadgnvvihgrRALADLADGNLprAAGPHNMAYVIFTSGSTGTPKGVVERHSQVI 2174
Cdd:cd17647    94 ------------------------------------RGLIVIRAAGV--VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2175 NLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQLV 2254
Cdd:cd17647   136 YYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLT 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2255 PyfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDGI--DPRWTS-----IPYGRPI 2327
Cdd:cd17647   216 A--QATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRssDPTFLKnlkdvMPAGRGM 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2328 QNARYYVLDRSGNP--CPIGVTGDLYIGGTCVSFGYYADPSQTAERFV------PD--------------PFSGEPGARL 2385
Cdd:cd17647   294 LNVQLLVVNRNDRTqiCGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvePDhwnyldkdnnepwrQFWLGPRDRL 373

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 260177242 2386 YRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd17647   374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHP 418
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 6-438 2.31e-46

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: 174.04  E-value: 2.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    6 PLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGVTD 85
Cdd:cd20484     3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   86 GSSWDEPTAAAWLQAEAARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRAATLT 164
Cdd:cd20484    83 ISSLKESEIIAYLREKAKEPFVLENGPLmRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  165 PISRGFRDYLVWHRDLLASDDASALVREWAAMV-GDLDVstpLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRESARA 243
Cdd:cd20484   163 SSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLsGTLPI---LELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  244 EGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRVTAKL 323
Cdd:cd20484   240 QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDH 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  324 QSVPLSRLAEQCRVPKSPGRMPLVQAVFqeirSFNEAIRPEGFGHMLRWSRGPLGFEV--EVPSELGSQLDLEVrcYDFF 401
Cdd:cd20484   320 AAYPFPAMVRDLNIPRSQANSPVFQVAF----FYQNFLQSTSLQQFLAEYQDVLSIEFveGIHQEGEYELVLEV--YEQE 393

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 260177242  402 SSSVRTCwRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd20484   394 DRFTLNI-KYNPDLFDASTIERMMEHYVKLAEELIAN 429
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 482-963 8.58e-46

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: 174.35  E-value: 8.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSN--VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSE 559
Cdd:cd05904    15 ASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  560 RLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERD---------AAPNDNVSAENLAYVMYTSGSTGKPK 630
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSdllfeadeaEPPVVVIKQDDVAALLYSSGTTGRSK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  631 GVAVTHRNVVRLVRGSSFA---TFGPDQVFLMMAPaafdasTFEIWG------ALLH-GARLVLFPP-ESptpEEIGRVV 699
Cdd:cd05904   175 GVMLTHRNLIAMVAQFVAGegsNSDSEDVFLCVLP------MFHIYGlssfalGLLRlGATVVVMPRfDL---EELLAAI 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  700 REHGVTTLWLTAPLFHAVADRGLD---QLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRG 776
Cdd:cd05904   246 ERYKVTHLPVVPPIVLALVKSPIVdkyDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEK 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  777 MGTGSVPIGKPIANTHVYLLD-EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARY 855
Cdd:cd05904   326 DRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW--------LHTGDLCYI 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  856 LPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGR------EAEVPRF----- 924
Cdd:cd05904   398 DEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKpgssltEDEIMDFvakqv 477

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 260177242  925 ---SELRKfllqrlpdhmipaaVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05904   478 apyKKVRK--------------VAFVDAIPKSPSGKILRKEL 505
PRK05691 PRK05691
peptide synthase; Validated
 474-1378 1.85e-45

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 182.68  E-value: 1.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVAL------DAGSNVVSYGELNRRADKLAHMLRLKGVGTEtRVGLCLERSVELVVGILGVLKAGG 547
Cdd:PRK05691   11 LVQALQRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARASFGD-RAVLLFPSGPDYVAAFFGCLYAGV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  548 AYVPldpAYPSE--------RLAFLAHDAGVQIVLSAA-------GAEERLGEGPWTVVRLDEDLGRPDERDAAPNdnVS 612
Cdd:PRK05691   90 IAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLTVAdlrdsllQMEELAAANAPELLCVDTLDPALAEAWQEPA--LQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  613 AENLAYVMYTSGSTGKPKGVAVTHRNVV---RLVRGSSFATFGPDQVFLMMAPAAFDAStfeIWGALLH----GARLVLF 685
Cdd:PRK05691  165 PDDIAFLQYTSGSTALPKGVQVSHGNLVaneQLIRHGFGIDLNPDDVIVSWLPLYHDMG---LIGGLLQpifsGVPCVLM 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  686 PPESptpeEIGRVVRehgvttlWLTA-----------PLF------HAVADRGLDQL--RGVRQLLAGGDVLSPKHVARV 746
Cdd:PRK05691  242 SPAY----FLERPLR-------WLEAiseyggtisggPDFayrlcsERVSESALERLdlSRWRVAYSGSEPIRQDSLERF 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  747 L-----LGLPALRLINGYGPTENTTFTTCHDVSRGM-----------------GTGSVPI--GKPIANTHVYLLDEQ-MN 801
Cdd:PRK05691  311 AekfaaCGFDPDSFFASYGLAEATLFVSGGRRGQGIpaleldaealarnraepGTGSVLMscGRSQPGHAVLIVDPQsLE 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  802 PVPPNAVGELFTGGDGLARGYHERPDQTAERFVPdpfsgVPGARLYRTGDLArYLPNGDMEFLGRRDGQVKIRGFRIELA 881
Cdd:PRK05691  391 VLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE-----HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQ 464

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  882 EVEAALLqhpalREAVVIaredRPGdkRLVAYVV---GRE-----AEVPRF-------SELRKFLLQRLPD--HMIPAAV 944
Cdd:PRK05691  465 DIEKTVE-----REVEVV----RKG--RVAAFAVnhqGEEgigiaAEISRSvqkilppQALIKSIRQAVAEacQEAPSVV 533

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  945 VALD--KLPLVPSGKLDRRA----LPAPTL-------SGRSGPFVAPEGHPEEVLARI---WERVLRVDAVGREDNFFEL 1008
Cdd:PRK05691  534 LLLNpgALPKTSSGKLQRSAcrlrLADGSLdsyalfpALQAVEAAQTAASGDELQARIaaiWCEQLKVEQVAADDHFFLL 613

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1009 GGDSILAIQVVAGARE-VDLKLTVRQIFTHPTLSSLAAAAQATAVSG-EDQGEIT-----GEMPLTPIQR-----WFLSG 1076
Cdd:PRK05691  614 GGNSIAATQVVARLRDeLGIDLNLRQLFEAPTLAAFSAAVARQLAGGgAAQAAIArlprgQALPQSLAQNrlwllWQLDP 693

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1077 EPAAphhFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSgGPVPYEVVDLSELPGEERRAAL 1156
Cdd:PRK05691  694 QSAA---YNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQ-GEFALQRIDLSDLPEAEREARA 769

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1157 EAR-AAEAQASLDLTDGPILRVVQFRLGPgEPDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEG---EIVRLPSKTTS 1232
Cdd:PRK05691  770 AQIrEEEARQPFDLEKGPLLRVTLVRLDD-EEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGqtaELAPLPLGYAD 848

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1233 LRRWGERLLAtvDEVVAAELPFWEAL--DGQGVRPLPRGCEPAEDREGDAQTVEVWLGGPETEALLGrVGEAYRTRADEV 1310
Cdd:PRK05691  849 YGAWQRQWLA--QGEAARQLAYWKAQlgDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRG-LAQAHQATLFMV 925

                         970       980       990      1000      1010      1020      1030
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260177242 1311 ILAALAGALTEWAGGEAAYVAVEGHGReelfPDIEVARTVGWFttIHPVVLPGRP---QSAGARLKAVKEA 1378
Cdd:PRK05691  926 LLAAFQALLHRYSGQGDIRIGVPNANR----PRLETQGLVGFF--INTQVLRAQLdgrLPFTALLAQVRQA 990
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 4-438 1.32e-43

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: 166.05  E-value: 1.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQS-LADVSAVDFG 82
Cdd:cd19066     1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVvLDKTVRFRIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   83 VTDGSSWDEPTAAAWLQA--EAARPFDLRAG-ALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGR 159
Cdd:cd19066    81 IIDLRNLADPEARLLELIdqIQQTIYDLERGpLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  160 AATLTPISRgFRDYLVWHRDLLASDDASALVREWAAMVGDLdvSTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRE 239
Cdd:cd19066   161 PTLPPPVGS-YADYAAWLEKQLESEAAQADLAYWTSYLHGL--PPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLRE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  240 SARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRV 319
Cdd:cd19066   238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  320 TAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSFNEAIRPEGFGHMlrwsrgplgfEVEVPSELGSQLDLEVRCYD 399
Cdd:cd19066   318 AIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFT----------TPVYTSSEGTVFDLDLEASE 387

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 260177242  400 FFSSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19066   388 DPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIEN 426
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 490-963 1.41e-43

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: 166.10  E-value: 1.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  490 ALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAG 569
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  570 VQIVLsaagaeerlgegpwtvvrldedlgrpderdaapndnVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFA 649
Cdd:cd05919    83 ARLVV------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMARE 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  650 TFG--PDQVFLMMAPAAFDAST-FEIWGALLHGARLVLFPpESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGL---D 723
Cdd:cd05919   127 ALGltPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNP-GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAgspD 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  724 QLRGVRQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTENT-TFTTCHDVSRGMGTgsvpIGKPIANTHVYLLDEQMNP 802
Cdd:cd05919   206 ALRSLRLCVSAGEAL-PRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPGAWRLGS----TGRPVPGYEIRLVDEEGHT 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  803 VPPNAVGELFTGGDGLARGYHERPDQTAERFVpdpfsgvpgARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAE 882
Cdd:cd05919   281 IPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN---------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  883 VEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFS---ELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLD 959
Cdd:cd05919   352 VESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431


                  ....
gi 260177242  960 RRAL 963
Cdd:cd05919   432 RFKL 435
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1063-1495 1.69e-43

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: 165.66  E-value: 1.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1063 EMPLTPIQRWFLSGEPAA--PHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDG-MWRARGMPSGGPVPY 1139
Cdd:cd19066     1 KIPLSPMQRGMWFLKKLAtdPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGrYEQVVLDKTVRFRIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1140 EvVDLSELPGEERRAALEARAAEAQAsLDLTDGPILRVVQFRLGPgEPDRLLVVVHHLAVDVVSWGILLADLATAHRQLV 1219
Cdd:cd19066    81 I-IDLRNLADPEARLLELIDQIQQTI-YDLERGPLVRVALFRLAD-ERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1220 EGEIVrLPSKTTSLRRWGERL-LATVDEVVAAELPFWEALDGQGVRPLPRGCEPAEDREGDAQ--TVEVWLGGPETEALL 1296
Cdd:cd19066   158 RQKPT-LPPPVGSYADYAAWLeKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEvlTLEFFLRSEETKRLR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1297 GRVGEAYRTRADeVILAALAGALTEWAGGEAAYVAVEGHGReelfPDIEVARTVGWFTTIHPVVLP-GRPQSAGARLKAV 1375
Cdd:cd19066   237 EVARESGTTPTQ-LLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDtSPDATFPELLKRT 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1376 KEAIRRVPKHGIGYGILRYLGSDEVVTrLARLPAPEVAFNYLGR-LDRALPKDGPFVMapeaagPSVSPRGKRSHALQTM 1454
Cdd:cd19066   312 KEQSREAIEHQRVPFIELVRHLGVVPE-APKHPLFEPVFTFKNNqQQLGKTGGFIFTT------PVYTSSEGTVFDLDLE 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 260177242 1455 VVAEPQG-LRTRFAFQPKRHSHEEIARLAARYGQLLEELIAH 1495
Cdd:cd19066   385 ASEDPDGdLLLRLEYSRGVYDERTIDRFAERYMTALRQLIEN 426
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 467-963 2.55e-43

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 168.21  E-value: 2.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  467 DYPRERCLHHLfEEEARRVPDAVALDAGSNVVSYGELNRRADKLA-HMLRLKGVGTETRVGLCLERSVELVVGILGVLKA 545
Cdd:PRK08314    6 TLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAgYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  546 GGAYVPLDPAYPSERLAFLAHDAG--VQIVLS-----AAGAEERLGEG--------------------PWTVVRLDEDLG 598
Cdd:PRK08314   85 NAVVVPVNPMNREEELAHYVTDSGarVAIVGSelapkVAPAVGNLRLRhvivaqysdylpaepeiavpAWLRAEPPLQAL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  599 RP----------DERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSF-ATFGPDQVFLMMAPaafda 667
Cdd:PRK08314  165 APggvvawkealAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLwSNSTPESVVLAVLP----- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  668 sTFEIWG-------ALLHGARLVLFPPESptPEEIGRVVREHGVtTLWLTAPL----FHA---VADRGLDQLRGVRqlla 733
Cdd:PRK08314  240 -LFHVTGmvhsmnaPIYAGATVVLMPRWD--REAAARLIERYRV-THWTNIPTmvvdFLAspgLAERDLSSLRYIG---- 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  734 GGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRgmgtgsvP----IGKPIANTHVYLLD-EQMNPVPPNAV 808
Cdd:PRK08314  312 GGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDR-------PklqcLGIPTFGVDARVIDpETLEELPPGEV 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  809 GELFTGGDGLARGYHERPDQTAERFVPdpfsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALL 888
Cdd:PRK08314  385 GEIVVHGPQVFKGYWNRPEATAEAFIE-----IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLY 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  889 QHPALREAVVIA-REDRPGDkRLVAYVVGREAEVPRFSELRkfLLQRLPDHM----IPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK08314  460 KHPAIQEACVIAtPDPRRGE-TVKAVVVLRPEARGKTTEEE--IIAWAREHMaaykYPRIVEFVDSLPKSGSGKILWRQL 536
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 495-963 8.30e-43

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: 163.76  E-value: 8.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  495 SNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFlahdagvqivl 574
Cdd:cd05971     4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEY----------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  575 saagaeeRLGEGPWTVVRLDEdlgrpderdaapndnvsAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFA-TFGP 653
Cdd:cd05971    73 -------RLSNSGASALVTDG-----------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPfNLFP 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  654 DQVFLMMAPAAfdastfeiWG-----------ALLHGARLVLFPPESPTPEEIGRVVREHGVTTLWLTAP---LFHAVAD 719
Cdd:cd05971   129 RDGDLYWTPAD--------WAwigglldvllpSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkMMRQQGE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  720 RGLDQLRGVRQLLAGGDVLSPKHV--ARVLLGLPALRLingYGPTE-NTTFTTCHDVsrgMGTGSVPIGKPIANTHVYLL 796
Cdd:cd05971   201 QLKHAQVKLRAIATGGESLGEELLgwAREQFGVEVNEF---YGQTEcNLVIGNCSAL---FPIKPGSMGKPIPGHRVAIV 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  797 DEQMNPVPPNAVGELftggdGLAR-------GYHERPDQTAERFVPDPFsgvpgarlyRTGDLARYLPNGDMEFLGRRDG 869
Cdd:cd05971   275 DDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL---------LTGDLGRKDSDGYFWYVGRDDD 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPR---FSELRKFLLQRLPDHMIPAAVVA 946
Cdd:cd05971   341 VITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEF 420

                         490
                  ....*....|....*..
gi 260177242  947 LDKLPLVPSGKLDRRAL 963
Cdd:cd05971   421 VNELPRTATGKIRRREL 437
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 2151-2431 2.50e-42

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: 159.37  E-value: 2.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 AYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDlrsPER 2230
Cdd:cd04433     3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2231 LAAELGRGTITFWDSAPAALQQLV--PYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEATVWSNY 2308
Cdd:cd04433    80 ALELIEREKVTILLGVPTLLARLLkaPESAG-YDLSSLRALVSGGAPLPPELLERFEEAP-GIKLVNGYGLTETGGTVAT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2309 FEVDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFvpdpfsgEPGarLYRT 2388
Cdd:cd04433   158 GPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDG--WYRT 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 260177242 2389 GDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd04433   227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPG 269
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 460-961 2.88e-42

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 165.56  E-value: 2.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  460 EWNQTASDYPRErCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGI 539
Cdd:PRK05605   21 PWTPHDLDYGDT-TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  540 LGVLKAGGAYVPLDPAYPSERLA--FLAHDAGVQIVLS-AAGAEERLGE--GPWTVVRLD-------------------- 594
Cdd:PRK05605  100 YAVLRLGAVVVEHNPLYTAHELEhpFEDHGARVAIVWDkVAPTVERLRRttPLETIVSVNmiaampllqrlalrlpipal 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  595 -----------------EDL---GRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV-RLVRGSSFATFGP 653
Cdd:PRK05605  180 rkaraaltgpapgtvpwETLvdaAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQGKAWVPGLG 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  654 DQ--VFLMMAPaafdasTFEIWG-------ALLHGARLVLFPpeSPTPEEIGRVVREHGVTtlWLTA--PLFHAVAD--- 719
Cdd:PRK05605  260 DGpeRVLAALP------MFHAYGltlcltlAVSIGGELVLLP--APDIDLILDAMKKHPPT--WLPGvpPLYEKIAEaae 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  720 -RGLDqLRGVRQLLAGGDVLSPKHVARvLLGLPALRLINGYGPTENTTFTTCHDVS--RGMGTgsvpIGKPIANTHVYLL 796
Cdd:PRK05605  330 eRGVD-LSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIVGNPMSddRRPGY----VGVPFPDTEVRIV 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  797 DEQmNP---VPPNAVGELFTGGDGLARGYHERPDQTAERFVPDpfsgvpgarLYRTGDLARylpngdMEflgrRDGQVKI 873
Cdd:PRK05605  404 DPE-DPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG---------WFRTGDVVV------ME----EDGFIRI 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  874 R----------GFRIELAEVEAALLQHPALREAVV--IAREDrpGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIP 941
Cdd:PRK05605  464 VdrikeliitgGFNVYPAEVEEVLREHPGVEDAAVvgLPRED--GSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVP 541

                         570       580
                  ....*....|....*....|
gi 260177242  942 AAVVALDKLPLVPSGKLDRR 961
Cdd:PRK05605  542 RRFYHVDELPRDQLGKVRRR 561
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1990-2431 3.83e-42

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 164.90  E-value: 3.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1990 HELFESSVERSPGSVALCYDGVPP----LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAY 2065
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGEDGeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2066 VPLDPRWPLERVAAVLGTTRPVCIVTDER---------HLGAVEIAARQL-GIEHVVSLDGDGKDADGNVVIHGRRALAD 2135
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELpSLEHVIVVGRTGADVPMEGDLDWDELLAA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2136 LADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYL-VGPSDRLLFVTSPSF--DLSvYDVFGMLA 2212
Cdd:COG0365   172 ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLdLKPGDVFWCTADIGWatGHS-YIVYGPLL 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2213 AGGSIhIASED--DLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEDG---SQLRLAFLSG--------DWVpig 2279
Cdd:COG0365   251 NGATV-VLYEGrpDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydlSSLRLLGSAGeplnpevwEWW--- 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2280 mldelRRAFpNVKLV-GLGGaTEaTVW---SNYfevDGIDPRWTSIpyGRPI--QNARyyVLDRSGNPCPIGVTGDLYIG 2353
Cdd:COG0365   327 -----YEAV-GVPIVdGWGQ-TE-TGGifiSNL---PGLPVKPGSM--GKPVpgYDVA--VVDEDGNPVPPGEEGELVIK 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2354 GTCVSF--GYYADPSQTAERFvpdpFSGEPGarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:COG0365   392 GPWPGMfrGYWNDPERYRETY----FGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 474-966 3.97e-42

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 162.85  E-value: 3.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALdaGSNVVSYGELNRRADKLAHmlRLKGVGtetRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:PRK07787    4 LNPAAVAAAADIADAVRI--GGRVLSRSDLAGAATAVAE--RVAGAR---RVAVLATPTLATVLAVVGALIAGVPVVPVP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 P-AYPSERlaflAHdagvqiVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGV 632
Cdd:PRK07787   77 PdSGVAER----RH------ILADSGAQAWLGPAPDDPAGLPHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  633 AVTHRNVVRLVRGSSFA-TFGPDQVFLMMAPaafdasTFE-------IWGALLHGARLVLFPpeSPTPEEIGRVVREHGv 704
Cdd:PRK07787  147 VLSRRAIAADLDALAEAwQWTADDVLVHGLP------LFHvhglvlgVLGPLRIGNRFVHTG--RPTPEAYAQALSEGG- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  705 tTLWLTAP-LFHAVADRG--LDQLRGVRQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTEN-TTFTTCHDVSRGMGTg 780
Cdd:PRK07787  218 -TLYFGVPtVWSRIAADPeaARALRGARLLVSGSAAL-PVPVFDRLAALTGHRPVERYGMTETlITLSTRADGERRPGW- 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  781 svpIGKPIANTHVYLLDEQMNPVP--PNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPN 858
Cdd:PRK07787  295 ---VGLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTADGW--------FRTGDVAVVDPD 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  859 GDMEFLGRRDGQ-VKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPrfSELRKFLLQRLPD 937
Cdd:PRK07787  364 GMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA--DELIDFVAQQLSV 441

                         490       500
                  ....*....|....*....|....*....
gi 260177242  938 HMIPAAVVALDKLPLVPSGKLDRRALPAP 966
Cdd:PRK07787  442 HKRPREVRFVDALPRNAMGKVLKKQLLSE 470
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1537-1954 5.30e-42

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: 161.39  E-value: 5.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1537 PLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVPEPLQVVRRLVRIPTERI 1616
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1617 DARSMAVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQHEA 1696
Cdd:cd19539    83 DLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1697 AHRTAPR-PHRDYVAWLR---GADAQSVE-RFWRRELGGFrEVTPLGIDRPPAGQRASSYRRFERALDEHTTARLEQVLR 1771
Cdd:cd19539   163 APLPELRqQYKEYAAWQRealAAPRAAELlDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1772 ERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPleGIERMVGLFINTVPMRAVVDPERPIGEWLteLQGRRAER 1851
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLI--ARVRKALV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1852 TAYEHASL--AQVQAWSEVPHGSALFESLIVVENYPVAPAFSGDELSVRLVGGDEQ----TNYPVTL-VALPGRRLTLRL 1924
Cdd:cd19539   318 DAQRHQELpfQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDipdgAKFDLNLtVTEEGTGLRGSL 397

                         410       420       430
                  ....*....|....*....|....*....|
gi 260177242 1925 LYEAERIPDGAAEGVLSHLESLLCAIADDP 1954
Cdd:cd19539   398 GYATSLFDEETIQGFLADYLQVLRQLLANP 427
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 2013-2423 1.41e-41

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: 160.72  E-value: 1.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2013 PLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTD 2092
Cdd:cd17654    16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ERhlgaVEIAARQLGIEHVVSldgdgkdadgnvvihgrraladladgNLPRaagPHNMAYVIFTSGSTGTPKGVVERHSQ 2172
Cdd:cd17654    96 KE----LDNAPLSFTPEHRHF--------------------------NIRT---DECLAYVIHTSGTTGTPKIVAVPHKC 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2173 VINLIEWVNRTYLVGPSDrLLFVTSP-SFDLSVYDVFGMLAAGGSIhIASEDDLRS-PERLAAEL-GRGTITFWDSAPAA 2249
Cdd:cd17654   143 ILPNIQHFRSLFNITSED-ILFLTSPlTFDPSVVEIFLSLSSGATL-LIVPTSVKVlPSKLADILfKRHRITVLQATPTL 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2250 LQQL---VPYFDRIEDGSQLRLAFLSGDWVPIGMLDE-LRRAFPNVKLVGLGGATEATVWSNYFEVDGIDprwTSIPYGR 2325
Cdd:cd17654   221 FRRFgsqSIKSTVLSATSSLRVLALGGEPFPSLVILSsWRGKGNRTRIFNIYGITEVSCWALAYKVPEED---SPVQLGS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2326 PIQNARYYVLDRSGNPcpigVTGDLYIGGtcVSFGYyadpsqtaerFVPDPFSGePGARLYRTGDLARfFRDGNIEFLGR 2405
Cdd:cd17654   298 PLLGTVIEVRDQNGSE----GTGQVFLGG--LNRVC----------ILDDEVTV-PKGTMRATGDFVT-VKDGELFFLGR 359

                         410
                  ....*....|....*...
gi 260177242 2406 ADSQVKIRGYRIECGEVE 2423
Cdd:cd17654   360 KDSQIKRRGKRINLDLIQ 377
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 482-963 6.37e-40

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 157.40  E-value: 6.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLSAAG----AEERLGEGPWTVVRLDEDLGRPD--------------ERDAAPNDNVSAENLAYVMYTS 623
Cdd:PRK08316  101 AYILDHSGARAFLVDPAlaptAEAALALLPVDTLILSLVLGGREapggwldfadwaeaGSVAEPDVELADDDLAQILYTS 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  624 GSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVFLMMAP----AAFDASTFEIwgaLLHGARLVLFPpeSPTPEEIGRV 698
Cdd:PRK08316  181 GTESLPKGAMLTHRALIAEYVSCIVAGdMSADDIPLHALPlyhcAQLDVFLGPY---LYVGATNVILD--APDPELILRT 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  699 VREHGVT------TLW---LTAPLFhAVADrgldqLRGVRQLLAGGDVLsPKHVARVLLG-LPALRLINGYGPTENTTFT 768
Cdd:PRK08316  256 IEAERITsffappTVWislLRHPDF-DTRD-----LSSLRKGYYGASIM-PVEVLKELRErLPGLRFYNCYGQTEIAPLA 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TC---HDVSRGMGTGsvpiGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgar 845
Cdd:PRK08316  329 TVlgpEEHLRRPGSA----GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF------- 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  846 lyRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFS 925
Cdd:PRK08316  398 --HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED 475

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 260177242  926 ELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK08316  476 ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 499-963 9.90e-40

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: 154.98  E-value: 9.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  499 SYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAG 578
Cdd:cd05973     2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  579 AEERLGEGPWTVvrldedlgrpderdaapndnvsaenlayvMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVF 657
Cdd:cd05973    82 NRHKLDSDPFVM-----------------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVdLRPEDSF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  658 LMMA-PAAFDASTFEIWGALLHGARLVLFppESP-TPEEIGRVVREHGVTTL---------WLTAPLfhAVADRGLDQLR 726
Cdd:cd05973   133 WNAAdPGWAYGLYYAITGPLALGHPTILL--EGGfSVESTWRVIERLGVTNLagsptayrlLMAAGA--EVPARPKGRLR 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  727 GVRqllAGGDVLSPKHV--ARVLLGLPalrLINGYGPTENTTF-TTCHDVSRGMGTGSVpiGKPIANTHVYLLDEQMNPV 803
Cdd:cd05973   209 RVS---SAGEPLTPEVIrwFDAALGVP---IHDHYGQTELGMVlANHHALEHPVHAGSA--GRAMPGWRVAVLDDDGDEL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  804 PPNAVGELFTGGDGLA----RGYHERPDQTaerfvpdpfsgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIE 879
Cdd:cd05973   281 GPGEPGRLAIDIANSPlmwfRGYQLPDTPA------------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  880 LAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVV---GREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSG 956
Cdd:cd05973   349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428


                  ....*..
gi 260177242  957 KLDRRAL 963
Cdd:cd05973   429 KIQRFLL 435
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 492-963 1.53e-39

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: 156.25  E-value: 1.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  492 DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVG-LCLE--RSVELVVGILGvlkAGGAYVPLDPAYPSERLAFLAHDA 568
Cdd:cd12119    20 EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVAtLAWNthRHLELYYAVPG---MGAVLHTINPRLFPEQIAYIINHA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  569 GVQIVLsAAGAEERLGE---GPWTVVRLDEDLGRPDERDAAPNDNVSA------------------ENLAYVM-YTSGST 626
Cdd:cd12119    97 EDRVVF-VDRDFLPLLEaiaPRLPTVEHVVVMTDDAAMPEPAGVGVLAyeellaaespeydwpdfdENTAAAIcYTSGTT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  627 GKPKGVAVTHRNVVrL----VRGSSFATFGPDQVFLMMAPAaFDASTfeiWG----ALLHGARLVLfPPESPTPEEIGRV 698
Cdd:cd12119   176 GNPKGVVYSHRSLV-LhamaALLTDGLGLSESDVVLPVVPM-FHVNA---WGlpyaAAMVGAKLVL-PGPYLDPASLAEL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  699 VRE------HGVTTLWLTapLFHAVADRGLDQLrGVRQLLAGGDVLsPKHVARVLLGLpALRLINGYGPTENTTFTTCHD 772
Cdd:cd12119   250 IERegvtfaAGVPTVWQG--LLDHLEANGRDLS-SLRRVVIGGSAV-PRSLIEAFEER-GVRVIHAWGMTETSPLGTVAR 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  773 VSRGMGTGSVP--------IGKPIANTHVYLLDEQMNPVP--PNAVGELFTGGDGLARGYHeRPDQTAERFVPDPFsgvp 842
Cdd:cd12119   325 PPSEHSNLSEDeqlalrakQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYY-KNDEESEALTEDGW---- 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  843 garlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVP 922
Cdd:cd12119   400 ----LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATV 475

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 260177242  923 RFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd12119   476 TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 482-962 1.20e-38

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: 153.93  E-value: 1.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVAL------DAGSNVVSYGELNRRADKLAHMLRLKGvGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPA 555
Cdd:cd05931     3 AAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  556 YPS---ERLAFLAHDAGVQIVLSAAGAEERLGEGPW------TVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGST 626
Cdd:cd05931    82 TPGrhaERLAAILADAGPRVVLTTAAALAAVRAFAAsrpaagTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  627 GKPKGVAVTHRNV---VRLVRGSSFATfgPDQVF-----------LMMApaafdastfeIWGALLHGARLVLFPPES--- 689
Cdd:cd05931   162 GTPKGVVVTHRNLlanVRQIRRAYGLD--PGDVVvswlplyhdmgLIGG----------LLTPLYSGGPSVLMSPAAflr 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 -PT--PEEIGRvvreHGVTtlWLTAPLF------HAVADRGLDQLR--GVRQLLAGGDVLSPKHVARVL-----LGLPAL 753
Cdd:cd05931   230 rPLrwLRLISR----YRAT--ISAAPNFaydlcvRRVRDEDLEGLDlsSWRVALNGAEPVRPATLRRFAeafapFGFRPE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  754 RLINGYGPTENTTFTTCHDVSRGM--------------------GTGSVPI---GKPIANTHVYLLDEQMN-PVPPNAVG 809
Cdd:cd05931   304 AFRPSYGLAEATLFVSGGPPGTGPvvlrvdrdalagravavaadDPAARELvscGRPLPDQEVRIVDPETGrELPDGEVG 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  810 ELFTGGDGLARGYHERPDQTAERFvpDPFSGVPGARLYRTGDLArYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQ 889
Cdd:cd05931   384 EIWVRGPSVASGYWGRPEATAETF--GALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEE 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  890 -HPALRE--AVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPD-HMIPAAVVAL---DKLPLVPSGKLDRRA 962
Cdd:cd05931   461 aHPALRPgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAReHGVAPADVVLvrpGSIPRTSSGKIQRRA 540
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1066-1305 1.55e-38

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 145.18  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1066 LTPIQRWFLSGEPAaPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSGgPVPYEVVDLS 1145
Cdd:COG4908     1 LSPAQKRFLFLEPG-SNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDA-DLPLEVVDLS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1146 ELPGEERRAALEARAA-EAQASLDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIV 1224
Cdd:COG4908    79 ALPEPEREAELEELVAeEASRPFDLARGPLLRAALIRLGEDE-HVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1225 RLPSKTTSLRRWGERLLATVD-EVVAAELPFW-EALDGQ-GVRPLPRGCEPAEDREGDAQTVEVWLGGPETEALLgRVGE 1301
Cdd:COG4908   158 PLPELPIQYADYAAWQRAWLQsEALEKQLEYWrQQLAGApPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALK-ALAK 236


                  ....
gi 260177242 1302 AYRT 1305
Cdd:COG4908   237 AHGA 240
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 486-958 5.12e-38

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 152.24  E-value: 5.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:PRK07786   31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLS------AAGAEERLGEGPWTVVRLD----------EDLGRPDERDAAPNDnVSAENLAYVMYTSGSTGKP 629
Cdd:PRK07786  111 SDCGAHVVVTeaalapVATAVRDIVPLLSTVVVAGgssddsvlgyEDLLAEAGPAHAPVD-IPNDSPALIMYTSGTTGRP 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  630 KGVAVTHRNVV----RLVRGSSFATfgPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTPEEIGRVVREHGVT 705
Cdd:PRK07786  190 KGAVLTHANLTgqamTCLRTNGADI--NSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVT 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  706 TLWLTAPLFHAVADRGLDQLRGVR-QLLAGGDVLSPKHVARVLLG-LPALRLINGYGPTENTTfTTC----HDVSRGMGT 779
Cdd:PRK07786  268 GIFLVPAQWQAVCAEQQARPRDLAlRVLSWGAAPASDTLLRQMAAtFPEAQILAAFGQTEMSP-VTCmllgEDAIRKLGS 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  780 gsvpIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLARYLPNG 859
Cdd:PRK07786  347 ----VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF---------HSGDLVRQDEEG 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  860 DMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGR-EAEVPRFSELRKFLLQRLPDH 938
Cdd:PRK07786  414 YVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnDDAALTLEDLAEFLTDRLARY 493

                         490       500
                  ....*....|....*....|
gi 260177242  939 MIPAAVVALDKLPLVPSGKL 958
Cdd:PRK07786  494 KHPKALEIVDALPRNPAGKV 513
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
463-934 1.27e-37

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 151.79  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  463 QTASDYPRERCLHHLFEEEARRVPDAVAL----DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVG 538
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALrekeDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  539 ILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIV-----------LSAAGA----------EERLGEGPWTVVRLDE-- 595
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLfvedqeqldklLEVRDElpslrhivvlDPRGLRDDPRLLSLDEll 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  596 DLGR----PDERDAAPnDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGS-SFATFGPDQVFLMMAPAA--FdAS 668
Cdd:COG1022   162 ALGRevadPAELEARR-AAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALlERLPLGPGDRTLSFLPLAhvF-ER 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  669 TFEIwGALLHGARLVLfpPESptPEEIGRVVREHGVTTLwLTAP-----------------------LF----------- 714
Cdd:COG1022   240 TVSY-YALAAGATVAF--AES--PDTLAEDLREVKPTFM-LAVPrvwekvyagiqakaeeagglkrkLFrwalavgrrya 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  715 ----------------HAVADRGLdqLRGVRQLLaGGDV---------LSPkHVARVL--LGLPalrLINGYGPTENTTF 767
Cdd:COG1022   314 rarlagkspslllrlkHALADKLV--FSKLREAL-GGRLrfavsggaaLGP-ELARFFraLGIP---VLEGYGLTETSPV 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  768 TTCHDVSRgMGTGSVpiGKPIANTHVYLLDEqmnpvppnavGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlY 847
Cdd:COG1022   387 ITVNRPGD-NRIGTV--GPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW--------L 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  848 RTGDLARYLPNGDMEFLGRrdgqVK--IR---GFRIELAEVEAALLQHPALREAVVIaredrpGDKR--LVAYVvgreae 920
Cdd:COG1022   446 HTGDIGELDEDGFLRITGR----KKdlIVtsgGKNVAPQPIENALKASPLIEQAVVV------GDGRpfLAALI------ 509

                         570
                  ....*....|....
gi 260177242  921 VPRFSELRKFLLQR 934
Cdd:COG1022   510 VPDFEALGEWAEEN 523
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 483-971 1.69e-37

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 150.14  E-value: 1.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  483 RRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVG-LCLERSVELVVGILGVLkAGGAYVPLDPAYPSERL 561
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVAlLSLNRPEVLMAIGAAQL-AGLRRTALHPLGSLDDH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLSAAGA-EER---LGEGPWTVVRL--------DEDLG--------RPDERDAAPNDnvsaenLAYVMY 621
Cdd:PRK06188  102 AYVLEDAGISTLIVDPAPfVERalaLLARVPSLKHVltlgpvpdGVDLLaaaakfgpAPLVAAALPPD------IAGLAY 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  622 TSGSTGKPKGVAVTHRNVVRLVRgSSFATFG-PDQV-FLMMAPAAFDASTFeIWGALLHGARLVLFPpeSPTPEEIGRVV 699
Cdd:PRK06188  176 TGGTTGKPKGVMGTHRSIATMAQ-IQLAEWEwPADPrFLMCTPLSHAGGAF-FLPTLLRGGTVIVLA--KFDPAEVLRAI 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  700 REHGVTTLWLTAPLFHAVADRGLDQLRGVRQL---LAGGDVLSPkhvARVLLGLPALRLING--YGPTENTTFTTC---- 770
Cdd:PRK06188  252 EEQRITATFLVPTMIYALLDHPDLRTRDLSSLetvYYGASPMSP---VRLAEAIERFGPIFAqyYGQTEAPMVITYlrkr 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  771 -HDVSRGMGTGSVpiGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFvpdpfsgvPGARLyRT 849
Cdd:PRK06188  329 dHDPDDPKRLTSC--GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--------RDGWL-HT 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  850 GDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRK 929
Cdd:PRK06188  398 GDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQA 477

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 260177242  930 FLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGR 971
Cdd:PRK06188  478 HVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGR 519
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
 1368-1523 4.46e-37

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: 137.79  E-value: 4.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  1368 AGARLKAVKEAIRRVPKHGIGYGILRYLgsDEVVTRLARLPAPEVAFNYLGRLDRALpKDGPFVMAPEAAGPSVSPRGKR 1447
Cdd:TIGR01720    2 LGRLIKAVKEQLRRIPNKGVGYGVLRYL--TEPEEKLAASPQPEISFNYLGQFDADS-NDELFQPSSYSPGEAISPESPR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242  1448 SHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAHAIDvGSEASWTPSDFPLARLEPHVLDAL 1523
Cdd:TIGR01720   79 PYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAG-KEGGGLTPSDFSLKDLTQDELDEL 153
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 464-963 5.69e-37

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 149.05  E-value: 5.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  464 TASDYPRERCLHHLFEEEARRVPDAVALDA------GSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVV 537
Cdd:PRK13295   16 IAAGHWHDRTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  538 GILGVLKAGGAYVPLDPAYPSERLAF-LAH-DAGVQIVLS----------AAGAEERL----------GEGPWTVVRLDE 595
Cdd:PRK13295   96 LYLACSRIGAVLNPLMPIFRERELSFmLKHaESKVLVVPKtfrgfdhaamARRLRPELpalrhvvvvgGDGADSFEALLI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  596 DLGRPDERDAAP---NDNVSAENLAYVMYTSGSTGKPKGVAVTHR----NVVRLVRGSSFatfGPDQVFLMMAPAAFdaS 668
Cdd:PRK13295  176 TPAWEQEPDAPAilaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANtlmaNIVPYAERLGL---GADDVILMASPMAH--Q 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  669 TFEIWGALLH---GARLVLfpPESPTPEEIGRVVREHGVTTLWLTAPLFH----AVADRGLDqLRGVRQLLAGGDVLSPK 741
Cdd:PRK13295  251 TGFMYGLMMPvmlGATAVL--QDIWDPARAAELIRTEGVTFTMASTPFLTdltrAVKESGRP-VSSLRTFLCAGAPIPGA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  742 HV--ARVLLGLpalRLINGYGPTENTTFTTCH---DVSRGMGTGsvpiGKPIANTHVYLLDEQMNPVPPNAVGELFTGGD 816
Cdd:PRK13295  328 LVerARAALGA---KIVSAWGMTENGAVTLTKlddPDERASTTD----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  817 GLARGYHERPDQTAerfvpDPFSGvpgarLYRTGDLARYLPNGDMEFLGR-RDgqVKIRGFR-IELAEVEAALLQHPALR 894
Cdd:PRK13295  401 SNFGGYLKRPQLNG-----TDADG-----WFDTGDLARIDADGYIRISGRsKD--VIIRGGEnIPVVEIEALLYRHPAIA 468

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  895 EAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFL-LQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK13295  469 QVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 4-438 1.38e-36

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: 145.04  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PL-PLSEGQ--RSLwlaqeLAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLV-VRPDNEGLVQSLADVSAV 79
Cdd:cd19543     3 PLsPMQEGMlfHSL-----LDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSfVWEGLGEPLQVVLKDRKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   80 DFGVTDGSSWDEPTAAAWLQAEA----ARPFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAA 154
Cdd:cd19543    78 PWRELDLSHLSEAEQEAELEALAeedrERGFDLARAPLmRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  155 DVEGRAATLTPIsRGFRDYLVWhrdlLASDDASALVREWAAMVGDLDVSTPLdlPTDLPRRAQQRYHVRQHFRDLGADLM 234
Cdd:cd19543   158 LGEGQPPSLPPV-RPYRDYIAW----LQRQDKEAAEAYWREYLAGFEEPTPL--PKELPADADGSYEPGEVSFELSAELT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  235 DRVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRtrtwQLGVVG--HMAGI----VPVPARIDAAATPRA 308
Cdd:cd19543   231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR----PAELPGieTMVGLfintLPVRVRLDPDQTVLE 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  309 IIRELRNALRVTAKLQSVPLSRLAeqcRVPKSPGRM----------PLVQAVFQEIRSFNEAIRPEgfgHMLRWSRGPLG 378
Cdd:cd19543   307 LLKDLQAQQLELREHEYVPLYEIQ---AWSEGKQALfdhllvfenyPVDESLEEEQDEDGLRITDV---SAEEQTNYPLT 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  379 FEVEVPSELGSQLDlevrcydffsssvrtcwrYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19543   381 VVAIPGEELTIKLS------------------YDAEVFDEATIERLLGHLRRVLEQVAAN 422
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 612-961 2.85e-36

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: 142.52  E-value: 2.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  612 SAENLaYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGA--LLHGARL------- 682
Cdd:cd05924     2 SADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAppLMHGTGSwtafggl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  683 -----VLFPPESPTPEEIGRVVREHGVTTLWLT-----APLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPA 752
Cdd:cd05924    81 lggqtVVLPDDRFDPEEVWRTIEKHKVTSMTIVgdamaRPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  753 LRLINGYGPTEnTTFTTCHdVSRGMGTGSVPigKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGL-ARGYHERPDQTAE 831
Cdd:cd05924   161 ITLVDAFGSSE-TGFTGSG-HSAGSGPETGP--FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  832 RFVPdpfsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLV 911
Cdd:cd05924   237 TFPE-----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242  912 AYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRR 961
Cdd:cd05924   312 AVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 488-963 4.38e-36

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: 144.16  E-value: 4.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  488 AVALDAGSNVVSYGELNRRADKLAHMLRLKGVG-TETRVGLCLERSVELVVGILGVLKAGGAYVPLDPaypserlaflah 566
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  567 dagvqiVLSAAGAEERLGEGPWTVVRLDEDLgrpderdaapndnVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGS 646
Cdd:cd05958    69 ------LLRPKELAYILDKARITVALCAHAL-------------TASDDICILAFTSGTTGAPKATMHFHRDPLASADRY 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  647 SFATFG--PDQVFLMMAPAAFdasTFEIWGALLH----GARLVLFPpeSPTPEEIGRVVREHGVTTLWlTAPLFHAVADR 720
Cdd:cd05958   130 AVNVLRlrEDDRFVGSPPLAF---TFGLGGVLLFpfgvGASGVLLE--EATPDLLLSAIARYKPTVLF-TAPTAYRAMLA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  721 GLDQ----LRGVRQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTENT-TFTTCHDVSRGMGTgsvpIGKPIANTHVYL 795
Cdd:cd05958   204 HPDAagpdLSSLRKCVSAGEAL-PAALHRAWKEATGIPIIDGIGSTEMFhIFISARPGDARPGA----TGKPVPGYEAKV 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  796 LDEQMNPVPPNAVGELFTGGDglaRGYHERPDQTAERFVPDPFSGvpgarlyrTGDLARYLPNGDMEFLGRRDGQVKIRG 875
Cdd:cd05958   279 VDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNI--------TGDTYSRDPDGYFRHQGRSDDMIVSGG 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  876 FRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPR---FSELRKFLLQRLPDHMIPAAVVALDKLPL 952
Cdd:cd05958   348 YNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTELPR 427

                         490
                  ....*....|.
gi 260177242  953 VPSGKLDRRAL 963
Cdd:cd05958   428 TATGKLQRFAL 438
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 482-965 1.11e-35

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 145.07  E-value: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVAL--DAGSnvVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSE 559
Cdd:PRK07788   59 ARRAPDRAALidERGT--LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  560 RLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRL-----DEDLGRPDERDAAPNDNV----SAENL-------AYVMYTS 623
Cdd:PRK07788  137 QLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLrawggNPDDDEPSGSTDETLDDLiagsSTAPLpkppkpgGIVILTS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  624 GSTGKPKGVAvthRNVVrlvrgSSFAT---------FGPDQVFLMMAPAaFDASTFEIWG-ALLHGARLVLfpPESPTPE 693
Cdd:PRK07788  217 GTTGTPKGAP---RPEP-----SPLAPlagllsrvpFRAGETTLLPAPM-FHATGWAHLTlAMALGSTVVL--RRRFDPE 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  694 EIGRVVREHGVTTLwLTAPLF---------HAVADRGLDQLRGVrqlLAGGDVLSPKHVARVL--LGLpalRLINGYGPT 762
Cdd:PRK07788  286 ATLEDIAKHKATAL-VVVPVMlsrildlgpEVLAKYDTSSLKII---FVSGSALSPELATRALeaFGP---VLYNLYGST 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  763 ENT--TFTTCHDVSRGMGTgsvpIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGY-HERPDQTaerfvpdpfs 839
Cdd:PRK07788  359 EVAfaTIATPEDLAEAPGT----VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYtDGRDKQI---------- 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  840 gVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREA 919
Cdd:PRK07788  425 -IDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG 501

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 260177242  920 EVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK07788  502 AALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 413-968 1.13e-35

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: 146.10  E-value: 1.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  413 PDL--FLPETVERWADYYAALLRELVgdlgrlalqIDFIPEPERRRVLVEWNQTASDYPRERC--LHHLFEEEARRVPDA 488
Cdd:cd05968     7 PDLeaFLERSAEDNAWFWGEFVKDVG---------IEWYEPPYQTLDLSGGKPWAAWFVGGRMniVEQLLDKWLADTRTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  489 VAL-----DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAF 563
Cdd:cd05968    78 PALrwegeDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAAT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  564 LAHDAGVQIVLSAAG-------------AEERLGEGPWT----VVR---------LDEDLGRPDERDAAPN--DNVSAEN 615
Cdd:cd05968   158 RLQDAEAKALITADGftrrgrevnlkeeADKACAQCPTVekvvVVRhlgndftpaKGRDLSYDEEKETAGDgaERTESED 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  616 LAYVMYTSGSTGKPKGVAVTHRNVVrlVRGSSFATFG-----PDQVFL------MMAPaafdastFEIWGALLHGARLVL 684
Cdd:cd05968   238 PLMIIYTSGTTGKPKGTVHVHAGFP--LKAAQDMYFQfdlkpGDLLTWftdlgwMMGP-------WLIFGGLILGATMVL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  685 FP--PESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLR--GVRQLLAGGDVLSP----------KHVarvllGL 750
Cdd:cd05968   309 YDgaPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNahDLSSLRVLGSTGEPwnpepwnwlfETV-----GK 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  751 PALRLINGYGPTEnttfttchdVSRGMgTGSVPIgKPIA----NTHV-----YLLDEQMNPVPPNaVGELFTGGD--GLA 819
Cdd:cd05968   384 GRNPIINYSGGTE---------ISGGI-LGNVLI-KPIKpssfNGPVpgmkaDVLDESGKPARPE-VGELVLLAPwpGMT 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  820 RGYHERPDqtaeRFVPDPFSGVPGARLYrtGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVI 899
Cdd:cd05968   452 RGFWRDED----RYLETYWSRFDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260177242  900 AREDRPGDKRLVAYVVGREAEVPRfSELRKFLLQRLPDHM----IPAAVVALDKLPLVPSGKLDRRALPAPTL 968
Cdd:cd05968   526 GVPHPVKGEAIVCFVVLKPGVTPT-EALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRAAYL 597
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 6-351 1.66e-35

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: 141.83  E-value: 1.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    6 PLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALR--LVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRtcFFTDPEDGEPMQGVLASSPLRLEH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSSWDEptAAAWLQAEAARPFDLRAG-ALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVaaeFAELCAAdveGRAAT 162
Cdd:cd19532    83 VQISDEAE--VEEEFERLKNHVYDLESGeTMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIF---LRDLERA---YNGQP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  163 LTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLDvsTPLDLptdLP------RRAQQRYHVRQHFRDLGADLMDR 236
Cdd:cd19532   155 LLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLP--EPLPL---LPfakvksRPPLTRYDTHTAERRLDAALAAR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  237 VRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNA 316
Cdd:cd19532   230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 260177242  317 lrVTAKLQ--SVPLSRLAEQCRVPKSPGRMPLVQAVF 351
Cdd:cd19532   310 --AYAALAhsRVPFDVLLDELGVPRSATHSPLFQVFI 344
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 468-963 1.90e-35

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: 144.21  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  468 YPRE----RCLHHLFEEEARRVPDAVAL-DAGSNV-VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILG 541
Cdd:cd17642     9 YPLEdgtaGEQLHKAMKRYASVPGTIAFtDAHTGVnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  542 VLKAGGAYVPLDPAYpSERLafLAHDAGV---QIVLSAAGAEERL----GEGPW--TVVRLD--EDLG----------RP 600
Cdd:cd17642    89 GLFIGVGVAPTNDIY-NERE--LDHSLNIskpTIVFCSKKGLQKVlnvqKKLKIikTIIILDskEDYKgyqclytfitQN 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  601 D-----ERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFATFG----PDQVFLMMAPAAFDASTFE 671
Cdd:cd17642   166 LppgfnEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGnqiiPDTAILTVIPFHHGFGMFT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  672 IWGALLHGARLVLFppesPTPEE--IGRVVREHGVTTLWLTAPLF-----HAVADRGldQLRGVRQLLAGGDVLSpKHVA 744
Cdd:cd17642   246 TLGYLICGFRVVLM----YKFEEelFLRSLQDYKVQSALLVPTLFaffakSTLVDKY--DLSNLHEIASGGAPLS-KEVG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  745 RVL---LGLPALRliNGYGPTENTT---FTTCHDVSRGmGTGSVpigKPIANTHVYLLDEQmNPVPPNAVGELFTGGDGL 818
Cdd:cd17642   319 EAVakrFKLPGIR--QGYGLTETTSailITPEGDDKPG-AVGKV---VPFFYAKVVDLDTG-KTLGPNERGELCVKGPMI 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  819 ARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVV 898
Cdd:cd17642   392 MKGYVNNPEATKALIDKDGW--------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGV 463

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242  899 IAREDRPGDKRLVAYVVGREAEVPRFSELRKFLL-QRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd17642   464 AGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVAsQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1989-2431 6.38e-35

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 141.97  E-value: 6.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPL 2068
Cdd:PRK07656    7 LPELLARAARRFGDKEAYVFGDQR-LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2069 DPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLG-IEHVVSLDGDGKDADGNVVIHGRRALADLADGNLPRAAGP 2147
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPaLEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2148 HNMAYVIFTSGSTGTPKGVVERHSQVI-NLIEWVNRTYLVgPSDRLLfVTSPSFDLSVYDVfGMLAA---GGSIHIASED 2223
Cdd:PRK07656  166 DDVADILFTSGTTGRPKGAMLTHRQLLsNAADWAEYLGLT-EGDRYL-AANPFFHVFGYKA-GVNAPlmrGATILPLPVF 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2224 DlrsPERLAAELGRGTITFWDSAPAALQQLVPYFDR-IEDGSQLRLAFLSGDWVPIGMLDELRRAFPnVKLVGLG-GATE 2301
Cdd:PRK07656  243 D---PDEVFRLIETERITVLPGPPTMYNSLLQHPDRsAEDLSSLRLAVTGAASMPVALLERFESELG-VDIVLTGyGLSE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2302 A--TVWSNYFEvDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsg 2379
Cdd:PRK07656  319 AsgVTTFNRLD-DDRKTVAGTI--GTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW-- 393

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242 2380 epgarLYrTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK07656  394 -----LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPA 439
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 469-963 1.28e-34

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 141.82  E-value: 1.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  469 PRERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGA 548
Cdd:PRK06155   18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  549 YVPLDPAYPSERLA-FLAHDAGVQIVLSAAGAEE---------------RLGEGP-WTVVRLDEDLGRPDERDAAPNDNV 611
Cdd:PRK06155   98 AVPINTALRGPQLEhILRNSGARLLVVEAALLAAleaadpgdlplpavwLLDAPAsVSVPAGWSTAPLPPLDAPAPAAAV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  612 SAENLAYVMYTSGSTGKPKGVAVTH-------RNVVRLVRgssfatFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVL 684
Cdd:PRK06155  178 QPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDLE------IGADDVLYTTLPLFHTNALNAFFQALLAGATYVL 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  685 FPPESP---TPEeigrvVREHGVTTLWL---TAPLFHAVADRGLDQLRGVRQLLAGGdvlSPKHVARVLLGLPALRLING 758
Cdd:PRK06155  252 EPRFSAsgfWPA-----VRRHGATVTYLlgaMVSILLSQPARESDRAHRVRVALGPG---VPAALHAAFRERFGVDLLDG 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  759 YGPTE-NTTFTTCHDVSRGMGTGSVPIGkpianTHVYLLDEQMNPVPPNAVGELFTGGD---GLARGYHERPDQTAERFV 834
Cdd:PRK06155  324 YGSTEtNFVIAVTHGSQRPGSMGRLAPG-----FEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWR 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  835 PDPFsgvpgarlyRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYV 914
Cdd:PRK06155  399 NLWF---------HTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAV 469

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 260177242  915 VGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK06155  470 VLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
479-963 1.98e-34

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 140.38  E-value: 1.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  479 EEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLK-GVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLS----AAGAEERLGE-GPWTVVRLdEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGV 632
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVektfQNMALSMQKVsYVQRVISI-TSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  633 AVTHRNVVRLVRGSSFAT-FGPDQVFLMMAPaafdasTFEIWG-------ALLHGARLVLfpPESPTPEEIGRVVREHGV 704
Cdd:PRK06839  168 VLTQENMFWNALNNTFAIdLTMHDRSIVLLP------LFHIGGiglfafpTLFAGGVIIV--PRKFEPTKALSMIEKHKV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  705 TTLwLTAPLFHA----VADRGLDQLRGVRQLLAGGdVLSPKHVARVLLGlPALRLINGYGPTEN--TTFTTCH-DVSRGM 777
Cdd:PRK06839  240 TVV-MGVPTIHQalinCSKFETTNLQSVRWFYNGG-APCPEELMREFID-RGFLFGQGFGMTETspTVFMLSEeDARRKV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  778 GTgsvpIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAErfvpdpfsGVPGARLYrTGDLARYLP 857
Cdd:PRK06839  317 GS----IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------TIQDGWLC-TGDLARVDE 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  858 NGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPD 937
Cdd:PRK06839  384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAK 463

                         490       500
                  ....*....|....*....|....*.
gi 260177242  938 HMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK06839  464 YKIPKEIVFLKELPKNATGKIQKAQL 489
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 5-438 2.36e-34

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: 138.55  E-value: 2.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    5 LPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVrPDNEGLVQSL---ADVSAVDF 81
Cdd:cd19538     2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVF-PEEDGVPYQLileEDEATPKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   82 GVTDGsswDEPTAAAWLQAEAARPFDLRA-GALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:cd19538    81 EIKEV---DEEELESEINEAVRYPFDLSEePPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWHRDLL--ASDDASALVREWAAMVGDLD-VSTPLDLPTDLPRRAQQRY---HVRqhFrDLGADLM 234
Cdd:cd19538   158 PELAPLPVQYADYALWQQELLgdESDPDSLIARQLAYWKKQLAgLPDEIELPTDYPRPAESSYeggTLT--F-EIDSELH 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  235 DRVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMagIVPVPARIDAAATPRaiIRELR 314
Cdd:cd19538   235 QQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFF--VNTLVLRTDTSGNPS--FRELL 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  315 NALRVTA----KLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQ---------EIRSFNEAIRPEGFGHmlrwSRGPLGFEV 381
Cdd:cd19538   311 ERVKETNleayEHQDIPFERLVEALNPTRSRSRHPLFQIMLAlqntpqpslDLPGLEAKLELRTVGS----AKFDLTFEL 386

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  382 EVPSELGSQLDLEVRCydffsssvrtcwRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19538   387 REQYNDGTPNGIEGFI------------EYRTDLFDHETIEALAQRYLLLLESAVEN 431
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 482-963 5.14e-34

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 139.25  E-value: 5.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLSAAGAEERLGEGPWTVVrLDED-------LGRPDErDAAPNDNVSAENLAYVMYTSGSTGKPKGVAV 634
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIV-IDAAaqadsrrLAQGGL-EIPPQAAVAPTDLVRLMYTSGTTDRPKGVMH 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  635 THRNVVRLVRGSSFAT-FGPDQVFLMMAP----AAFDASTFEIwgaLLHGARLVLFppESPTPEEIGRVVREHGVTTLWL 709
Cdd:PRK06145  170 SYGNLHWKSIDHVIALgLTASERLLVVGPlyhvGAFDLPGIAV---LWVGGTLRIH--REFDPEAVLAAIERHRLTCAWM 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  710 tAPLFH----AVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGM-GTGSVpi 784
Cdd:PRK06145  245 -APVMLsrvlTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIeKIGST-- 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  785 GKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLArYLPNGDMEFL 864
Cdd:PRK06145  322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF---------RSGDVG-YLDEEGFLYL 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  865 GRRDGQVKIRGFR-IELAEVEAALLQHPALREAVVI-AREDRPGDkRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPA 942
Cdd:PRK06145  392 TDRKKDMIISGGEnIASSEVERVIYELPEVAEAAVIgVHDDRWGE-RITAVVVLNPGATLTLEALDRHCRQRLASFKVPR 470

                         490       500
                  ....*....|....*....|.
gi 260177242  943 AVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK06145  471 QLKVRDELPRNPSGKVLKRVL 491
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 474-963 7.81e-34

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 139.78  E-value: 7.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 PAYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPWT-------VVRLDEDLGRPD------------------------- 601
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSAtkiehviVTRIADFLPFPKnllypfvqkkqsnlvvkvsesetih 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  602 -------ERDAAPNDNVSAEN-LAYVMYTSGSTGKPKGVAVTHRNVV-RLVRGSS--FATFGPDQVFLMMAPaafdasTF 670
Cdd:PRK06710  186 lwnsvekEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQwlYNCKEGEEVVLGVLP------FF 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  671 EIWG-------ALLHGARLVLFPPESPtpEEIGRVVREHGVTtLWLTAP-LFHAVADRGLDQ---LRGVRQLLAGGDVLs 739
Cdd:PRK06710  260 HVYGmtavmnlSIMQGYKMVLIPKFDM--KMVFEAIKKHKVT-LFPGAPtIYIALLNSPLLKeydISSIRACISGSAPL- 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  740 PKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSvpIGKPIANTHVYLLD-EQMNPVPPNAVGELFTGGDGL 818
Cdd:PRK06710  336 PVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGS--IGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQI 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  819 ARGYHERPDQTAerfvpdpfsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVV 898
Cdd:PRK06710  414 MKGYWNKPEETA---------AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  899 IAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK06710  485 IGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 492-963 1.27e-33

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: 137.85  E-value: 1.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  492 DAGSNVVSYGELNRRADKLAHMLRlKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQ 571
Cdd:cd05909     2 DTLGTSLTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  572 IVLSAAGAEERLG-------EGPWTVVRLDE---DLGRPDERDAA--------------PNDNVSAENLAYVMYTSGSTG 627
Cdd:cd05909    81 TVLTSKQFIEKLKlhhlfdvEYDARIVYLEDlraKISKADKCKAFlagkfppkwllrifGVAPVQPDDPAVILFTSGSEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  628 KPKGVAVTHRNVVRLVRGSS-FATFGPDQVFLMMAPaAFDASTFE--IWGALLHGARLVLFPpeSPT-PEEIGRVVREHG 703
Cdd:cd05909   161 LPKGVVLSHKNLLANVEQITaIFDPNPEDVVFGALP-FFHSFGLTgcLWLPLLSGIKVVFHP--NPLdYKKIPELIYDKK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  704 VTTLWLTAPLFHAVADRGL-DQLRGVRQLLAGGDVLSPKhVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSV 782
Cdd:cd05909   238 ATILLGTPTFLRGYARAAHpEDFSSLRLVVAGAEKLKDT-LRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  783 piGKPIANTHVYLLD-EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAErfvpdpfsgVPGARLYRTGDLARYLPNGDM 861
Cdd:cd05909   317 --GRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF---------AFGDGWYDTGDIGKIDGEGFL 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  862 EFLGRRDGQVKIRGFRIELAEVEAALLQH-PALREAVVIARED-RPGDKrLVAYVVGREAEVprfSELRKFLLQ-RLPDH 938
Cdd:cd05909   386 TITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDgRKGEK-IVLLTTTTDTDP---SSLNDILKNaGISNL 461

                         490       500
                  ....*....|....*....|....*
gi 260177242  939 MIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05909   462 AKPSYIHQVEEIPLLGTGKPDYVTL 486
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 472-963 1.99e-33

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: 137.26  E-value: 1.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  472 RCLHHLFEEEARRVPDAVAL--DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAY 549
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIadPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  550 VPLDPAYPSERLAFLAHDAGVQIVLSAAGAE----ERLGEGPWTVVRLDEDLGRPDERDAAPND-NVSAENLAYVMYTSG 624
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVIAVDAQvmdaIFQSGVRVLALSDLVGLGEPESAGPLIEDpPREPEQPAFVFYTSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  625 STGKPKGVAVTHRNvvRLVRGSSFAT-----FGPDQVFLMMAPAAFDASTFEIW-GALLHGARLVlfPPESPTPEEIGRV 698
Cdd:cd05923   161 TTGLPKGAVIPQRA--AESRVLFMSTqaglrHGRHNVVLGLMPLYHVIGFFAVLvAALALDGTYV--VVEEFDPADALKL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  699 VREHGVTTLWLTAPLFHAVADRGL---DQLRGVRQLLAGGDVLSPKHVARVLLGLPALRlINGYGPTENTTFTTCHDVSR 775
Cdd:cd05923   237 IEQERVTSLFATPTHLDALAAAAEfagLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK-VNIYGTTEAMNSLYMRDART 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  776 GMGtgsvpiGKPIANTHVYLLDEQMNPVPPNAVGE-----LFTGGDGLARGYHERPDQTAERFVpdpfsgvpgARLYRTG 850
Cdd:cd05923   316 GTE------MRPGFFSEVRIVRIGGSPDEALANGEegeliVAAAADAAFTGYLNQPEATAKKLQ---------DGWYRTG 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  851 DLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRfSELRKF 930
Cdd:cd05923   381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSA-DELDQF 459

                         490       500       510
                  ....*....|....*....|....*....|....
gi 260177242  931 LL-QRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05923   460 CRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 495-958 2.00e-33

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: 138.86  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  495 SNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVL 574
Cdd:cd17634    82 SRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLI 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  575 SAAG----------------AEERLGEGPWTVVRLDE-----------DLGRPDERDAAPNDN----VSAENLAYVMYTS 623
Cdd:cd17634   162 TADGgvragrsvplkknvddALNPNVTSVEHVIVLKRtgsdidwqegrDLWWRDLIAKASPEHqpeaMNAEDPLFILYTS 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  624 GSTGKPKGVAVTHRNVVrLVRGSSFAT---FGPDQVFLMMAPAAF-DASTFEIWGALLHGARLVLFP--PESPTPEEIGR 697
Cdd:cd17634   242 GTTGKPKGVLHTTGGYL-VYAATTMKYvfdYGPGDIYWCTADVGWvTGHSYLLYGPLACGATTLLYEgvPNWPTPARMWQ 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  698 VVREHGVTTLWLTAPLFHAVADRGLDQLRG-----VRQLLAGGDVLSPKHVARVL--LGLPALRLINGYGPTENTTFttC 770
Cdd:cd17634   321 VVDKHGVNILYTAPTAIRALMAAGDDAIEGtdrssLRILGSVGEPINPEAYEWYWkkIGKEKCPVVDTWWQTETGGF--M 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  771 HDVSRG---MGTGSVPigKPIANTHVYLLDEQMNPVPPNAVGELFTGGD--GLARGYHERPDqtaeRFVPDPFSGVPGar 845
Cdd:cd17634   399 ITPLPGaieLKAGSAT--RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKG-- 470

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  846 LYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPR-- 923
Cdd:cd17634   471 MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpe 550

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 260177242  924 -FSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKL 958
Cdd:cd17634   551 lYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 482-963 2.57e-33

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 138.25  E-value: 2.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLS---------AAGAEERLGEGPWT----VVRLDEDLGRPDERDAA---------------------P 607
Cdd:PRK06178  123 SYELNDAGAEVLLAldqlapvveQVRAETSLRHVIVTsladVLPAEPTLPLPDSLRAPrlaaagaidllpalractapvP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  608 NDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFATF--GPDQVFLMMAPaafdastfEIWGA---------L 676
Cdd:PRK06178  203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVvgGEDSVFLSFLP--------EFWIAgenfgllfpL 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  677 LHGARLVLFPPESPtpEEIGRVVREHGVTTLWLTAP-----LFH-AVADRGLDQLRGVRqllaggdvlspkhVARVLLGL 750
Cdd:PRK06178  275 FSGATLVLLARWDA--VAFMAAVERYRVTRTVMLVDnavelMDHpRFAEYDLSSLRQVR-------------VVSFVKKL 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  751 -PALR----------LING-YGPTENTTfttCHDVSRGMGTG-----SVPI--GKPIANTHVYLLDEQMN-PVPPNAVGE 810
Cdd:PRK06178  340 nPDYRqrwraltgsvLAEAaWGMTETHT---CDTFTAGFQDDdfdllSQPVfvGLPVPGTEFKICDFETGeLLPLGAEGE 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  811 LFTGGDGLARGYHERPDQTAERFVpDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQH 890
Cdd:PRK06178  417 IVVRTPSLLKGYWNKPEATAEALR-DGW--------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQH 487

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260177242  891 PALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPaAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK06178  488 PAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 487-965 3.13e-33

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 138.10  E-value: 3.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  487 DAVAL---DAGSNV-VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY------ 556
Cdd:PRK04319   59 DKVALrylDASRKEkYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFmeeavr 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 ---------------------PSERLAFLAHdagvqIVLsaAGAEERLGEGpwtVVRLDEDL-GRPDERDAAPNDnvsAE 614
Cdd:PRK04319  139 drledseakvlittpallerkPADDLPSLKH-----VLL--VGEDVEEGPG---TLDFNALMeQASDEFDIEWTD---RE 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRNVV-RLVRGSSFATFGPDQVFLMMA-PAAFDASTFEIWGALLHGARLVL----Fppe 688
Cdd:PRK04319  206 DGAILHYTSGSTGKPKGVLHVHNAMLqHYQTGKYVLDLHEDDVYWCTAdPGWVTGTSYGIFAPWLNGATNVIdggrF--- 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  689 spTPEEIGRVVREHGVTtLWLTAPlfhavadrgldqlRGVRQLLAGGDVLSPKHvarvllGLPALRLINGYG-------- 760
Cdd:PRK04319  283 --SPERWYRILEDYKVT-VWYTAP-------------TAIRMLMGAGDDLVKKY------DLSSLRHILSVGeplnpevv 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  761 ---------PTENT---TFTTCHDVSRgmgTGSVPI-----GKPIANTHVYLLDEQMNPVPPNAVGELF--TGGDGLARG 821
Cdd:PRK04319  341 rwgmkvfglPIHDNwwmTETGGIMIAN---YPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAikKGWPSMMRG 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  822 YHERPDQTAERFVPDpfsgvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAR 901
Cdd:PRK04319  418 IWNNPEKYESYFAGD---------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  902 EDRPGDKRLVAYVVGREAEVPRFS---ELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK04319  489 PDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 481-971 4.92e-33

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 136.09  E-value: 4.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  481 EARRVPDAVALD--AGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPS 558
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  559 ERLAFLAHDAGVQIVLSAAG-AEERLGEGPWTVVRLDEDLGRPDERDAAPNDNVSaenlaYVMYTSGSTGKPKGVAVTHR 637
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAvAAGRTDVEDLAAFIASADALEPADTPSIPPERVS-----LILFTSGTSGQPKGVMLSER 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  638 NVVRLVRGSSFAT-FGPDQVFLMMAPaafdasTFEIWG-------ALLHGARLVLFPPESPtpeeiGRVVREHGVTTLWL 709
Cdd:PRK09088  159 NLQQTAHNFGVLGrVDAHSSFLCDAP------MFHIIGlitsvrpVLAVGGSILVSNGFEP-----KRTLGRLGDPALGI 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  710 T--------APLFHAVADRGLDQLRGVRQLLAGGdvlSPkHVARVLLGLPA--LRLINGYGPTE-NTTFTTCHDVSRGMG 778
Cdd:PRK09088  228 ThyfcvpqmAQAFRAQPGFDAAALRHLTALFTGG---AP-HAAEDILGWLDdgIPMVDGFGMSEaGTVFGMSVDCDVIRA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  779 -TGSVPIGKPIANTHVylLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLP 857
Cdd:PRK09088  304 kAGAAGIPTPTVQTRV--VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW--------FRTGDIARRDA 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  858 NGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPD 937
Cdd:PRK09088  374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAK 453

                         490       500       510
                  ....*....|....*....|....*....|....
gi 260177242  938 HMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGR 971
Cdd:PRK09088  454 YKVPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 4-351 9.62e-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. 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: 133.92  E-value: 9.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:cd20483     1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSSWDEPTAAAWLQAEAAR--PFDLRAGAL-RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:cd20483    81 IDLSEAADPEAALDQLVRNLRrqELDIEEGEViRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 -ATLTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLDVSTPLdlptdLP-----RRAQQRYHVRQHFRDLGADLM 234
Cdd:cd20483   161 lATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKL-----LPfakaeRPPVKDYERSTVEATLDKELL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  235 DRVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELR 314
Cdd:cd20483   236 ARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTK 315

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 260177242  315 NALRVTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVF 351
Cdd:cd20483   316 TTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAV 352
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 498-928 1.46e-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: 133.87  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLsaa 577
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 gaeerlGEGPwtvvrldedlgrpderdaapndnvsaENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSS-FATFGPDQV 656
Cdd:cd05907    83 ------VEDP--------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAeRLPATEGDR 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  657 FLMMAPAafdASTFE----IWGALLHGARLVLFPPESPTPEEIgRVVRehgvTTLWLTAPLF--------HAVADRGLDQ 724
Cdd:cd05907   131 HLSFLPL---AHVFErragLYVPLLAGARIYFASSAETLLDDL-SEVR----PTVFLAVPRVwekvyaaiKVKAVPGLKR 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  725 -------LRGVRQLLAGGDVLSPkHVARVL--LGLPalrLINGYGPTENTTFTTCHDVsRGMGTGSVpiGKPIANTHVYL 795
Cdd:cd05907   203 klfdlavGGRLRFAASGGAPLPA-ELLHFFraLGIP---VYEGYGLTETSAVVTLNPP-GDNRIGTV--GKPLPGVEVRI 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  796 LDEqmnpvppnavGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGdmeFL---GR-RDGQV 871
Cdd:cd05907   276 ADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW--------LHTGDLGEIDEDG---FLhitGRkKDLII 334

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  872 KIRGFRIELAEVEAALLQHPALREAVVIArEDRPgdkRLVAYVVGREAEVPRFSELR 928
Cdd:cd05907   335 TSGGKNISPEPIENALKASPLISQAVVIG-DGRP---FLVALIVPDPEALEAWAEEH 387
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1996-2431 2.12e-32

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: 133.12  E-value: 2.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1996 SVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLE 2075
Cdd:cd17631     4 RARRHPDRTALVFGGRS-LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2076 RVAAVLGttrpvcivtderhlgaveiaarqlgiehvvsldgdgkDADGNVVIHgrraladladgnlpraagphNMAYVIF 2155
Cdd:cd17631    83 EVAYILA-------------------------------------DSGAKVLFD--------------------DLALLMY 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2156 TSGSTGTPKGVVERH----SQVINLIEwvnrTYLVGPSDRLLfVTSPSFDLSVYDVFGM--LAAGGSIHIASEDDlrsPE 2229
Cdd:cd17631   106 TSGTTGRPKGAMLTHrnllWNAVNALA----ALDLGPDDVLL-VVAPLFHIGGLGVFTLptLLRGGTVVILRKFD---PE 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLAAELGRGTITFWDSAPAALQQLV--PYFDRIeDGSQLRLAFLSGDWVPIGMLDELRRAfpNVKLVGLGGATEATVWSN 2307
Cdd:cd17631   178 TVLDLIERHRVTSFFLVPTMIQALLqhPRFATT-DLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVT 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2308 YFEVDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlyR 2387
Cdd:cd17631   255 FLSPEDHRRKLGSA--GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF---------H 323

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 260177242 2388 TGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17631   324 TGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPA 367
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
486-963 2.93e-32

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 134.35  E-value: 2.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGgaYVPLDPAYPSERLAFLA 565
Cdd:PRK10946   37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSELNA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLSAAGAEERL-------------GEGPWTVVRLDEDLGRP-DERDAAPNDNVS-----AENLAYVMYTSGST 626
Cdd:PRK10946  115 YASQIEPALLIADRQHALfsdddflntlvaeHSSLRVVLLLNDDGEHSlDDAINHPAEDFTatpspADEVAFFQLSGGST 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  627 GKPKGVAVTHRNVVRLVRGSS-FATFGPDQVFLMMAPAA--FDASTFEIWGALLHGARLVLFPpeSPTPEEIGRVVREHG 703
Cdd:PRK10946  195 GTPKLIPRTHNDYYYSVRRSVeICGFTPQTRYLCALPAAhnYPMSSPGALGVFLAGGTVVLAP--DPSATLCFPLIEKHQ 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  704 VT---------TLWLtaplfHAVADRG-LDQLRGVRQLLAGGDVLSPKHVARVllglPAL---RLINGYGPTE---NTT- 766
Cdd:PRK10946  273 VNvtalvppavSLWL-----QAIAEGGsRAQLASLKLLQVGGARLSETLARRI----PAElgcQLQQVFGMAEglvNYTr 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  767 --------FTTchdvsrgmgtgsvpIGKPIA-NTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDP 837
Cdd:PRK10946  344 lddsderiFTT--------------QGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  838 FsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIARED-RPGDKRlVAYVVG 916
Cdd:PRK10946  410 F--------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDeLMGEKS-CAFLVV 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242  917 REAEVPrfSELRKFLLQR------LPDHmipaaVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK10946  481 KEPLKA--VQLRRFLREQgiaefkLPDR-----VECVDSLPLTAVGKVDKKQL 526
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 482-960 3.22e-32

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: 134.55  E-value: 3.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVAL----DAG-SNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:cd05970    27 AKEYPDKLALvwcdDAGeERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 PSERLAFLAHDAGVQIVLSAAGA------EERLGEGP---------------WTVVRLDEDLGRPDERDAAPNDNVSAEN 615
Cdd:cd05970   107 TAKDIVYRIESADIKMIVAIAEDnipeeiEKAAPECPskpklvwvgdpvpegWIDFRKLIKNASPDFERPTANSYPCGED 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  616 LAYVMYTSGSTGKPKGVAvtHRNVVRL---VRGSSFATFGPDQVFLMMAPAAFDASTF-EIWGALLHGARLVLFPPESPT 691
Cdd:cd05970   187 ILLVYFSSGTTGMPKMVE--HDFTYPLghiVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYDKFD 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  692 PEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQ--LRGVRQLLAGGDVLSPKhVARVLLGLPALRLINGYGPTEnTTFTT 769
Cdd:cd05970   265 PKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRydLSSLRYCTTAGEALNPE-VFNTFKEKTGIKLMEGFGQTE-TTLTI 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  770 ChdVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGD-----GLARGYHERPDQTAERFvpdpFSGVpga 844
Cdd:cd05970   343 A--TFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW----HDGY--- 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  845 rlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVV---GREAEV 921
Cdd:cd05970   414 --YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakGYEPSE 491

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 260177242  922 PRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:cd05970   492 ELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
474-963 7.97e-32

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 133.09  E-value: 7.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSN--VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVP 551
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  552 LDPAYPSERLAFLAHDAGVQIVL--SAAGAEERLGEGPW--TVVRLDEDLGRPD-----ERDA--APNDNVSAE-----N 615
Cdd:PRK05852   98 LDPALPIAEQRVRSQAAGARVVLidADGPHDRAEPTTRWwpLTVNVGGDSGPSGgtlsvHLDAatEPTPATSTPeglrpD 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  616 LAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFA-TFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPEsptpee 694
Cdd:PRK05852  178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGyRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPAR------ 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  695 iGRVVRE------HGVTTLWLTA-PLFHAV---------ADRGLDQLRGVRQLLAGgdvLSPK--HVARVLLGLPalrLI 756
Cdd:PRK05852  252 -GRFSAHtfwddiKAVGATWYTAvPTIHQIlleraatepSGRKPAALRFIRSCSAP---LTAEtaQALQTEFAAP---VV 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  757 NGYGPTENTTFTTC-------HDVSRGMGTGsvPIGKPIAnTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQT 829
Cdd:PRK05852  325 CAFGMTEATHQVTTtqiegigQTENPVVSTG--LVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTIT 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  830 AERFVPDPFsgvpgarlyRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKR 909
Cdd:PRK05852  402 AANFTDGWL---------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 260177242  910 LVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK05852  473 VAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 2014-2431 1.11e-31

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: 131.95  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:cd05911    11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHLGAVEIAARQLG-IEHVVSLDGDGKDADGNVVIHGRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQ 2172
Cdd:cd05911    91 DGLEKVKEAAKELGpKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2173 VINLIEWVNRT--YLVGPSDRLLFVtspsfdLSVYDVFGMLAA------GGSIHIASEDDlrsPERLAAELGRGTITFWD 2244
Cdd:cd05911   171 LIANLSQVQTFlyGNDGSNDVILGF------LPLYHIYGLFTTlasllnGATVIIMPKFD---SELFLDLIEKYKITFLY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2245 SAPAALQQLV--PYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSnyfevdGIDPRWTSIP 2322
Cdd:cd05911   242 LVPPIAAALAksPLLDK-YDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGIL------TVNPDGDDKP 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2323 --YGRPIQNARYYVLDRSGNP-CPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGN 2399
Cdd:cd05911   315 gsVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW--------LHTGDIGYFDEDGY 386

                         410       420       430
                  ....*....|....*....|....*....|..
gi 260177242 2400 IEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05911   387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPG 418
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2015-2434 1.39e-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. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 130.10  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDEr 2094
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2095 hlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagphnmAYVIFTSGSTGTPKGVVERHSQVI 2174
Cdd:cd05934    84 --------------------------------------------------------ASILYTSGTTGPPKGVVITHANLT 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2175 NLIEWVNRTYLVGPSDRLLfVTSPSF--DLSVYDVFGMLAAGGSIHIASEddlRSPERLAAELGRGTITFWDSAPAALQQ 2252
Cdd:cd05934   108 FAGYYSARRFGLGEDDVYL-TVLPLFhiNAQAVSVLAALSVGATLVLLPR---FSASRFWSDVRRYGATVTNYLGAMLSY 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2253 LVPYFDRIEDGS-QLRLAFLSGdwVPIGMLDELRRAFpNVKLVGLGGATE--ATVWSNYFEVDgidpRWTSIPYGRPIQN 2329
Cdd:cd05934   184 LLAQPPSPDDRAhRLRAAYGAP--NPPELHEEFEERF-GVRLLEGYGMTEtiVGVIGPRDEPR----RPGSIGRPAPGYE 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2330 ARyyVLDRSGNPCPIGVTGDLYI---GGTCVSFGYYADPSQTAERFvPDPFsgepgarlYRTGDLARFFRDGNIEFLGRA 2406
Cdd:cd05934   257 VR--IVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW--------FHTGDLGYRDADGFFYFVDRK 325

                         410       420
                  ....*....|....*....|....*...
gi 260177242 2407 DSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd05934   326 KDMIRRRGENISSAEVERAILRHPAVRE 353
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 474-963 2.54e-31

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 131.70  E-value: 2.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLD 553
Cdd:PRK07470    9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  554 PAYPSERLAFLAHDAGVQIVLSAAG------AEERLGEGPWTVVRLD--------EDLGRPDERDAAPNDNVSAENLAYV 619
Cdd:PRK07470   89 FRQTPDEVAYLAEASGARAMICHADfpehaaAVRAASPDLTHVVAIGgaragldyEALVARHLGARVANAAVDHDDPCWF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  620 MYTSGSTGKPKGVAVTH--------RNVVRLVRGSSfatfgPDQVFLMMAPAAFDASTFeiwgALL---HGARLVLFPPE 688
Cdd:PRK07470  169 FFTSGTTGRPKAAVLTHgqmafvitNHLADLMPGTT-----EQDASLVVAPLSHGAGIH----QLCqvaRGAATVLLPSE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  689 SPTPEEIGRVVREHGVTTLWlTAPLF------H-AVADRGLDQLRGVrqLLAGgdvlSPKHVARVLLGLPAL--RLINGY 759
Cdd:PRK07470  240 RFDPAEVWALVERHRVTNLF-TVPTIlkmlveHpAVDRYDHSSLRYV--IYAG----APMYRADQKRALAKLgkVLVQYF 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  760 GPTENTTFTTC-----HDVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFV 834
Cdd:PRK07470  313 GLGEVTGNITVlppalHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  835 PDPFsgvpgarlyRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYV 914
Cdd:PRK07470  393 DGWF---------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVC 463

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 260177242  915 VGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK07470  464 VARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 2014-2430 2.58e-31

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: 129.93  E-value: 2.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd05969    81 E----------------------------------------------LYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAM 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INliEWVNRTYLVG--PSDRLLFVTSPSFDL-SVYDVFGMLAAGgsIHIASEDDLRSPERLAAELGRGTITFWDSAPAAL 2250
Cdd:cd05969   115 IF--YYFTGKYVLDlhPDDIYWCTADPGWVTgTVYGIWAPWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAI 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2251 QQLVPYFD---RIEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATE--ATVWSNYFevdGIDPRWTSIpyGR 2325
Cdd:cd05969   191 RMLMKEGDelaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTEtgSIMIANYP---CMPIKPGSM--GK 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2326 PIQNARYYVLDRSGNPCPIGVTGDLYI--GGTCVSFGYYADPSQTAERFVPDpfsgepgarLYRTGDLARFFRDGNIEFL 2403
Cdd:cd05969   265 PLPGVKAAVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIDG---------WYLTGDLAYRDEDGYFWFV 335

                         410       420
                  ....*....|....*....|....*..
gi 260177242 2404 GRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05969   336 GRADDIIKTSGHRVGPFEVESALMEHP 362
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 472-963 3.22e-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: 131.25  E-value: 3.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  472 RCLHHLFEEEARRVPDA----VALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGG 547
Cdd:cd05906    10 RTLLELLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  548 AYVPLDPA----YPSERLAFLAH-----DAGVqIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDNV---SAEN 615
Cdd:cd05906    90 VPAPLTVPptydEPNARLRKLRHiwqllGSPV-VLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLpqsRPDD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  616 LAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVFLmmapaafdastfeIWGALLHGARLV---LFPPES-- 689
Cdd:cd05906   169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNgLTPQDVFL-------------NWVPLDHVGGLVelhLRAVYLgc 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 -----PTPEEIGRVVR------EHGVTTLWltAPLF-----HAVADRGLDQ---LRGVRQLLAGGDVLSPKHVARVL--- 747
Cdd:cd05906   236 qqvhvPTEEILADPLRwldlidRYRVTITW--APNFafallNDLLEEIEDGtwdLSSLRYLVNAGEAVVAKTIRRLLrll 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  748 --LGLPALRLINGYGPTEnttftTCHDV--SRGMGTGSVP-------IGKPIANTHVYLLDEQMNPVPPNAVGELFTGGD 816
Cdd:cd05906   314 epYGLPPDAIRPAFGMTE-----TCSGViySRSFPTYDHSqalefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  817 GLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLArYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREA 896
Cdd:cd05906   389 VVTKGYYNNPEANAEAFTEDGW--------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPS 459

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  897 VVIA---REDRPGDKRLVAYVVGREAEVPRFSEL----RKFLLQRL---PDHMIPaavVALDKLPLVPSGKLDRRAL 963
Cdd:cd05906   460 FTAAfavRDPGAETEELAIFFVPEYDLQDALSETlraiRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
453-963 4.87e-31

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 131.02  E-value: 4.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  453 ERRRVLVE---W-NQTASDYPRERClhhlfeeeaRRVPDAVAL--DAGSNVvSYGELNRRADKLAHMLRLKGVGTETRVG 526
Cdd:PRK06087    9 QRRAAYRQqgyWgDASLADYWQQTA---------RAMPDKIAVvdNHGASY-TYSALDHAASRLANWLLAKGIEPGDRVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  527 LCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVR-----LDEDLGRPD 601
Cdd:PRK06087   79 FQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQnqlpqLQQIVGVDK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  602 ERDAAPND----------------NVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRgsSFAT---FGPDQVFLMMAP 662
Cdd:PRK06087  159 LAPATSSLslsqiiadyeplttaiTTHGDELAAVLFTSGTEGLPKGVMLTHNNILASER--AYCArlnLTWQDVFMMPAP 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  663 AAFDASTFE-IWGALLHGARLVLFppESPTPEEIGRVVREHGVTTLWLTAP----LFHAVADRGLDqLRGVRQLLAGGDV 737
Cdd:PRK06087  237 LGHATGFLHgVTAPFLIGARSVLL--DIFTPDACLALLEQQRCTCMLGATPfiydLLNLLEKQPAD-LSALRFFLCGGTT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  738 LsPKHVARVLLGlPALRLINGYGPTENT--TFTTCHD-VSRGMGTGsvpiGKPIANTHVYLLDEQMNPVPPNAVGELFTG 814
Cdd:PRK06087  314 I-PKKVARECQQ-RGIKLLSVYGSTESSphAVVNLDDpLSRFMHTD----GYAAAGVEIKVVDEARKTLPPGCEGEEASR 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  815 GDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDgQVKIRGFR-IELAEVEAALLQHPAL 893
Cdd:PRK06087  388 GPNVFMGYLDEPELTARALDEEGW--------YYSGDLCRMDEAGYIKITGRKK-DIIVRGGEnISSREVEDILLQHPKI 458

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242  894 REAVVIAREDRPGDKRLVAYVVGREAE-VPRFSELRKFL-LQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK06087  459 HDACVVAMPDERLGERSCAYVVLKAPHhSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 1996-2431 5.03e-31

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: 130.18  E-value: 5.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1996 SVERSPGSVALCYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLE 2075
Cdd:cd05959    12 NLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2076 RVAAVLGTTRPVCIVTDERHLGAVEIAARQLG--IEHVVSLDGDGKDADgnvVIHGRRALADLADGNLPRAAGPHNMAYV 2153
Cdd:cd05959    92 DYAYYLEDSRARVVVVSGELAPVLAAALTKSEhtLVVLIVSGGAGPEAG---ALLLAELVAAEAEQLKPAATHADDPAFW 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2154 IFTSGSTGTPKGVVERHSQVInlieWVNRTYlvgpSDRLLFVTSPSFDLSVYDVF---GM-------LAAGGSIhiased 2223
Cdd:cd05959   169 LYSSGSTGRPKGVVHLHADIY----WTAELY----ARNVLGIREDDVCFSAAKLFfayGLgnsltfpLSVGATT------ 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2224 dLRSPERLAA-------ELGRGTI-----TFWDSAPAA--LQQlvpyfdriEDGSQLRLAFLSGDWVPIGMLDELRRAFP 2289
Cdd:cd05959   235 -VLMPERPTPaavfkriRRYRPTVffgvpTLYAAMLAApnLPS--------RDLSSLRLCVSAGEALPAEVGERWKARFG 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2290 NVKLVGLgGATEA--TVWSNyfevdgidpRWTSIPY---GRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYAD 2364
Cdd:cd05959   306 LDILDGI-GSTEMlhIFLSN---------RPGRVRYgttGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNN 375

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242 2365 PSQTAERFVpdpfsGEpgarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05959   376 RDKTRDTFQ-----GE----WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPA 433
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 498-963 5.68e-31

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: 128.23  E-value: 5.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIvlsaa 577
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 gaeerlgegpwtvvrldedlgrpderdaapndnvsaENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFaTFG--PDQ 655
Cdd:cd05912    77 ------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSAL-NLGltEDD 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  656 VFLMMAPaafdasTFEIWG------ALLHGARLVLFppESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQ----L 725
Cdd:cd05912   120 NWLCALP------LFHISGlsilmrSVIYGMTVYLV--DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGypnnL 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  726 RGVrqLLAGGDVLSPKHVARVLLGLPalrLINGYGPTENT----TFTTCHDVSRgmgTGSVpiGKPIANTHVYLLDEQmn 801
Cdd:cd05912   192 RCI--LLGGGPAPKPLLEQCKEKGIP---VYQSYGMTETCsqivTLSPEDALNK---IGSA--GKPLFPVELKIEDDG-- 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  802 pVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLArYLPN-GDMEFLGRRDGQVKIRGFRIEL 880
Cdd:cd05912   260 -QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF---------KTGDIG-YLDEeGFLYVLDRRSDLIISGGENIYP 328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  881 AEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGrEAEVPRfSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:cd05912   329 AEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS-ERPISE-EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406


                  ...
gi 260177242  961 RAL 963
Cdd:cd05912   407 HEL 409
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1537-1857 1.27e-30

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: 127.54  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1537 PLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFlwegvPE----PLQVVRrlvriP 1612
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVF-----PEddggPYQVVL-----P 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1613 TERIDARSMAVDGDA-WIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYS-- 1689
Cdd:cd19540    73 AAEARPDLTVVDVTEdELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAar 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1690 -GGmqheAAHRTAPRP--HRDYVAWLR-----GADAQSVE----RFWRRELGGFREVTPLGIDRP-PAGQrasSYR--RF 1754
Cdd:cd19540   153 rAG----RAPDWAPLPvqYADYALWQRellgdEDDPDSLAarqlAYWRETLAGLPEELELPTDRPrPAVA---SYRggTV 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1755 ERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAplEGIERMVGLFINTVPMRAVVDPE 1834
Cdd:cd19540   226 EFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGD--EALDDLVGMFVNTLVLRTDVSGD 303

                         330       340
                  ....*....|....*....|...
gi 260177242 1835 RPIGEWLTELqgRRAERTAYEHA 1857
Cdd:cd19540   304 PTFAELLARV--RETDLAAFAHQ 324
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
482-963 1.30e-30

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 128.54  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:PRK03640   12 AFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLSAAGAEERLGEGpwTVVRLDEdLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVR 641
Cdd:PRK03640   92 LWQLDDAEVKCLITDDDFEAKLIPG--ISVKFAE-LMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWW 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  642 LVRGSSFaTFG--PDQVFLMMAPAaFDASTFEI-WGALLHGARLVLFppESPTPEEIGRVVREHGVTTLWLTAP----LF 714
Cdd:PRK03640  169 SAVGSAL-NLGltEDDCWLAAVPI-FHISGLSIlMRSVIYGMRVVLV--EKFDAEKINKLLQTGGVTIISVVSTmlqrLL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  715 HAVADRGL-DQLRGVrqLLAGGDVLSPKHVARVLLGLPalrLINGYGPTEnttftTCHDV----SRGMGT--GSVpiGKP 787
Cdd:PRK03640  245 ERLGEGTYpSSFRCM--LLGGGPAPKPLLEQCKEKGIP---VYQSYGMTE-----TASQIvtlsPEDALTklGSA--GKP 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  788 IANTHVYLLDeQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLArYLpngDME-FL-- 864
Cdd:PRK03640  313 LFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---------KTGDIG-YL---DEEgFLyv 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  865 -GRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVgREAEVPRfSELRKFLLQRLPDHMIPAA 943
Cdd:PRK03640  379 lDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV-KSGEVTE-EELRHFCEEKLAKYKVPKR 456

                         490       500
                  ....*....|....*....|
gi 260177242  944 VVALDKLPLVPSGKLDRRAL 963
Cdd:PRK03640  457 FYFVEELPRNASGKLLRHEL 476
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 476-963 1.98e-30

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 129.19  E-value: 1.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  476 HLFEEEARrvPDAVAL-DAGSN-VVSYGELNRRADKLAHML-RLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPL 552
Cdd:PLN02574   45 FIFSHHNH--NGDTALiDSSTGfSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTM 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  553 DPAYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDE----DLGRPD----------ERDAAPNDNVSAENLAY 618
Cdd:PLN02574  123 NPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPEnydfDSKRIEfpkfyelikeDFDFVPKPVIKQDDVAA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNVVRLVR------GSSFATFGPDQVFLMMAPA--AFDASTFEIwGALLHGARLVLFppESP 690
Cdd:PLN02574  203 IMYSSGTTGASKGVVLTHRNLIAMVElfvrfeASQYEYPGSDNVYLAALPMfhIYGLSLFVV-GLLSLGSTIVVM--RRF 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  691 TPEEIGRVVREHGVTTLWLTAP----LFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTT 766
Cdd:PLN02574  280 DASDMVKVIDRFKVTHFPVVPPilmaLTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTA 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  767 FTTchdvsRGMGTGSV----PIGKPIANTHVYLLD-EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgv 841
Cdd:PLN02574  360 VGT-----RGFNTEKLskysSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW--- 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  842 pgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEV 921
Cdd:PLN02574  432 -----LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGST 506

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 260177242  922 PRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PLN02574  507 LSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 2006-2433 5.66e-30

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: 125.65  E-value: 5.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2006 LCYDGVppLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTR 2085
Cdd:cd05919     5 YAADRS--VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2086 PVCIVTDerhlgaveiaarqlgiehvvsldgdgkDADgnvvihgrraladladgnlpraagphnMAYVIFTSGSTGTPKG 2165
Cdd:cd05919    83 ARLVVTS---------------------------ADD---------------------------IAYLLYSSGTTGPPKG 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2166 VVERHSQVINLIEWVNRTYL-VGPSDRLLFVTSPSFDLSV-YDVFGMLAAGGSIHIASEddLRSPERLAAELGRGTITFW 2243
Cdd:cd05919   109 VMHAHRDPLLFADAMAREALgLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVL 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2244 DSAPAALQQLVPYFDRI-EDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGgATEA--TVWSNyfEVDGIDPRWTs 2320
Cdd:cd05919   187 YGVPTFYANLLDSCAGSpDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIG-ATEVghIFLSN--RPGAWRLGST- 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2321 ipyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFvpdpfSGEpgarLYRTGDLARFFRDGNI 2400
Cdd:cd05919   263 ---GRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-----NGG----WYRTGDKFCRDADGWY 330

                         410       420       430
                  ....*....|....*....|....*....|...
gi 260177242 2401 EFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:cd05919   331 THAGRADDMLKVGGQWVSPVEVESLIIQHPAVA 363
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 616-963 5.84e-30

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: 123.21  E-value: 5.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  616 LAYVMYTSGSTGKPKGVAVTHRNVVRLVRGS-SFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTPEE 694
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLhSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  695 IGRvvreHGVTTLWLTAPLFHAVADRGL--DQLRGVRQLLAGGDVLSPKHVARVL-LGLPalrLINGYGPTEnTTFTTCH 771
Cdd:cd17630    82 LAP----PGVTHVSLVPTQLQRLLDSGQgpAALKSLRAVLLGGAPIPPELLERAAdRGIP---LYTTYGMTE-TASQVAT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  772 DVSRGMGTGSVpiGKPIANTHVYLLDEqmnpvppnavGELFTGGDGLARGYHERPdqtaerfVPDPFsgvPGARLYRTGD 851
Cdd:cd17630   154 KRPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEF---NEDGWFTTKD 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  852 LARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPrfSELRKFL 931
Cdd:cd17630   212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP--AELRAWL 289

                         330       340       350
                  ....*....|....*....|....*....|..
gi 260177242  932 LQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd17630   290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 2014-2435 9.97e-30

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: 127.01  E-value: 9.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP----RWP------LERVAAVLGt 2083
Cdd:cd05906    40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPnarlrkLRHIWQLLG- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2084 tRPVCIVTDERHLGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHgrraladladgnlprAAGPHNMAYVIFTSGSTGTP 2163
Cdd:cd05906   119 -SPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLP---------------QSRPDDLALLMLTSGSTGFP 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2164 KGVVERHSQVINLIEWVNRTYLVGPSDRLL------FVTSpsfdLSVYDVFGMLAAGGSIHIASEDDLRSPERLA--AEL 2235
Cdd:cd05906   183 KAVPLTHRNILARSAGKIQHNGLTPQDVFLnwvpldHVGG----LVELHLRAVYLGCQQVHVPTEEILADPLRWLdlIDR 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2236 GRGTITFwdsAPA-ALQQLVPYFDRIEDG----SQLRLAFLSGDWVPIGMLDELRRAF-----PNVKLVGLGGATEA--- 2302
Cdd:cd05906   259 YRVTITW---APNfAFALLNDLLEEIEDGtwdlSSLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPAFGMTETcsg 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2303 TVWSNYFEVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepg 2382
Cdd:cd05906   336 VIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW----- 410

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2383 arlYRTGDLArFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQRG 2435
Cdd:cd05906   411 ---FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPS 459
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 488-971 1.83e-29

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 125.40  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  488 AVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHD 567
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  568 AGVQIVLS----AAGAEERLGEGPWTVVRLDEDLGR-------PDERDAAPNDNVSAENLAYVM-YTSGSTGKPKGV--A 633
Cdd:PRK08276   82 SGAKVLIVsaalADTAAELAAELPAGVPLLLVVAGPvpgfrsyEEALAAQPDTPIADETAGADMlYSSGTTGRPKGIkrP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  634 VTHRNV-----VRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFppESPTPEEIGRVVREHGVTTLW 708
Cdd:PRK08276  162 LPGLDPdeapgMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVM--EKFDAEEALALIERYRVTHSQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  709 LTAPLFHavadRGLDQLRGVRqllAGGDVLS-----------PKHVARvllglpalRLINGYGP--------TE--NTTF 767
Cdd:PRK08276  240 LVPTMFV----RMLKLPEEVR---ARYDVSSlrvaihaaapcPVEVKR--------AMIDWWGPiiheyyasSEggGVTV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  768 TTCHDVSRGMGTgsvpIGKPIANThVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGVpgarly 847
Cdd:PRK08276  305 ITSEDWLAHPGS----VGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTV------ 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  848 rtGDLArYLpngDME---FLGRRDGQVKIR-GFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAyVV----GREA 919
Cdd:PRK08276  374 --GDVG-YL---DEDgylYLTDRKSDMIISgGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVqpadGADA 446

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242  920 EVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGR 971
Cdd:PRK08276  447 GDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGR 498
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1989-2431 1.87e-29

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 125.68  E-value: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALcYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPL 2068
Cdd:PRK06187    8 IGRILRHGARKHPDKEAV-YFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2069 DPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHGRRALADLADGNLP-RAAGP 2147
Cdd:PRK06187   87 NIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEELLAAASDTFDfPDIDE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2148 HNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTsPSFdlsvyDVFGM------LAAGGSIHIAS 2221
Cdd:PRK06187  167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIV-PMF-----HVHAWglpylaLMAGAKQVIPR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2222 EDDlrsPERLAAELGRGTITFWDSAPAALQQLVPYFD-RIEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGAT 2300
Cdd:PRK06187  241 RFD---PENLLDLIETERVTFFFAVPTIWQMLLKAPRaYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2301 EA--TVWSNYFEvDGIDPRWTsIPY--GRPIQNARYYVLDRSGNPCP--IGVTGDLYIGGTCVSFGYYADPSQTAERFVP 2374
Cdd:PRK06187  317 ETspVVSVLPPE-DQLPGQWT-KRRsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDG 394

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242 2375 DpfsgepgarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK06187  395 G---------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPA 442
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2021-2427 1.88e-29

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: 124.47  E-value: 1.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2021 GRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGayvpldprwpleRVAAVLGTTRPVCIVTDERHLGAVE 2100
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGG------------RLGLVFVPLNPTLKESVLRYLVADA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2101 IAARQLGIEHVVSLDGDGKDA--DGNVVIHGRRALADLADGNLPRAAGPhNMAYVIFTSGSTGTPKGVVERHSQVINLIE 2178
Cdd:cd05922    69 GGRIVLADAGAADRLRDALPAspDPGTVLDADGIRAARASAPAHEVSHE-DLALLLYTSGSTGSPKLVRLSHQNLLANAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2179 WVNrTYL-VGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIasEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPY- 2256
Cdd:cd05922   148 SIA-EYLgITADDRALTVLPLSYDYGLSVLNTHLLRGATLVL--TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLg 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2257 FDRIEDGSqLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDGIDPRWTSIpyGRPIQNARYYVLD 2336
Cdd:cd05922   225 FDPAKLPS-LRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILD 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2337 RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAErfvpdpfSGEPGARLYrTGDLARFFRDGNIEFLGRADSQVKIRGYR 2416
Cdd:cd05922   302 DDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRK-------EGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNR 373

                         410
                  ....*....|.
gi 260177242 2417 IECGEVEVALA 2427
Cdd:cd05922   374 ISPTEIEAAAR 384
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 2014-2431 3.47e-29

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: 123.22  E-value: 3.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagpHNMAYVIFTSGSTGTPKGVVERHS-- 2171
Cdd:cd05972    81 ------------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHSyp 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2172 --QVINLIEWVNrtylVGPSDRLLFVTSPSFDLSVY-DVFGMLAAGGSIHIASEDDLrSPERLAAELGRGTITFWDSAPA 2248
Cdd:cd05972   107 lgHIPTAAYWLG----LRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRF-DAERILELLERYGVTSFCGPPT 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2249 AL----QQLVPYFDRiedgSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEATVWSNYFEvdGIDPRWTSIpyG 2324
Cdd:cd05972   182 AYrmliKQDLSSYKF----SHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFP--DMPVKPGSM--G 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2325 RPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSF--GYYADPSQTAERFVPDpfsgepgarLYRTGDLARFFRDGNIEF 2402
Cdd:cd05972   253 RPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD---------YYLTGDRAYRDEDGYFWF 323

                         410       420
                  ....*....|....*....|....*....
gi 260177242 2403 LGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05972   324 VGRADDIIKSSGYRIGPFEVESALLEHPA 352
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 486-963 8.78e-29

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: 125.05  E-value: 8.78e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   486 PDAVAL-----DAG-SNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSE 559
Cdd:TIGR02188   71 PDKVAIiwegdEPGeVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAE 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   560 RLAFLAHDAGVQIVLSAAG-------------AEERLGEGPWTV------VRLDEDL-----GR--------PDERDAAP 607
Cdd:TIGR02188  151 ALADRINDAGAKLVITADEglrggkviplkaiVDEALEKCPVSVehvlvvRRTGNPVvpwveGRdvwwhdlmAKASAYCE 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   608 NDNVSAENLAYVMYTSGSTGKPKGV-----------AVTHRNVvrlvrgssfatFG--PDQVFLMMApaafD-----AST 669
Cdd:TIGR02188  231 PEPMDSEDPLFILYTSGSTGKPKGVlhttggyllyaAMTMKYV-----------FDikDGDIFWCTA----DvgwitGHS 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   670 FEIWGALLHGARLVLFP--PESPTPEEIGRVVREHGVTTLWlTAPlfhavadrgldqlRGVRQLLAGGDVLSPKHvarvl 747
Cdd:TIGR02188  296 YIVYGPLANGATTVMFEgvPTYPDPGRFWEIIEKHKVTIFY-TAP-------------TAIRALMRLGDEWVKKH----- 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   748 lGLPALRLINGYG-PTENTTFTTCHDVsrgMGTGSVPIG----------------------KPIANT------HVYLLDE 798
Cdd:TIGR02188  357 -DLSSLRLLGSVGePINPEAWMWYYKV---VGKERCPIVdtwwqtetggimitplpgatptKPGSATlpffgiEPAVVDE 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   799 QMNPVPPNAVGELFTGGD---GLARGYHERPdqtaERFVPDPFSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRG 875
Cdd:TIGR02188  433 EGNPVEGPGEGGYLVIKQpwpGMLRTIYGDH----ERFVDTYFSPFPG--YYFTGDGARRDKDGYIWITGRVDDVINVSG 506

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   876 FRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRfSELRKFLLQRL---------PDHMIPAavva 946
Cdd:TIGR02188  507 HRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPD-DELRKELRKHVrkeigpiakPDKIRFV---- 581

                          570
                   ....*....|....*..
gi 260177242   947 lDKLPLVPSGKLDRRAL 963
Cdd:TIGR02188  582 -PGLPKTRSGKIMRRLL 597
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 495-963 1.03e-28

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: 124.74  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  495 SNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVL 574
Cdd:cd05967    80 ERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  575 SA-AGAE---------------ERLGEGPWTVVRLDEDLGRPD----ERD---------AAPND--NVSAENLAYVMYTS 623
Cdd:cd05967   160 TAsCGIEpgkvvpykplldkalELSGHKPHHVLVLNRPQVPADltkpGRDldwsellakAEPVDcvPVAATDPLYILYTS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  624 GSTGKPKGVavthrnvVRLVRGSSFAT---------FGPDQVFlmmapaaFDAS--------TFEIWGALLHGARLVLF- 685
Cdd:cd05967   240 GTTGKPKGV-------VRDNGGHAVALnwsmrniygIKPGDVW-------WAASdvgwvvghSYIVYGPLLHGATTVLYe 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  686 --PPESPTPEEIGRVVREHGVTTLWlTAPL-FHAV--ADRGLDQLRGV-----RQLLAGGDVLSP--KHVARVLLGLPal 753
Cdd:cd05967   306 gkPVGTPDPGAFWRVIEKYQVNALF-TAPTaIRAIrkEDPDGKYIKKYdlsslRTLFLAGERLDPptLEWAENTLGVP-- 382

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  754 rLINGYGPTENTTFTTCHdvSRGMGTGSVPIG---KPIANTHVYLLDEQMNPVPPNAVGELFTGGDgLARGYHERPDQTA 830
Cdd:cd05967   383 -VIDHWWQTETGWPITAN--PVGLEPLPIKAGspgKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWKND 458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  831 ERFVPDPFSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRL 910
Cdd:cd05967   459 ERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVP 536

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  911 VAYVVGREAEVPRFSELRKFLLQRLPDHMIPAA----VVALDKLPLVPSGKLDRRAL 963
Cdd:cd05967   537 LGLVVLKEGVKITAEELEKELVALVREQIGPVAafrlVIFVKRLPKTRSGKILRRTL 593
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 621-960 1.09e-28

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: 120.08  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  621 YTSGSTGKPKGVAVTHRNVVrlvrGSSFAT-----FGPDQVflMMAPAAFdastFEIWG-------ALLHGARLVlFPPE 688
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIV----NNGYFIgerlgLTEQDR--LCIPVPL----FHCFGsvlgvlaCLTHGATMV-FPSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  689 SPTPEEIGRVVRE------HGVTTLW---LTAPLFhavADRGLDQLRGVrqlLAGGDVLSPKHVARVL--LGLPALRLin 757
Cdd:cd05917    78 SFDPLAVLEAIEKekctalHGVPTMFiaeLEHPDF---DKFDLSSLRTG---IMAGAPCPPELMKRVIevMNMKDVTI-- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  758 GYGPTENTTFTTCHDVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPP-NAVGELFTGGDGLARGYHERPDQTAERFVPD 836
Cdd:cd05917   150 AYGMTETSPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  837 pfsgvpgaRLYRTGDLARYLPNGDMEFLGR-RDgqVKIRGFR-IELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYV 914
Cdd:cd05917   230 --------GWLHTGDLAVMDEDGYCRIVGRiKD--MIIRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWI 299

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 260177242  915 VGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:cd05917   300 RLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 482-963 1.72e-28

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: 123.83  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVAL----DAGSN--VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPA 555
Cdd:cd05966    63 LKERGDKVAIiwegDEPDQsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  556 YPSERLAFLAHDAGVQIVLSAAG-------------AEERLGEGP-----WTVVRLDEDL----GR--------PDERDA 605
Cdd:cd05966   143 FSAESLADRINDAQCKLVITADGgyrggkviplkeiVDEALEKCPsvekvLVVKRTGGEVpmteGRdlwwhdlmAKQSPE 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  606 APNDNVSAENLAYVMYTSGSTGKPKGV-----------AVTHRNVVRLvrgssfatfGPDQVFLMMApaafD-----AST 669
Cdd:cd05966   223 CEPEWMDSEDPLFILYTSGSTGKPKGVvhttggyllyaATTFKYVFDY---------HPDDIYWCTA----DigwitGHS 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  670 FEIWGALLHGARLVLFP--PESPTPEEIGRVVREHGVTTLWlTAPlfhavadrgldqlRGVRQLLAGGDVLSPKHvarvl 747
Cdd:cd05966   290 YIVYGPLANGATTVMFEgtPTYPDPGRYWDIVEKHKVTIFY-TAP-------------TAIRALMKFGDEWVKKH----- 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  748 lGLPALRLINGYG-PTENTTFTTCHDVsrgMGTGSVPIG----------------------KPIANT------HVYLLDE 798
Cdd:cd05966   351 -DLSSLRVLGSVGePINPEAWMWYYEV---IGKERCPIVdtwwqtetggimitplpgatplKPGSATrpffgiEPAILDE 426

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  799 QMNPVPPNAVGELFTGGD--GLARGYHERPdqtaERFVPDPFSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGF 876
Cdd:cd05966   427 EGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKFPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGH 500

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  877 RIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVV---GREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLV 953
Cdd:cd05966   501 RLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKT 580

                         570
                  ....*....|
gi 260177242  954 PSGKLDRRAL 963
Cdd:cd05966   581 RSGKIMRRIL 590
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 4-438 2.75e-28

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: 120.66  E-value: 2.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSA--VDF 81
Cdd:cd19546     4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAarPEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   82 GVTDGSSWDEPtaaAWLQAEAARPFDL-RAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRA 160
Cdd:cd19546    84 PVVPATEEELP---ALLADRAAHLFDLtRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  161 ATLTPISRGFRDYLVWHRDLLA-SDDASALVRE----WAAMVGDLDvsTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMD 235
Cdd:cd19546   161 PERAPLPLQFADYALWERELLAgEDDRDSLIGDqiayWRDALAGAP--DELELPTDRPRPVLPSRRAGAVPLRLDAEVHA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  236 RVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQL-GVVGHMAGivPVPARIDAAATP--RAIIRE 312
Cdd:cd19546   239 RLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGDLeGMVGPFAR--PLALRTDLSGDPtfRELLGR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  313 LRNALRVTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAVFQeIRSfnEAIRPEGFGHM--LRWSRGPLGFEVevpselgSQ 390
Cdd:cd19546   317 VREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALD-VRD--DDNDPWDAPELpgLRTSPVPLGTEA-------ME 386

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242  391 LDLEVRCYDFFSSS-----VRTCWRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19546   387 LDLSLALTERRNDDgdpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAAD 439
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 498-934 2.78e-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: 121.31  E-value: 2.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAF-LAHDAGVQIVLsa 576
Cdd:cd17640     6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYiLNHSESVALVV-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  577 agaeerlgegpwtvvrldedlgrpderDAAPNDnvsaenLAYVMYTSGSTGKPKGVAVTHRNVV-RLVRGSSFATFGPDQ 655
Cdd:cd17640    84 ---------------------------ENDSDD------LATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGD 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  656 VFLMMAPA--AFD--ASTFEI-WGALLHGARLVLFPpesptpEEIGRVVrehgvTTLWLTAP-LFHAVADRGLDQLRG-- 727
Cdd:cd17640   131 RFLSILPIwhSYErsAEYFIFaCGCSQAYTSIRTLK------DDLKRVK-----PHYIVSVPrLWESLYSGIQKQVSKss 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  728 -VRQLLAGGDVLS-------------PKHVARVL--LGLPalrLINGYGPTENTTFTTCHDVSRGMgTGSVpiGKPIANT 791
Cdd:cd17640   200 pIKQFLFLFFLSGgifkfgisgggalPPHVDTFFeaIGIE---VLNGYGLTETSPVVSARRLKCNV-RGSV--GRPLPGT 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  792 HVYLLDEQMN-PVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGR-RDG 869
Cdd:cd17640   274 EIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW--------FNTGDLGWLTCGGELVLTGRaKDT 345

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIArEDRpgdKRLVAYVvgreaeVPRFSELRKFLLQR 934
Cdd:cd17640   346 IVLSNGENVEPQPIEEALMRSPFIEQIMVVG-QDQ---KRLGALI------VPNFEELEKWAKES 400
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 2014-2431 5.53e-28

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: 119.79  E-value: 5.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHlgaveiaarqlgiehvvsldgdgkdadgnvvihGRRALADLadgnlpraagPHNMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd05903    82 RF---------------------------------RQFDPAAM----------PDAVALLLFTSGTTGEPKGVMHSHNTL 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLIEWVNRTYLVGPSDRLLfVTSP--SFDLSVYDVFGMLAAGGSIHIaseDDLRSPERLAAELGRGTITFWDSAPAALQ 2251
Cdd:cd05903   119 SASIRQYAERLGLGPGDVFL-VASPmaHQTGFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFLT 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2252 QLVPYFDRI-EDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEATVWSNYFEVDGIDPRWTSipYGRPIQNA 2330
Cdd:cd05903   195 DLLNAVEEAgEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLYT--DGRPLPGV 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2331 RYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAeRFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRAdSQV 2410
Cdd:cd05903   272 EIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTA-DAAPEGW--------FRTGDLARLDEDGYLRITGRS-KDI 341

                         410       420
                  ....*....|....*....|..
gi 260177242 2411 KIR-GYRIECGEVEVALAQHPG 2431
Cdd:cd05903   342 IIRgGENIPVLEVEDLLLGHPG 363
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 469-956 6.51e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 121.39  E-value: 6.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  469 PRERCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGA 548
Cdd:PRK06164    7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  549 YVPLDPAYPSERLAFLAHDAGVQIVLSAAGAE-----ERLGE-----------------------GPWTVVRLDE-DLGR 599
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGFKgidfaAILAAvppdalpplraiavvddaadatpAPAPGARVQLfALPD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  600 PDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFA-TFGPDQVFLMMAP--AAFDASTfeIWGAL 676
Cdd:PRK06164  167 PAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAyGYDPGAVLLAALPfcGVFGFST--LLGAL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  677 LHGARLVLFPPESPTPEeiGRVVREHGVTtlwltaplfHAVAD----RGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPA 752
Cdd:PRK06164  245 AGGAPLVCEPVFDAART--ARALRRHRVT---------HTFGNdemlRRILDTAGERADFPSARLFGFASFAPALGELAA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  753 LRLING------YGPTENTTFTTCHDVSRGMGTGSVPIGKPI-ANTHVYLLDEQMNPV-PPNAVGELFTGGDGLARGYHE 824
Cdd:PRK06164  314 LARARGvpltglYGSSEVQALVALQPATDPVSVRIEGGGRPAsPEARVRARDPQDGALlPDGESGEIEIRAPSLMRGYLD 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  825 RPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREdR 904
Cdd:PRK06164  394 NPDATARALTDDGY--------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-R 464

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242  905 PGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSG 956
Cdd:PRK06164  465 DGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 486-957 2.32e-27

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: 118.94  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVL--SAAGAEERLGEG-PWtvvrldEDLGRP-DERDA-APNdnvsaenlayvmYTSGSTGKPKGVAVTHRNVV 640
Cdd:cd12118    98 RHSEAKVLFvdREFEYEDLLAEGdPD------FEWIPPaDEWDPiALN------------YTSGTTGRPKGVVYHHRGAY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  641 rLVRGSSFATFGPDQ--VFLMMAPAaFDAS--TFeIWGALLHGARLVLFPpeSPTPEEIGRVVREHGVTTLWLTAPLFHA 716
Cdd:cd12118   160 -LNALANILEWEMKQhpVYLWTLPM-FHCNgwCF-PWTVAAVGGTNVCLR--KVDAKAIYDLIEKHKVTHFCGAPTVLNM 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  717 VAD------RGLDqlRGVRQLLAGgdvlSPKHvARVLLGLPAL--RLINGYGPTENTtfttchdvsrgmGTGSVPIGKP- 787
Cdd:cd12118   235 LANappsdaRPLP--HRVHVMTAG----APPP-AAVLAKMEELgfDVTHVYGLTETY------------GPATVCAWKPe 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  788 --------------------IANTHVYLLD-EQMNPVPPNA--VGELFTGGDGLARGYHERPDQTAERFVpdpfSGVpga 844
Cdd:cd12118   296 wdelpteerarlkarqgvryVGLEEVDVLDpETMKPVPRDGktIGEIVFRGNIVMKGYLKNPEATAEAFR----GGW--- 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  845 rlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRF 924
Cdd:cd12118   369 --FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE 446

                         490       500       510
                  ....*....|....*....|....*....|...
gi 260177242  925 SELRKFLLQRLPDHMIPAAVVALDkLPLVPSGK 957
Cdd:cd12118   447 EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 470-960 2.87e-27

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 119.49  E-value: 2.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  470 RERCLHHLFEEEARRVPDAVALDAGSNVV--SYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGG 547
Cdd:PRK12583   16 LTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  548 AYVPLDPAYPSERLAFLAHDAGVQIVLSAAG-------------------------AEERLGEGPWtVVRLD-------- 594
Cdd:PRK12583   96 ILVNINPAYRASELEYALGQSGVRWVICADAfktsdyhamlqellpglaegqpgalACERLPELRG-VVSLApapppgfl 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  595 ---EDLGRPD----ERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV---RLVrGSSFATFGPDQvflMMAPAA 664
Cdd:PRK12583  175 awhELQARGEtvsrEALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILnngYFV-AESLGLTEHDR---LCVPVP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  665 FdastFEIWGALL-------HGARLVlFPPESPTPEEIGRVVRE------HGVTTLWLtAPLFHAvaDRGLDQLRGVRQL 731
Cdd:PRK12583  251 L----YHCFGMVLanlgcmtVGACLV-YPNEAFDPLATLQAVEEerctalYGVPTMFI-AELDHP--QRGNFDLSSLRTG 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  732 LAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGEL 811
Cdd:PRK12583  323 IMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGEL 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  812 FTGGDGLARGYHERPDQTAErfvpdpfsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHP 891
Cdd:PRK12583  403 CTRGYSVMKGYWNNPEATAE--------SIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHP 474

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  892 ALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:PRK12583  475 AVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1537-1931 3.07e-27

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: 117.36  E-value: 3.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1537 PLTPLQEGILF-HALLEpGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFlWEGVPEPLQVVRRLVRIPTER 1615
Cdd:cd20483     3 PMSTFQRRLWFlHNFLE-DKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAY-FEGDDFGEQQVLDDPSFHLIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1616 IDArSMAVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQHe 1695
Cdd:cd20483    81 IDL-SEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1696 AAHRTAPRPHRDYV-------AWLRGADAQSVERFWRRELGGFREVTPL----GIDRPPAGQRASSYRRFerALDEHTTA 1764
Cdd:cd20483   159 RDLATVPPPPVQYIdftlwhnALLQSPLVQPLLDFWKEKLEGIPDASKLlpfaKAERPPVKDYERSTVEA--TLDKELLA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1765 RLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPleGIERMVGLFINTVPMRAVVDPERPIGEWLTEL 1844
Cdd:cd20483   237 RMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHP--DFDDLVGFFVNMLPIRCRMDCDMSFDDLLEST 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1845 QGRRAErtAYEHASLA---QVQAwSEVPHGSALFESLIVVENYPV---APAFSGDELSVRLVGGDE-QTNYPVTLVAL-- 1915
Cdd:cd20483   315 KTTCLE--AYEHSAVPfdyIVDA-LDVPRSTSHFPIGQIAVNYQVhgkFPEYDTGDFKFTDYDHYDiPTACDIALEAEed 391

                         410       420
                  ....*....|....*....|.
gi 260177242 1916 PGRRLTLRL-----LYEAERI 1931
Cdd:cd20483   392 PDGGLDLRLefsttLYDSADM 412
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 2009-2431 4.27e-27

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: 118.18  E-value: 4.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2009 DGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVC 2088
Cdd:cd05926    10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2089 IVTDERHLGAVEIAARQLGIEHV--VSLDGDGKDADGNVVIHGRraLADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGV 2166
Cdd:cd05926    90 VLTPKGELGPASRAASKLGLAILelALDVGVLIRAPSAESLSNL--LADKKNAKSEGVPLPDDLALILHTSGTTGRPKGV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2167 VERHSQVINLIEWVNRTYLVGPSDRLLFVtspsfdLSVYDVFGM-------LAAGGSIHIaseddlrsPERLAAElgrgt 2239
Cdd:cd05926   168 PLTHRNLAASATNITNTYKLTPDDRTLVV------MPLFHVHGLvasllstLAAGGSVVL--------PPRFSAS----- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2240 iTFWD----------SA-PAALQQL--VPYFDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEAT--V 2304
Cdd:cd05926   229 -TFWPdvrdynatwyTAvPTIHQILlnRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAhqM 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2305 WSNYFEVDGIDPRwtsiPYGRPiQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgar 2384
Cdd:cd05926   307 TSNPLPPGPRKPG----SVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------- 374

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 260177242 2385 lYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05926   375 -FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPA 420
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1536-1856 7.10e-27

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: 116.31  E-value: 7.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1536 YPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVpEPLQVVRRLVRIPTER 1615
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEG-EPYQWIDPYTPVPIRH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1616 IDARSMAvDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQHE 1695
Cdd:cd19533    81 IDLSGDP-DPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1696 AAHRTAPRPHRDYV---AWLRGADAQSVER-FWRRELGGFREVTPLGidrPPAGQRASSYRRFERALDEHTTARLEQVLR 1771
Cdd:cd19533   160 PAPPAPFGSFLDLVeeeQAYRQSERFERDRaFWTEQFEDLPEPVSLA---RRAPGRSLAFLRRTAELPPELTRTLLEAAE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1772 ERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGR--SAPLEgierMVGLFINTVPMRAVVDPERPIGEWLTELqgRRA 1849
Cdd:cd19533   237 AHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAARQ----TPGMVANTLPLRLTVDPQQTFAELVAQV--SRE 310


                  ....*..
gi 260177242 1850 ERTAYEH 1856
Cdd:cd19533   311 LRSLLRH 317
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1536-1845 8.20e-27

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: 116.26  E-value: 8.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1536 YPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWE-GVPepLQVVRRLVRIPTE 1614
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEdGVP--FQKIEPSKPLSFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1615 RIDARSMavdgDAW-IVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRY---SG 1690
Cdd:cd20484    80 EEDISSL----KESeIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqalLQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1691 GMQHEAAHRTAprPHRDYVAW----LRGADAQSVERFWRRELGGFREVTPLGIDRPpagqRASSyRRFE-----RALDEH 1761
Cdd:cd20484   156 GKQPTLASSPA--SYYDFVAWeqdmLAGAEGEEHRAYWKQQLSGTLPILELPADRP----RSSA-PSFEgqtytRRLPSE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1762 TTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRsaPLEGIERMVGLFINTVPMRAVVDPERPIGEWL 1841
Cdd:cd20484   229 LSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR--PEERFDSLIGYFINMLPIRSRILGEETFSDFI 306


                  ....
gi 260177242 1842 TELQ 1845
Cdd:cd20484   307 RKLQ 310
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 465-963 1.17e-26

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 117.43  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  465 ASDYPRercLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLK 544
Cdd:PRK07059   19 ASQYPS---LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  545 AGGAYVPLDPAYPSERLAFLAHDAGVQ--IVLS--AAGAEERLGEGP--------------------------------- 587
Cdd:PRK07059   96 AGYVVVNVNPLYTPRELEHQLKDSGAEaiVVLEnfATTVQQVLAKTAvkhvvvasmgdllgfkghivnfvvrrvkkmvpa 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  588 WTV---VRLDEDLGRPDERDAAPnDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSS------FATFG-PDQVF 657
Cdd:PRK07059  176 WSLpghVRFNDALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqpaFEKKPrPDQLN 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  658 LMMAPAAFD--ASTFEIWGALLHGARLVLFPpespTPEEIGRVVRE---------HGVTTLW---LTAPLFHAVADRGLd 723
Cdd:PRK07059  255 FVCALPLYHifALTVCGLLGMRTGGRNILIP----NPRDIPGFIKElkkyqvhifPAVNTLYnalLNNPDFDKLDFSKL- 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  724 qlrgvrQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSvpIGKPIANTHVYLLDEQMNPV 803
Cdd:PRK07059  330 ------IVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGT--IGLPLPSTEVSIRDDDGNDL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  804 PPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEV 883
Cdd:PRK07059  402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF--------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEI 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  884 EAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRfSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK07059  474 EEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTE-EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 501-963 1.28e-26

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: 116.32  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  501 GELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAGae 580
Cdd:cd05929    21 DVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCGLFT-- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  581 erLGEGPWTVVRLDEDLGRPDErdaAPNDNVSAENlaYVMYTSGSTGKPKGVAVTHRNV---VRLVRGSSF-ATFGPDQV 656
Cdd:cd05929    99 --GGGALDGLEDYEAAEGGSPE---TPIEDEAAGW--KMLYSGGTTGRPKGIKRGLPGGppdNDTLMAAALgFGPGADSV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  657 FLMMAPAAFDASTFEIWGALLHGARLVLFppESPTPEEIGRVVREHGVTTLWLTAPLFHAV-----ADRGLDQLRGVRQL 731
Cdd:cd05929   172 YLSPAPLYHAAPFRWSMTALFMGGTLVLM--EKFDPEEFLRLIERYRVTFAQFVPTMFVRLlklpeAVRNAYDLSSLKRV 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  732 LAGGDVLSPKhVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSVpiGKPIANThVYLLDEQMNPVPPNAVGEL 811
Cdd:cd05929   250 IHAAAPCPPW-VKEQWIDWGGPIIWEYYGGTEGQGLTIINGEEWLTHPGSV--GRAVLGK-VHILDEDGNEVPPGEIGEV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  812 -FTGGDGLArgYHERPDQTAERFVPDPFSGVpgarlyrtGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQH 890
Cdd:cd05929   326 yFANGPGFE--YTNDPEKTAAARNEGGWSTL--------GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242  891 PALREAVVIAREDRPGDKRLVAYV---VGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05929   396 PKVLDAAVVGVPDEELGQRVHAVVqpaPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 486-963 1.64e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 116.42  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGvGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLA 565
Cdd:PRK07638   15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  566 HDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVM-YTSGSTGKPKGVAVTHRNVVrlvr 644
Cdd:PRK07638   94 AISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQNAPFYMgFTSGSTGKPKAFLRAQQSWL---- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  645 gSSFA----TFGPDQVFLMMAPAAFDASTFeIWGA---LLHGARLVLFPPESPTPE----EIGRVVREHGVTTLwLTAPL 713
Cdd:PRK07638  170 -HSFDcnvhDFHMKREDSVLIAGTLVHSLF-LYGAistLYVGQTVHLMRKFIPNQVldklETENISVMYTVPTM-LESLY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 fhaVADRGLDQlrgVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSVpiGKPIANTHV 793
Cdd:PRK07638  247 ---KENRVIEN---KMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDEESERRPNSV--GRPFHNVQV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  794 YLLDEQMNPVPPNAVGELFTGGDGLARGYherpdqtaerfvpdpfsgVPGARLYRTGDLARYLPNGDMEFL--------- 864
Cdd:PRK07638  319 RICNEAGEEVQKGEIGTVYVKSPQFFMGY------------------IIGGVLARELNADGWMTVRDVGYEdeegfiyiv 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  865 GRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEvprfSELRKFLLQRLPDHMIPAAV 944
Cdd:PRK07638  381 GREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATK----QQLKSFCLQRLSSFKIPKEW 456

                         490
                  ....*....|....*....
gi 260177242  945 VALDKLPLVPSGKLDRRAL 963
Cdd:PRK07638  457 HFVDEIPYTNSGKIARMEA 475
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1537-1856 2.06e-26

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: 115.05  E-value: 2.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1537 PLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGvPEPLQVVR----RLVRIP 1612
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEED-GVPYQLILeedeATPKLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1613 TERIDARSMAvdgdawivERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGM 1692
Cdd:cd19538    82 IKEVDEEELE--------SEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARC 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1693 QHEAAHRTA-PRPHRDYVAWLR------GADAQSVER---FWRRELGGFREVTPLGIDRP-PAgqrASSYR----RFEra 1757
Cdd:cd19538   154 KGEAPELAPlPVQYADYALWQQellgdeSDPDSLIARqlaYWKKQLAGLPDEIELPTDYPrPA---ESSYEggtlTFE-- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1758 LDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAplEGIERMVGLFINTVPMRAVV--DPEr 1835
Cdd:cd19538   229 IDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRTDTsgNPS- 305

                         330       340
                  ....*....|....*....|...
gi 260177242 1836 pigewLTELQGR--RAERTAYEH 1856
Cdd:cd19538   306 -----FRELLERvkETNLEAYEH 323
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 615-960 3.39e-26

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: 111.73  E-value: 3.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRnvvrlvrgsSFATFGPDQVFLMMAPAAfdaSTFEIWGALLH-----GARLVLFPPES 689
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSER---------SWIESFVCNEDLFNISGE---DAILAPGPLSHslflyGAISALYLGGT 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 ------PTPEEIGRVVREHGVTTLWLTAPLFHAVAdRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTE 763
Cdd:cd17633    69 figqrkFNPKSWIRKINQYNATVIYLVPTMLQALA-RTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  764 nTTFTT--CHDVSRGmgTGSVpiGKPIANTHVYLLDEQmnpvpPNAVGELFTGGDGLARGYherpdqTAERFV-PDPFsg 840
Cdd:cd17633   148 -LSFITynFNQESRP--PNSV--GRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGY------VRGGFSnPDGW-- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  841 vpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAE 920
Cdd:cd17633   210 ------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLT 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 260177242  921 VPrfsELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:cd17633   284 YK---QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 2004-2430 4.27e-26

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 116.15  E-value: 4.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2004 VALCY---DGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:PRK04319   61 VALRYldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDR 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTTRPVCIVTDERHLGAVeIAARQLGIEHVVSLDGDGKDADGnvVIHGRRALADLADGNLPRAAGPHNMAYVIFTSGST 2160
Cdd:PRK04319  141 LEDSEAKVLITTPALLERK-PADDLPSLKHVLLVGEDVEEGPG--TLDFNALMEQASDEFDIEWTDREDGAILHYTSGST 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERHSQVInlIEWVNRTYLVG--PSDRLL------FVTSPSfdlsvYDVFGMLAAGGSIHIASEDdlRSPERLA 2232
Cdd:PRK04319  218 GKPKGVLHVHNAML--QHYQTGKYVLDlhEDDVYWctadpgWVTGTS-----YGIFAPWLNGATNVIDGGR--FSPERWY 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2233 AELGRGTITFWDSAPAALQQLvpyfdriedgsqlrlaflsgdwvpIGMLDELRR--AFPNVKLVGLGGAT---EATVW-- 2305
Cdd:PRK04319  289 RILEDYKVTVWYTAPTAIRML------------------------MGAGDDLVKkyDLSSLRHILSVGEPlnpEVVRWgm 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2306 ---------------------SNYFEVDgIDPrwTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYI--GGTCVSFGYY 2362
Cdd:PRK04319  345 kvfglpihdnwwmtetggimiANYPAMD-IKP--GSM--GKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIW 419

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 2363 ADPSQTAERFVPDpfsgepgarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK04319  420 NNPEKYESYFAGD---------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHP 478
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 475-951 6.58e-26

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 114.59  E-value: 6.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  475 HHLFE--EEARRVPDAVALDAGSN-VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVP 551
Cdd:PRK07514    3 NNLFDalRAAFADRDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  552 LDPAYPSERLAFLAHDAGVQIVLSAAGAEERLGE-----GPWTVVRLDED---------LGRPDERDAAPndnVSAENLA 617
Cdd:PRK07514   83 LNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKiaaaaGAPHVETLDADgtgslleaaAAAPDDFETVP---RGADDLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  618 YVMYTSGSTGKPKGVAVTHRNVvrlvrGSSFAT------FGPDQVFLMMAP-----AAFDASTfeiwGALLHGARLVLFP 686
Cdd:PRK07514  160 AILYTSGTTGRSKGAMLSHGNL-----LSNALTlvdywrFTPDDVLIHALPifhthGLFVATN----VALLAGASMIFLP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  687 PESPtpeeiGRVVREHGVTTLWLTAPLFHA--VADRGLDQ--LRGVRQLLAGGDVLSPK-HVA-RVLLGLPAL-RlingY 759
Cdd:PRK07514  231 KFDP-----DAVLALMPRATVMMGVPTFYTrlLQEPRLTReaAAHMRLFISGSAPLLAEtHREfQERTGHAILeR----Y 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  760 GPTENTTFTTC-HDVSRGMGTgsvpIGKPIANTHVYLLD-EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDP 837
Cdd:PRK07514  302 GMTETNMNTSNpYDGERRAGT----VGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  838 FsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGR 917
Cdd:PRK07514  378 F--------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPK 449

                         490       500       510
                  ....*....|....*....|....*....|....
gi 260177242  918 EAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLP 951
Cdd:PRK07514  450 PGAALDEAAILAALKGRLARFKQPKRVFFVDELP 483
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 491-904 7.36e-26

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: 113.69  E-value: 7.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  491 LDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGV 570
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  571 QIVLSAagaeerlgegpwtvvrlDEDlgrpderdaapndnvsaeNLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG-SSFA 649
Cdd:cd05914    81 KAIFVS-----------------DED------------------DVALINYTSGTTGNSKGVMLTYRNIVSNVDGvKEVV 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  650 TFGPDQVFLMMAPAAFD-ASTFEIWGALLHGARLVLFPpESPTPEEIG----RVVREHGVTTLW---------------- 708
Cdd:cd05914   126 LLGKGDKILSILPLHHIyPLTFTLLLPLLNGAHVVFLD-KIPSAKIIAlafaQVTPTLGVPVPLviekifkmdiipkltl 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  709 ------LTAPLF-----HAVADRGLDQLRG-VRQLLAGGDVLSPKhVARVL--LGLPAlrlINGYGPTEnTTFTTCHDVS 774
Cdd:cd05914   205 kkfkfkLAKKINnrkirKLAFKKVHEAFGGnIKEFVIGGAKINPD-VEEFLrtIGFPY---TIGYGMTE-TAPIISYSPP 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  775 RGMGTGSVpiGKPIANTHVYLLDeqmnPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLAR 854
Cdd:cd05914   280 NRIRLGSA--GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW--------FHTGDLGK 345

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 260177242  855 YLPNGDMEFLGRRDGQ-VKIRGFRIELAEVEAALLQHPALREAVVIAREDR 904
Cdd:cd05914   346 IDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKK 396
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 1991-2431 8.12e-26

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: 113.81  E-value: 8.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP 2070
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRK-LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 RWPLERVAAVLGttrpvcivtderhlgaveiaarqlgiehvvslDGDGKDAdgnVVIHG-RRALADLADGNLPRAAGPHN 2149
Cdd:cd05936    82 LYTPRELEHILN--------------------------------DSGAKAL---IVAVSfTDLLAAGAPLGERVALTPED 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2150 MAYVIFTSGSTGTPKGVVERHSQ-VINL---IEWVNRtyLVGPSDRLLFVtspsfdLSVYDVFGM-------LAAGGSIH 2218
Cdd:cd05936   127 VAVLQYTSGTTGVPKGAMLTHRNlVANAlqiKAWLED--LLEGDDVVLAA------LPLFHVFGLtvalllpLALGATIV 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2219 IASEDDlrsPERLAAELGRGTITFWDSAPAALQQLVPYFDRIE-DGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLG 2297
Cdd:cd05936   199 LIPRFR---PIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKrDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGY 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2298 GATEA--TVWSNYFEvdgIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPD 2375
Cdd:cd05936   275 GLTETspVVAVNPLD---GPRKPGSI--GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG 349

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 2376 PFsgepgarlyRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05936   350 WL---------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPA 396
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 499-867 1.56e-25

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: 113.85  E-value: 1.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  499 SYGELNRRADKLAHMLRLKGV--GTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSA 576
Cdd:cd05927     7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  577 AGaeerlgegpWTVVRLDE--DLGRPDERDAAPNDnvsAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT---- 650
Cdd:cd05927    87 AG---------VKVYSLEEfeKLGKKNKVPPPPPK---PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeiln 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  651 -FGPDQVFLMMAPAafdASTFE---IWGALLHGARLVLF---PPE--------SPT-----PEEIGRV---VREHGVTTL 707
Cdd:cd05927   155 kINPTDVYISYLPL---AHIFErvvEALFLYHGAKIGFYsgdIRLllddikalKPTvfpgvPRVLNRIydkIFNKVQAKG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  708 WLTAPLFHAVADRGLDQLRG------------------------VRQLLAGGDVLSPkHV---ARVLLGLPalrLINGYG 760
Cdd:cd05927   232 PLKRKLFNFALNYKLAELRSgvvraspfwdklvfnkikqalggnVRLMLTGSAPLSP-EVlefLRVALGCP---VLEGYG 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  761 PTENT--TFTTCHDVsrgMGTGSVpiGKPIANTHVYLLD-EQMN--PVPPNAVGELFTGGDGLARGYHERPDQTAERFVP 835
Cdd:cd05927   308 QTECTagATLTLPGD---TSVGHV--GGPLPCAEVKLVDvPEMNydAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDE 382

                         410       420       430
                  ....*....|....*....|....*....|..
gi 260177242  836 DPFsgvpgarlYRTGDLARYLPNGDMEFLGRR 867
Cdd:cd05927   383 DGW--------LHTGDIGEWLPNGTLKIIDRK 406
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 1979-2434 1.80e-25

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: 112.81  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1979 TARAYARERCIHELFESSVERSPGSVALCyDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGI 2058
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVV-DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2059 LKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIA-ARQLgiehvvsldgdgkdadgnvvihgrraLADLA 2137
Cdd:cd05920    86 LRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRAlAREL--------------------------AESIP 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2138 DgnlpraagphnMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPS--FDLSVYDVFGMLAAGG 2215
Cdd:cd05920   140 E-----------VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGG 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2216 SIHIASEDdlrSPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEDG-SQLRLAFLSGDWVPIGMLDELRRAFpNVKLV 2294
Cdd:cd05920   209 RVVLAPDP---SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADlSSLRLLQVGGARLSPALARRVPPVL-GCTLQ 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2295 GLGGATEATVwsNYFEVDgiDPRWTSI-PYGRPIQ-NARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERF 2372
Cdd:cd05920   285 QVFGMAEGLL--NYTRLD--DPDEVIIhTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF 360

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242 2373 VPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd05920   361 TPDGF--------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD 414
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 469-963 2.56e-25

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 115.41  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  469 PRERCLHHLFEEEARRVPDAVAL-DAGSNVVSYGELNRRADKLAHMLRlKGVGTETRVGLCLERSVELVVGILGVLKAGG 547
Cdd:PRK08633  612 EALPPLAEAWIDTAKRNWSRLAVaDSTGGELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAGK 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  548 AYVPLDpaYPSERLAFLA--HDAGVQIVLSAAGAEERLGEGPWTV-------VRLDEDLG-RPDERD------------- 604
Cdd:PRK08633  691 VPVNLN--YTASEAALKSaiEQAQIKTVITSRKFLEKLKNKGFDLelpenvkVIYLEDLKaKISKVDkltallaarllpa 768

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  605 ----AAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRN----------VVRLVRGSS-------FATFGpdqvflmmapa 663
Cdd:PRK08633  769 rllkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNilsnieqisdVFNLRNDDVilsslpfFHSFG----------- 837

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  664 aFDASTfeiWGALLHGARLVLFPpeSPT-PEEIGRVVREHGVTTLWLTAPLFHAVAdRGL----DQLRGVRQLLAGGDVL 738
Cdd:PRK08633  838 -LTVTL---WLPLLEGIKVVYHP--DPTdALGIAKLVAKHRATILLGTPTFLRLYL-RNKklhpLMFASLRLVVAGAEKL 910

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  739 SPKhVARVLLGLPALRLINGYGPTENTTFTTCH-------DVSRGMGT--GSVpiGKPIANTHVYLLD-EQMNPVPPNAV 808
Cdd:PRK08633  911 KPE-VADAFEEKFGIRILEGYGATETSPVASVNlpdvlaaDFKRQTGSkeGSV--GMPLPGVAVRIVDpETFEELPPGED 987

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  809 GELFTGGDGLARGYHERPDQTAErFVPDpfsgVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVE---A 885
Cdd:PRK08633  988 GLILIGGPQVMKGYLGDPEKTAE-VIKD----IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelA 1062

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  886 ALLQHPALREAVVIAREDRPGDKrlVAYVVGREAEvpRFSELRKFLLQ-RLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK08633 1063 KALGGEEVVFAVTAVPDEKKGEK--LVVLHTCGAE--DVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1980-2431 4.86e-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: 112.16  E-value: 4.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1980 ARAYARERCIHELFESSVERSPGSVALCyDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGIL 2059
Cdd:COG1021    18 EAGYWRGETLGDLLRRRAERHPDRIAVV-DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2060 KTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLG------AVEIAARQLGIEHVVsLDGDGKDAdgnvvihgrRAL 2133
Cdd:COG1021    97 RAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyralARELQAEVPSLRHVL-VVGDAGEF---------TSL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2134 ADL----ADGNLPRAAgPHNMAYVIFTSGSTGTPKgvverhsqvinLIEWVNRTYL-----------VGPSDRLLfVTSP 2198
Cdd:COG1021   167 DALlaapADLSEPRPD-PDDVAFFQLSGGTTGLPK-----------LIPRTHDDYLysvrasaeicgLDADTVYL-AALP 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2199 ---SFDLSVYDVFGMLAAGGSIHIASEDdlrSPER----LAAElgRGTIT--------FWDSAPAAlqqlvpyfdRIEDG 2263
Cdd:COG1021   234 aahNFPLSSPGVLGVLYAGGTVVLAPDP---SPDTafplIERE--RVTVTalvpplalLWLDAAER---------SRYDL 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2264 SQLRLAFLSGDWVPigmlDELRRAFPNVklvgLG-------GATEATVwsNYFEVDgiDPRWTSIPY-GRPIQNA---Ry 2332
Cdd:COG1021   300 SSLRVLQVGGAKLS----PELARRVRPA----LGctlqqvfGMAEGLV--NYTRLD--DPEEVILTTqGRPISPDdevR- 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2333 yVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVkI 2412
Cdd:COG1021   367 -IVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDGYLVVEGRAKDQI-N 436

                         490       500
                  ....*....|....*....|
gi 260177242 2413 R-GYRIECGEVEVALAQHPG 2431
Cdd:COG1021   437 RgGEKIAAEEVENLLLAHPA 456
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2015-2430 9.57e-25

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: 110.21  E-value: 9.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDer 2094
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2095 hlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraaGPHNMAYVIFTSGSTGTPKGVVERHSQVI 2174
Cdd:cd05971    86 ---------------------------------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLL 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2175 NLIEWVNRTYLVGPSDRLLFVTSPSFDL--SVYDVFGMLAAGGSIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQ 2252
Cdd:cd05971   115 GHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKM 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2253 LVPYFDRIEDgSQLRLAFLSGDWVPIG--MLDELRRAFpNVKLVGLGGATEAT-VWSNYFEVDGIDPrwTSIpyGRPIQN 2329
Cdd:cd05971   195 MRQQGEQLKH-AQVKLRAIATGGESLGeeLLGWAREQF-GVEVNEFYGQTECNlVIGNCSALFPIKP--GSM--GKPIPG 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2330 ARYYVLDRSGNPCPIGVTGDLYIGGTC-VSF-GYYADPSQTAERFVPDPFsgepgarlyRTGDLARFFRDGNIEFLGRAD 2407
Cdd:cd05971   269 HRVAIVDDNGTPLPPGEVGEIAVELPDpVAFlGYWNNPSATEKKMAGDWL---------LTGDLGRKDSDGYFWYVGRDD 339

                         410       420
                  ....*....|....*....|...
gi 260177242 2408 SQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05971   340 DVITSSGYRIGPAEIEECLLKHP 362
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1978-2406 1.02e-24

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 112.12  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1978 DTARAYARERCIHELFESSVERSPGSVALCY--DGVP-PLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVA 2054
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkeDGIWqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2055 LLGILKTGGAYVPLDPRWPLERVAAVLGTTRP-VCIVTDERHLGAVEIAARQL-GIEHVVSLDGDGKDADGNVVI----- 2127
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAkVLFVEDQEQLDKLLEVRDELpSLRHIVVLDPRGLRDDPRLLSldell 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2128 -HGRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLfvtspSF-DLS-V 2204
Cdd:COG1022   162 aLGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-----SFlPLAhV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2205 YD---VFGMLAAGGSIHIASE-----DDLRS--P----------ERL-------AAELG--RGTITFWdsapaALQQLVP 2255
Cdd:COG1022   237 FErtvSYYALAAGATVAFAESpdtlaEDLREvkPtfmlavprvwEKVyagiqakAEEAGglKRKLFRW-----ALAVGRR 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2256 YFDRIEDGSQLRLaflsGDWVPIGMLDEL-----RRAF-PNVKLVGLGGA-----------------------TEATVWS 2306
Cdd:COG1022   312 YARARLAGKSPSL----LLRLKHALADKLvfsklREALgGRLRFAVSGGAalgpelarffralgipvlegyglTETSPVI 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2307 NYFEVDGIDPRwtSIpyGRPIQN--ARyyvldrsgnpcpIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgar 2384
Cdd:COG1022   388 TVNRPGDNRIG--TV--GPPLPGveVK------------IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------- 444

                         490       500
                  ....*....|....*....|..
gi 260177242 2385 lYRTGDLARFFRDGNIEFLGRA 2406
Cdd:COG1022   445 -LHTGDIGELDEDGFLRITGRK 465
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
466-963 1.06e-24

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 111.68  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  466 SDYPRE------RCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRR----ADKLAHMLRL-KGvgteTRVGLCLERSVE 534
Cdd:PRK08974   11 ADVPAEinpdryQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERsrafAAYLQNGLGLkKG----DRVALMMPNLLQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  535 LVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQ--IVLS--AAGAEE-------------RLGE----GPWTVV-- 591
Cdd:PRK08974   87 YPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKaiVIVSnfAHTLEKvvfktpvkhviltRMGDqlstAKGTLVnf 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  592 ------RLDEDLGRPDE---RDAAPND--------NVSAENLAYVMYTSGSTGKPKGVAVTHRNVVrlvrgssfatfgpd 654
Cdd:PRK08974  167 vvkyikRLVPKYHLPDAisfRSALHKGrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNML-------------- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  655 qVFLMMAPAAFdastfeiwGALLH-GARLV-----------------LFPPESPT------PEEIGRVVRE--------- 701
Cdd:PRK08974  233 -ANLEQAKAAY--------GPLLHpGKELVvtalplyhifaltvnclLFIELGGQnllitnPRDIPGFVKElkkypftai 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  702 HGVTTL---WLTAPLFHAVadrGLDQLRgvrqLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTC--HDVSRG 776
Cdd:PRK08974  304 TGVNTLfnaLLNNEEFQEL---DFSSLK----LSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVnpYDLDYY 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  777 MGTgsvpIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAErfvpdpfsgVPGARLYRTGDLARYL 856
Cdd:PRK08974  377 SGS----IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE---------VIKDGWLATGDIAVMD 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  857 PNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRfSELRKFLLQRLP 936
Cdd:PRK08974  444 EEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTE-EELITHCRRHLT 522

                         570       580
                  ....*....|....*....|....*..
gi 260177242  937 DHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK08974  523 GYKVPKLVEFRDELPKSNVGKILRREL 549
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 1994-2433 1.47e-24

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 110.82  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1994 ESSVERSPGSVALCYDGVPpLTYSDLNGRANRL-GWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRW 2072
Cdd:PRK08314   17 EVSARRYPDKTAIVFYGRA-ISYRELLEEAERLaGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2073 PLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVS------LDGDGKDA--DGNVVIHGRRALAD--------- 2135
Cdd:PRK08314   96 REEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVaqysdyLPAEPEIAvpAWLRAEPPLQALAPggvvawkea 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2136 LADGNLPRA--AGPHNMAYVIFTSGSTGTPKGVVERHSQVINLI----EWVNrtylvGPSDRLLFVTSPSFDLS--VYDV 2207
Cdd:PRK08314  176 LAAGLAPPPhtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAvgsvLWSN-----STPESVVLAVLPLFHVTgmVHSM 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2208 FGMLAAGGSIHIASeddlRSPERLAAEL-GRGTITFWDSAPAALQQLV--PYFDRiEDGSQLRLAFLSGDWVPIGMLDEL 2284
Cdd:PRK08314  251 NAPIYAGATVVLMP----RWDREAAARLiERYRVTHWTNIPTMVVDFLasPGLAE-RDLSSLRYIGGGGAAMPEAVAERL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2285 RRAFpNVKLVGLGGATE--ATVWSNyfevdgidprwtsiPYGRPIQN----------ARyyVLD-RSGNPCPIGVTGDLY 2351
Cdd:PRK08314  326 KELT-GLDYVEGYGLTEtmAQTHSN--------------PPDRPKLQclgiptfgvdAR--VIDpETLEELPPGEVGEIV 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2352 IGGTCVSFGYYADPSQTAERFVpdPFSGEpgaRLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK08314  389 VHGPQVFKGYWNRPEATAEAFI--EIDGK---RFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPA 463


                  ..
gi 260177242 2432 AQ 2433
Cdd:PRK08314  464 IQ 465
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 477-963 4.38e-24

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 109.47  E-value: 4.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLR-LKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPA 555
Cdd:PRK05677   29 VLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  556 YPSERLAFLAHDAGVQIVLSAAG----AEERLgegPWT----------------------------------------VV 591
Cdd:PRK05677  109 YTAREMEHQFNDSGAKALVCLANmahlAEKVL---PKTgvkhvivtevadmlpplkrllinavvkhvkkmvpayhlpqAV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  592 RLDEDLGRPDERDAAPNdNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV------RLVRGSSFAtfgpDQVFLMMAPA-- 663
Cdd:PRK05677  186 KFNDALAKGAGQPVTEA-NPQADDVAVLQYTGGTTGVAKGAMLTHRNLVanmlqcRALMGSNLN----EGCEILIAPLpl 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  664 ----AFdasTFEIWGALLHGARLVLFPpespTPEEIGRVVREH---------GVTTLWltAPLFHAVADRGLDqLRGVRQ 730
Cdd:PRK05677  261 yhiyAF---TFHCMAMMLIGNHNILIS----NPRDLPAMVKELgkwkfsgfvGLNTLF--VALCNNEAFRKLD-FSALKL 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  731 LLAGGDVLSpKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSR-GMGTgsvpIGKPIANTHVYLLDEQMNPVPPNAVG 809
Cdd:PRK05677  331 TLSGGMALQ-LATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAiQVGT----IGIPVPSTLCKVIDDDGNELPLGEVG 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  810 ELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQ 889
Cdd:PRK05677  406 ELCVKGPQVMKGYWQRPEATDEILDSDGW--------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAA 477

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242  890 HPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK05677  478 LPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1566-1859 5.15e-24

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: 107.54  E-value: 5.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1566 LEGALDFDRLQQAWDETLGAHPALRASFLWEGVP-EPLQVVRRLVRIPTERIDARSMAVdgdawiVERARDE-RRRGFAL 1643
Cdd:cd19532    32 LTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDgEPMQGVLASSPLRLEHVQISDEAE------VEEEFERlKNHVYDL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1644 DAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQHeaahrTAPRPHRDYVAWLR-----GADAQ 1718
Cdd:cd19532   106 ESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLL-----PPPLQYLDFAARQRqdyesGALDE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1719 SVErFWRRELGGFREVTPL-----GIDRPPagQRASSYRRFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYG 1793
Cdd:cd19532   181 DLA-YWKSEFSTLPEPLPLlpfakVKSRPP--LTRYDTHTAERRLDAALAARIKEASRKLRVTPFHFYLAALQVLLARLL 257

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 1794 GRRDVVFGETVSGRSAplEGIERMVGLFINTVPMRAVVDPERPIGEWLTElqGRRAERTAYEHASL 1859
Cdd:cd19532   258 DVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRRDPSQTFADVLKE--TRDKAYAALAHSRV 319
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 1984-2433 1.92e-23

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: 107.66  E-value: 1.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1984 ARERCIHELFESSVERSPGSVALCYDG-----VPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGI 2058
Cdd:cd17634    50 ATLNLAANALDRHLRENGDRTAIIYEGddtsqSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLAC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2059 LKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE------RHLGAVEIAARQLG-----IEHVVSLDGDGKDADGNVV- 2126
Cdd:cd17634   130 ARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragRSVPLKKNVDDALNpnvtsVEHVIVLKRTGSDIDWQEGr 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2127 -IHGRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNR-TYLVGPSDRLLFVTSPSFDLS- 2203
Cdd:cd17634   210 dLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyVFDYGPGDIYWCTADVGWVTGh 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2204 VYDVFGMLAAGG-SIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPY-FDRIE--DGSQLRLAFLSGD-WVPi 2278
Cdd:cd17634   290 SYLLYGPLACGAtTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAgDDAIEgtDRSSLRILGSVGEpINP- 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2279 gmldELRRAFpnVKLVGLGGATEATVWSNYfEVDG--IDPRWTSIPYG-----RPIQNARYYVLDRSGNPCPIGVTGDLY 2351
Cdd:cd17634   369 ----EAYEWY--WKKIGKEKCPVVDTWWQT-ETGGfmITPLPGAIELKagsatRPVFGVQPAVVDNEGHPQPGGTEGNLV 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2352 IGGTC--VSFGYYADPsqtaERFVPDPFSGEPGarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQH 2429
Cdd:cd17634   442 ITDPWpgQTRTLFGDH----ERFEQTYFSTFKG--MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAH 515


                  ....
gi 260177242 2430 PGAQ 2433
Cdd:cd17634   516 PKVA 519
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 475-1043 2.35e-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: 108.64  E-value: 2.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  475 HHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDP 554
Cdd:COG3319     4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  555 AYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTG-----KP 629
Cdd:COG3319    84 LALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGggggaGV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  630 KGVAVTHRNVVRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTPEEIGRVVREHGVTTLWL 709
Cdd:COG3319   164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  710 TAPLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSVPIGKPIA 789
Cdd:COG3319   244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPG 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  790 NTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGVPGARLYRTGDLARYLPNGDMEFLGRRDG 869
Cdd:COG3319   324 LLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRL 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  870 QVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRfsELRKFLLQRLPDHMIPAAVVALDK 949
Cdd:COG3319   404 QRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAA--ALLLLLLLLLLPPPLPPALLLLLL 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  950 LPLVPSGKLDRRALPAPTLSGRSGPFVAPEGHPEEVLARIWERVLRVDAVGREDNFFELGGDSILAIQVVAGAREVDLKL 1029
Cdd:COG3319   482 LLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRL 561

                         570
                  ....*....|....
gi 260177242 1030 TVRQIFTHPTLSSL 1043
Cdd:COG3319   562 LLLLALLLAPTLAA 575
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 471-963 3.71e-23

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 106.31  E-value: 3.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  471 ERCLHHLFEEEARRVPDAVAL---DAGSNV--VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKA 545
Cdd:PRK08008    6 GQHLRQMWDDLADVYGHKTALifeSSGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  546 GGAYVPLDPAYPSERLAFLAHDAGV-------------------------QIVLSAAGAEERLGegpwtVVRLDEDLGR- 599
Cdd:PRK08008   86 GAIMVPINARLLREESAWILQNSQAsllvtsaqfypmyrqiqqedatplrHICLTRVALPADDG-----VSSFTQLKAQq 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  600 PDERDAAPNdnVSAENLAYVMYTSGSTGKPKGVAVTHRNVvrLVRG--SSFAT-FGPDQVFLMMAPAafdastFEI---- 672
Cdd:PRK08008  161 PATLCYAPP--LSTDDTAEILFTSGTTSRPKGVVITHYNL--RFAGyySAWQCaLRDDDVYLTVMPA------FHIdcqc 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  673 ---WGALLHGARLVLFppESPTPEEIGRVVREHGVT----------TLWLTAPlfhaVADRGLDQLRGVRQLLAGGDVLS 739
Cdd:PRK08008  231 taaMAAFSAGATFVLL--EKYSARAFWGQVCKYRATitecipmmirTLMVQPP----SANDRQHCLREVMFYLNLSDQEK 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  740 PKHVARVllglpALRLINGYGPTENTTfttchdvsrGMgTGSVP--------IGKPIANTHVYLLDEQMNPVPPNAVGEL 811
Cdd:PRK08008  305 DAFEERF-----GVRLLTSYGMTETIV---------GI-IGDRPgdkrrwpsIGRPGFCYEAEIRDDHNRPLPAGEIGEI 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  812 F---TGGDGLARGYHERPDQTAERFVPDPFsgvpgarLYrTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALL 888
Cdd:PRK08008  370 CikgVPGKTIFKEYYLDPKATAKVLEADGW-------LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIA 441

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  889 QHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK08008  442 THPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PLN02246 PLN02246
4-coumarate--CoA ligase
 474-965 8.34e-23

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 105.45  E-value: 8.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVALDAGSN--VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVP 551
Cdd:PLN02246   25 LHDYCFERLSEFSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  552 LDPAYPSERLAFLAHDAGVQIVLSAAGAEERL----GEGPWTVVRLDED---------LGRPDErDAAPNDNVSAENLAY 618
Cdd:PLN02246  105 ANPFYTPAEIAKQAKASGAKLIITQSCYVDKLkglaEDDGVTVVTIDDPpegclhfseLTQADE-NELPEVEISPDDVVA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNVVrlvrgSSFAT----------FGPDQVFLMMAPaafdasTFEIWG-------ALLHGAR 681
Cdd:PLN02246  184 LPYSSGTTGLPKGVMLTHKGLV-----TSVAQqvdgenpnlyFHSDDVILCVLP------MFHIYSlnsvllcGLRVGAA 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  682 LVLFPpesptPEEIGRV---VREHGVTTLWLTAPLFHAVA---DRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRL 755
Cdd:PLN02246  253 ILIMP-----KFEIGALlelIQRHKVTIAPFVPPIVLAIAkspVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  756 INGYGPTE------------NTTFTT----CHDVSRgmgtgsvpigkpiaNTHVYLLD-EQMNPVPPNAVGELFTGGDGL 818
Cdd:PLN02246  328 GQGYGMTEagpvlamclafaKEPFPVksgsCGTVVR--------------NAELKIVDpETGASLPRNQPGEICIRGPQI 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  819 ARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLArYLPNGDMEFLGRRDGQ-VKIRGFRIELAEVEAALLQHPALREAV 897
Cdd:PLN02246  394 MKGYLNDPEATANTIDKDGW--------LHTGDIG-YIDDDDELFIVDRLKElIKYKGFQVAPAELEALLISHPSIADAA 464

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242  898 VIAREDRPGDKRLVAYVVGR------EAEVPRFSELRKFLLQRLpdHMipaaVVALDKLPLVPSGKLDRRALPA 965
Cdd:PLN02246  465 VVPMKDEVAGEVPVAFVVRSngseitEDEIKQFVAKQVVFYKRI--HK----VFFVDSIPKAPSGKILRKDLRA 532
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 1993-2431 8.39e-23

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 105.73  E-value: 8.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1993 FESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRW 2072
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQS-ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2073 PLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHGRRALADLADGNLPRAAGPH--NM 2150
Cdd:PRK08279  122 RGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTakDT 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 AYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRlLFVTSP---SFDLSVydVFG-MLAAGGSIHI-----AS 2221
Cdd:PRK08279  202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDV-LYCCLPlyhNTGGTV--AWSsVLAAGATLALrrkfsAS 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2222 E--DDLRSpERLAA-----ELGRgtitFWDSAPAALQqlvpyfDRiedGSQLRLAF---LSGD-WvpigmlDELRRAFPN 2290
Cdd:PRK08279  279 RfwDDVRR-YRATAfqyigELCR----YLLNQPPKPT------DR---DHRLRLMIgngLRPDiW------DEFQQRFGI 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2291 VKLVGLGGATEATVwsNYFEVDGID------PRWTSIPY---------GRPIQNARYYVLdrsgnPCPIGVTGDLyIG-- 2353
Cdd:PRK08279  339 PRILEFYAASEGNV--GFINVFNFDgtvgrvPLWLAHPYaivkydvdtGEPVRDADGRCI-----KVKPGEVGLL-IGri 410

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 2354 GTCVSFGYYADPSQTAERFVPDPFsgEPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK08279  411 TDRGPFDGYTDPEASEKKILRDVF--KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPG 486
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 477-963 1.33e-22

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 104.90  E-value: 1.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKgvgTE----TRVGLCLERSVELVVGILGVLKAGGAYVPL 552
Cdd:PRK12492   29 VFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQH---TDlvpgDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  553 DPAYPSERLAFLAHDAG-------------VQIVLSAAGA----EERLGE-----GPW---TVV----------RLDEDL 597
Cdd:PRK12492  106 NPLYTAREMRHQFKDSGaralvylnmfgklVQEVLPDTGIeyliEAKMGDllpaaKGWlvnTVVdkvkkmvpayHLPQAV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  598 G-----RPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV---RLVRgSSFATFGPDQVFL-------MMAP 662
Cdd:PRK12492  186 PfkqalRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVanmLQVR-ACLSQLGPDGQPLmkegqevMIAP 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  663 A------AFDASTFEIwgaLLHGARLVLFPpespTPEEIGRVVREHG---VTTLWLTAPLFHAVAD----RGLDqLRGVR 729
Cdd:PRK12492  265 LplyhiyAFTANCMCM---MVSGNHNVLIT----NPRDIPGFIKELGkwrFSALLGLNTLFVALMDhpgfKDLD-FSALK 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  730 QLLAGGDVLSpKHVARVLLGLPALRLINGYGPTENTTFTTCH---DVSRgMGTgsvpIGKPIANTHVYLLDEQMNPVPPN 806
Cdd:PRK12492  337 LTNSGGTALV-KATAERWEQLTGCTIVEGYGLTETSPVASTNpygELAR-LGT----VGIPVPGTALKVIDDDGNELPLG 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  807 AVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAA 886
Cdd:PRK12492  411 ERGELCIKGPQVMKGYWQQPEATAEALDAEGW--------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDV 482

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  887 LLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVpRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK12492  483 VMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGL-SVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 1970-2433 1.44e-22

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 104.38  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1970 RQVvadWNDTARAYARERCIheLFESSVerspGSVAlcydgvpPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAP 2049
Cdd:PRK08008   10 RQM---WDDLADVYGHKTAL--IFESSG----GVVR-------RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2050 ELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLG--IEHVVSLDGDGKDADGnvVI 2127
Cdd:PRK08008   74 EFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAtpLRHICLTRVALPADDG--VS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2128 HGRRALADLADG-NLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSqviNLI------EWVNRtylVGPSDRLLFVTsPSF 2200
Cdd:PRK08008  152 SFTQLKAQQPATlCYAPPLSTDDTAEILFTSGTTSRPKGVVITHY---NLRfagyysAWQCA---LRDDDVYLTVM-PAF 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2201 --DLSVYDVFGMLAAGGSIHIAseddlrspERLAAElgrgtiTFWDSA---PAALQQLVPYFDRI---------EDGSQL 2266
Cdd:PRK08008  225 hiDCQCTAAMAAFSAGATFVLL--------EKYSAR------AFWGQVckyRATITECIPMMIRTlmvqppsanDRQHCL 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2267 R--LAFLSgdwvpigMLDELRRAFP---NVKLVGLGGATEATVWsnyfeVDGIDP----RWTSIpyGRPIQNARYYVLDR 2337
Cdd:PRK08008  291 RevMFYLN-------LSDQEKDAFEerfGVRLLTSYGMTETIVG-----IIGDRPgdkrRWPSI--GRPGFCYEAEIRDD 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2338 SGNPCPIGVTGDLYIGGT---CVSFGYYADPSQTAERFVPDPFsgepgarLYrTGDLARFFRDGNIEFLGRADSQVKIRG 2414
Cdd:PRK08008  357 HNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGW-------LH-TGDTGYVDEEGFFYFVDRRCNMIKRGG 428

                         490
                  ....*....|....*....
gi 260177242 2415 YRIECGEVEVALAQHPGAQ 2433
Cdd:PRK08008  429 ENVSCVELENIIATHPKIQ 447
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 619-960 1.51e-22

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: 101.58  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNVVrLVRGSSFATFG--PDQVFLMMAPaafdasTFEIWG-----ALLH--GARLVLfppES 689
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLI-AANLQLIHAMGltEADVYLNMLP------LFHIAGlnlalATFHagGANVVM---EK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 PTPEEIGRVVREHGVTTLWLTAPLFHAVAD------RGLDQLRGVrqllAGGDVlsPKHVARVLLGLPAlRLINGYGPTE 763
Cdd:cd17637    75 FDPAEALELIEEEKVTLMGSFPPILSNLLDaaeksgVDLSSLRHV----LGLDA--PETIQRFEETTGA-TFWSLYGQTE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  764 NTTFTTCHDVSRGMGTGsvpiGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFvpdpfsgvpg 843
Cdd:cd17637   148 TSGLVTLSPYRERPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  844 aR--LYRTGDLARYLPNGDMEFLGRRDGQ--VKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREA 919
Cdd:cd17637   214 -RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 260177242  920 EVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:cd17637   293 ATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 498-963 1.62e-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: 103.03  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPldpaypserlaflahdagVQIVLSAA 577
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 GAEERLGEGPWTVVRLDEdlgrpderdaapndNVSAENLAYVMYTSGSTGKPKGVAVTHRNV-VRLVRGSSFATFGPDQV 656
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDE--------------NTHADDPMLLYFTSGTTSKPKLVEHTHRSYpVGHLSTMYWIGLKPGDV 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  657 FLMMAPAAFD----ASTFEIWGAllhGARLVLFPPESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLR-GVRQL 731
Cdd:cd05974   129 HWNISSPGWAkhawSCFFAPWNA---GATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDvKLREV 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  732 LAGGDVLSPKHVARVLlGLPALRLINGYGPTEnTTFTTCHDVSRGMGTGSvpIGKPIANTHVYLLDEQMNPVppnAVGEL 811
Cdd:cd05974   206 VGAGEPLNPEVIEQVR-RAWGLTIRDGYGQTE-TTALVGNSPGQPVKAGS--MGRPLPGYRVALLDPDGAPA---TEGEV 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  812 -FTGGD----GLARGYHERPDQTAerfvpdpfsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAA 886
Cdd:cd05974   279 aLDLGDtrpvGLMKGYAGDPDKTA---------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESV 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  887 LLQHPALREAVVIAredRPGDKRLV---AYVVGREAEVPRfSELRKFLLQRLPDHMIPAAVV---ALDKLPLVPSGKLDR 960
Cdd:cd05974   350 LIEHPAVAEAAVVP---SPDPVRLSvpkAFIVLRAGYEPS-PETALEIFRFSRERLAPYKRIrrlEFAELPKTISGKIRR 425


                  ...
gi 260177242  961 RAL 963
Cdd:cd05974   426 VEL 428
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
482-1028 1.77e-22

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 105.50  E-value: 1.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDA----GSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYP 557
Cdd:PRK06060   11 AEQASEAGWYDRpafyAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAHDAGVQIVLSAAGAEERLgeGPWTVVRLDEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHR 637
Cdd:PRK06060   91 RDDHALAARNTEPALVVTSDALRDRF--QPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  638 NVVRLVRG--SSFATFGPDQVFLMMAPAAFDAST-FEIWGALLHGARLVLFPpeSPTPEEIGRVVREHGVTTLWLTAPLF 714
Cdd:PRK06060  169 DPLTFVDAmcRKALRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVINS--APVTPEAAAILSARFGPSVLYGVPNF 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  715 HA--VADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTE-NTTFTTCHDVSRGMGTgsvpIGKPIANT 791
Cdd:PRK06060  247 FArvIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEvGQTFVSNRVDEWRLGT----LGRVLPPY 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  792 HVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERfvpdpfsgvpGARLyRTGDLARYLPNGDMEFLGRRDGQV 871
Cdd:PRK06060  323 EIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVAN----------EGWL-DTRDRVCIDSDGWVTYRCRADDTE 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  872 KIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELR---KFLLQRLPDHMIPAAVVALD 948
Cdd:PRK06060  392 VIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRdlhRGLLNRLSAFKVPHRFAVVD 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  949 KLPLVPSGKLDRRALPAPTlsgrsgpfvapeghPEEvlaRIWERVL---RVDAVGREDnffelGGDSILAIQVVAGAREV 1025
Cdd:PRK06060  472 RLPRTPNGKLVRGALRKQS--------------PTK---PIWELSLtepGSGVRAQRD-----DLSASNMTIAGGNDGGA 529


                  ...
gi 260177242 1026 DLK 1028
Cdd:PRK06060  530 TLR 532
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 2009-2435 1.84e-22

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: 104.24  E-value: 1.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2009 DGVPPLTYSDLNGRANRL-GWLLRGLGAGpeERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWP---LERVAAVLGTT 2084
Cdd:cd05931    20 GREETLTYAELDRRARAIaARLQAVGKPG--DRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPgrhAERLAAILADA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2085 RPVCIVTDERHLGAV-EIAARQLGIEHVVSLDGDGKDADGnvvihgrraladlADGNLPRAAGPHNMAYVIFTSGSTGTP 2163
Cdd:cd05931    98 GPRVVLTTAAALAAVrAFAASRPAAGTPRLLVVDLLPDTS-------------AADWPPPSPDPDDIAYLQYTSGSTGTP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2164 KGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLS-VYDVFGMLAAGGSIH-IASEDDLRSPERLAAELGR--GT 2239
Cdd:cd05931   165 KGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVlMSPAAFLRRPLRWLRLISRyrAT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2240 ITFwdsAPA-ALQQLVpyfDRIEDG-------SQLRLAFLSGDWVPIGMLDELRRAF------PNVKLVGLGGAtEATV- 2304
Cdd:cd05931   245 ISA---APNfAYDLCV---RRVRDEdlegldlSSWRVALNGAEPVRPATLRRFAEAFapfgfrPEAFRPSYGLA-EATLf 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2305 --------------------WSNYFEVDGIDPRWTSIP-YGRPIQNARYYVLDR-SGNPCPIGVTGDLYIGGTCVSFGYY 2362
Cdd:cd05931   318 vsggppgtgpvvlrvdrdalAGRAVAVAADDPAARELVsCGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGPSVASGYW 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2363 ADPSQTAERFvpDPFSGEPGARLYRTGDLArFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQRG 2435
Cdd:cd05931   398 GRPEATAETF--GALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRP 467
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 1979-2431 2.21e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 104.05  E-value: 2.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1979 TARAYARERCIHELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGI 2058
Cdd:PRK06164    2 PHDAAPRADTLASLLDAHARARPDAVALIDEDRP-LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2059 LKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERH--------LGAVEIAARQlGIEHVVSLDGDGKDADGNVVIhGR 2130
Cdd:PRK06164   81 ARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFkgidfaaiLAAVPPDALP-PLRAIAVVDDAADATPAPAPG-AR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2131 RALADLAD-----GNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVtspsfdLSVY 2205
Cdd:PRK06164  159 VQLFALPDpappaAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAA------LPFC 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2206 DVFGM------LAAGGSIHiaSEDDLRSPeRLAAELGRGTITFWDSAPAALQQLVPYFDRIEDGSQLRL----AFLSGdw 2275
Cdd:PRK06164  233 GVFGFstllgaLAGGAPLV--CEPVFDAA-RTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLfgfaSFAPA-- 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2276 vpIGMLDELRRAfPNVKLVGLGGATEA-TVWSNYFEVDGIDPRWtsIPYGRPIQ-NARYYVLD-RSGNPCPIGVTGDLYI 2352
Cdd:PRK06164  308 --LGELAALARA-RGVPLTGLYGSSEVqALVALQPATDPVSVRI--EGGGRPASpEARVRARDpQDGALLPDGESGEIEI 382

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2353 GGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK06164  383 RAPSLMRGYLDNPDATARALTDDGY--------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPG 453
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 498-926 3.82e-22

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: 103.06  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGgayVPLDPAYpserlAFLAHDAgVQIVLSAA 577
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVY-----ATLGEDA-LIHSLNET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 GAEerlgegpwTVVRldedlgrpderdaapndNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFATF---GPD 654
Cdd:cd17639    77 ECS--------AIFT-----------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPellGPD 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  655 QVFLMMAPAA----FDA-STFEIWGALL----------------HGaRLVLFPP-------------------ESPTPEE 694
Cdd:cd17639   132 DRYLAYLPLAhifeLAAeNVCLYRGGTIgygsprtltdkskrgcKG-DLTEFKPtlmvgvpaiwdtirkgvlaKLNPMGG 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  695 IGRVVREHGVTT-----LWL-TAPLFHAVADRGLDQLRG--VRQLLAGGDVLSP--KHVARVLLGlpalRLINGYGPTE- 763
Cdd:cd17639   211 LKRTLFWTAYQSklkalKEGpGTPLLDELVFKKVRAALGgrLRYMLSGGAPLSAdtQEFLNIVLC----PVIQGYGLTEt 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  764 --NTTFTTCHDvsrgMGTGSVpiGKPIANTHVYLLD-EQMNPVP--PNAVGELFTGGDGLARGYHERPDQTAERFVPDpf 838
Cdd:cd17639   287 caGGTVQDPGD----LETGRV--GPPLPCCEIKLVDwEEGGYSTdkPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGD-- 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  839 sgvpgaRLYRTGDLARYLPNGDMEFLGRRDGQVKIR-GFRIELAEVEAALLQHPALREAVVIAREDRPgdkRLVAYVVGR 917
Cdd:cd17639   359 ------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKS---YPVAIVVPN 429


                  ....*....
gi 260177242  918 EAEVPRFSE 926
Cdd:cd17639   430 EKHLTKLAE 438
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 494-966 4.07e-22

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 102.85  E-value: 4.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  494 GSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIV 573
Cdd:PRK12406    8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  574 LSAA----GAEERLGEGPWTVV-----------RLDEDLGRPDE---------RDAAPNDNVSAENLAYVMYTSGSTGKP 629
Cdd:PRK12406   88 IAHAdllhGLASALPAGVTVLSvptppeiaaayRISPALLTPPAgaidwegwlAQQEPYDGPPVPQPQSMIYTSGTTGHP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  630 KGV---------AVTHRNVVRLVRGssfatFGPDQVFLMMAPAAFDA-STFEIWGALLhGARLVLFPpeSPTPEEIGRVV 699
Cdd:PRK12406  168 KGVrraaptpeqAAAAEQMRALIYG-----LKPGIRALLTGPLYHSApNAYGLRAGRL-GGVLVLQP--RFDPEELLQLI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  700 REHGVTTLWLTAPLFHavadRGLDQLRGVRqllAGGDVLS-----------PKHVARVLLGLPALRLINGYGPTEN--TT 766
Cdd:PRK12406  240 ERHRITHMHMVPTMFI----RLLKLPEEVR---AKYDVSSlrhvihaaapcPADVKRAMIEWWGPVIYEYYGSTESgaVT 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  767 FTTCHDVSRGMGTgsvpIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLAR-GYHERPDQTAErfvpdpfsgVPGAR 845
Cdd:PRK12406  313 FATSEDALSHPGT----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE---------IDRGG 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  846 LYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFS 925
Cdd:PRK12406  380 FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEA 459

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 260177242  926 ELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAP 966
Cdd:PRK12406  460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 619-959 6.56e-22

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: 99.30  E-value: 6.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNV----VRLVRGSSFatfGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPtpEE 694
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALlaqaLVLAVLQAI---DEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDA--EE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  695 IGRVVREHGVTTLWLTAPLFH----AVADRGLD--QLRGVRQLLAGGDVLSPKHVarvllglPALRLINGYGPTENTTFT 768
Cdd:cd17636    80 VLELIEAERCTHAFLLPPTIDqiveLNADGLYDlsSLRSSPAAPEWNDMATVDTS-------PWGRKPGGYGQTEVMGLA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TCHdvsrGMGTGSVPI-GKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVpdpfsgvpgARLY 847
Cdd:cd17636   153 TFA----ALGGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR---------GGWH 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  848 RTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSEL 927
Cdd:cd17636   220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAEL 299

                         330       340       350
                  ....*....|....*....|....*....|..
gi 260177242  928 RKFLLQRLPDHMIPAAVVALDKLPLVPSGKLD 959
Cdd:cd17636   300 IEHCRARIASYKKPKSVEFADALPRTAGGADD 331
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 498-963 7.41e-22

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 102.36  E-value: 7.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAA 577
Cdd:PLN02330   56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTND 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 GAEERLGEGPWTVVRLDE----------DLGRPDER--DAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG 645
Cdd:PLN02330  136 TNYGKVKGLGLPVIVLGEekiegavnwkELLEAADRagDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCS 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  646 SSFATfGPDQV----FLMMAPaafdasTFEIWG-------ALLHGARLVLfppesptpeeIGR--------VVREHGVTT 706
Cdd:PLN02330  216 SLFSV-GPEMIgqvvTLGLIP------FFHIYGitgiccaTLRNKGKVVV----------MSRfelrtflnALITQEVSF 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  707 LWLTAPLFHA------VADRGLDQLRgVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFTTCH-DVSRGMGT 779
Cdd:PLN02330  279 APIVPPIILNlvknpiVEEFDLSKLK-LQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHgDPEKGHGI 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  780 GSV-PIGKPIANTHVYLLD-EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLP 857
Cdd:PLN02330  358 AKKnSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW--------LHTGDIGYIDD 429

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  858 NGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPD 937
Cdd:PLN02330  430 DGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAH 509

                         490       500
                  ....*....|....*....|....*.
gi 260177242  938 HMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PLN02330  510 YKKVRVVQFVDSIPKSLSGKIMRRLL 535
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 1989-2441 1.51e-21

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: 102.18  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALCYDG----VPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGA 2064
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGedgtSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2065 YVPLDPRWPLERVAAVL------------GTTRPVCIV--TDErhlgAVEIAARQLGIEHVVSLDGDGKDADGNVVihGR 2130
Cdd:cd05968   143 VVPIFSGFGKEAAATRLqdaeakalitadGFTRRGREVnlKEE----ADKACAQCPTVEKVVVVRHLGNDFTPAKG--RD 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2131 RALADLADGNLPRAAGPHNM--AYVIFTSGSTGTPKGVVERHSQV-INLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDV 2207
Cdd:cd05968   217 LSYDEEKETAGDGAERTESEdpLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLI 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2208 FGMLAAGGSIHI-ASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFD---RIEDGSQLRLAFLSGD-WVPIGMLD 2282
Cdd:cd05968   297 FGGLILGATMVLyDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDapvNAHDLSSLRVLGSTGEpWNPEPWNW 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2283 ELR-RAFPNVKLVGLGGATEAT--VWSNYFeVDGIDPrwtsIPYGRPIQNARYYVLDRSGNPCPiGVTGDL-----YIGG 2354
Cdd:cd05968   377 LFEtVGKGRNPIINYSGGTEISggILGNVL-IKPIKP----SSFNGPVPGMKADVLDESGKPAR-PEVGELvllapWPGM 450

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2355 TcvsFGYYADPsqtaERFVPDPFSGEPGARLYrtGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd05968   451 T---RGFWRDE----DRYLETYWSRFDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521


                  ....*..
gi 260177242 2435 GRGSGGP 2441
Cdd:cd05968   522 SAAIGVP 528
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 5-439 1.78e-21

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: 99.83  E-value: 1.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    5 LPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEG----LVQSLADVSAVD 80
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGqpvqVVHRQAQVPVTE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   81 FGVTDGSSWDEPtAAAWLQAEAARPFDLRaGALRVRA-LRRAPD--QWQILFAFHHIVCDGWSAMIVAAEFAELCAADVE 157
Cdd:cd19536    82 LDLTPLEEQLDP-LRAYKEETKIRRFDLG-RAPLVRAaLVRKDEreRFLLVISDHHSILDGWSLYLLVKEILAVYNQLLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  158 GRAATLTPiSRGFRDYLVWHRdllASDDASALVREWAAMVGDLDVSTPLdlptdLPRRAQQRYHVRQHFRDLGADLMDRV 237
Cdd:cd19536   160 YKPLSLPP-AQPYRDFVAHER---ASIQQAASERYWREYLAGATLATLP-----ALSEAVGGGPEQDSELLVSVPLPVRS 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  238 RESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTrtwqLGVVG--HMAG--IVPVPARIDAAATP-RAIIRE 312
Cdd:cd19536   231 RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRS----EETTGaeRLLGlfLNTLPLRVTLSEETvEDLLKR 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  313 LRNALRVTAKLQSVPLSRLAEQCRVPkspgrmPLVQAVFQ-----EIRSFNEAIRPEGFGHMLRWSRGPLGFEVEVpSEL 387
Cdd:cd19536   307 AQEQELESLSHEQVPLADIQRCSEGE------PLFDSIVNfrhfdLDFGLPEWGSDEGMRRGLLFSEFKSNYDVNL-SVL 379

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242  388 GSQLDLEVRCYdffsssvrtcwrYDPDLFLPETVERWADYYAALLRELVGDL 439
Cdd:cd19536   380 PKQDRLELKLA------------YNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 1992-2431 1.94e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 101.12  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1992 LFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPR 2071
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRR-LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2072 WPLERVAAVLGTTRPVCIVTDERHLGAV-EIAARQLGIEHVVSLDGDGKDADGNVVIHGRRALADLADGNLPRAAGPHNM 2150
Cdd:PRK07798   87 YVEDELRYLLDDSDAVALVYEREFAPRVaEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERDFGERSPDDL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 aYVIFTSGSTGTPKGVVERHSQVInliewvnRTYLVGPSdrllFVTSP----SFDLSV---------------------- 2204
Cdd:PRK07798  167 -YLLYTGGTTGMPKGVMWRQEDIF-------RVLLGGRD----FATGEpiedEEELAKraaagpgmrrfpapplmhgagq 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2205 YDVFGMLAAGGSIHIASEDDLRSPE--RLAAELGRGTITFWDSAPA-----ALQQLVPYfdrieDGSQLRLAFLSGDWVP 2277
Cdd:PRK07798  235 WAAFAALFSGQTVVLLPDVRFDADEvwRTIEREKVNVITIVGDAMArplldALEARGPY-----DLSSLFAIASGGALFS 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2278 IGMLDELRRAFPNVKLVGLGGATEATVwsNYFEVDGIDPRWTSIPYGRPiqNARYYVLDRSGNPCP--IGVTGDLYIGGT 2355
Cdd:PRK07798  310 PSVKEALLELLPNVVLTDSIGSSETGF--GGSGTVAKGAVHTGGPRFTI--GPRTVVLDEDGNPVEpgSGEIGWIARRGH 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2356 cVSFGYYADPSQTAERF-VPDpfsgepGARLYRTGDLARFFRDGNIEFLGRaDSQVkirgyrIECG-------EVEVALA 2427
Cdd:PRK07798  386 -IPLGYYKDPEKTAETFpTID------GVRYAIPGDRARVEADGTITLLGR-GSVC------INTGgekvfpeEVEEALK 451


                  ....
gi 260177242 2428 QHPG 2431
Cdd:PRK07798  452 AHPD 455
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 482-963 2.14e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 100.92  E-value: 2.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPD--AVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSE 559
Cdd:PRK13391    7 AQTTPDkpAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  560 RLAFLAHDAGVQIVLSAAG----AEERLGEGPwtVVRLDEDLGRPDERD----------AAPNDNVSAENLAYVM-YTSG 624
Cdd:PRK13391   87 EAAYIVDDSGARALITSAAkldvARALLKQCP--GVRHRLVLDGDGELEgfvgyaeavaGLPATPIADESLGTDMlYSSG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  625 STGKPKGV--AVTHRNVV----------RLVRgssfatFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFppESPTP 692
Cdd:PRK13391  165 TTGRPKGIkrPLPEQPPDtplpltaflqRLWG------FRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVM--EHFDA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  693 EEIGRVVREHGVTTLWLTAPLFhavaDRGLDQLRGVRQLLaggDVLSPKHVARVLLGLPAL---RLINGYGP-------- 761
Cdd:PRK13391  237 EQYLALIEEYGVTHTQLVPTMF----SRMLKLPEEVRDKY---DLSSLEVAIHAAAPCPPQvkeQMIDWWGPiiheyyaa 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  762 TENTTFTTCHDVSRGMGTGSVpiGKPIANThVYLLDEQMNPVPPNAVGELFTGGdGLARGYHERPDQTAERFVPDP-FSG 840
Cdd:PRK13391  310 TEGLGFTACDSEEWLAHPGTV--GRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDGtWST 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  841 VpgarlyrtGDLArYLPNGDMEFLGRRDGQVKIR-GFRIELAEVEAALLQHPALREAVVIAREDRP-GD--KRLVAYVVG 916
Cdd:PRK13391  386 V--------GDIG-YVDEDGYLYLTDRAAFMIISgGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEevKAVVQPVDG 456

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 260177242  917 REAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK13391  457 VDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 495-963 3.03e-21

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 100.99  E-value: 3.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  495 SNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILG-------------------------------VL 543
Cdd:PRK00174   96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAcarigavhsvvfggfsaealadriidagaklVI 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  544 KA-----GGAYVPL----DPAypserlafLAHDAGVQ--IVLSAAGaeerlGEGPWTVVRlD---EDL--GRPDERDAAP 607
Cdd:PRK00174  176 TAdegvrGGKPIPLkanvDEA--------LANCPSVEkvIVVRRTG-----GDVDWVEGR-DlwwHELvaGASDECEPEP 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  608 ndnVSAENLAYVMYTSGSTGKPKGV-----------AVTHRNV--------------VRLVRGSSFATFGPdqvflmmap 662
Cdd:PRK00174  242 ---MDAEDPLFILYTSGSTGKPKGVlhttggylvyaAMTMKYVfdykdgdvywctadVGWVTGHSYIVYGP--------- 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  663 aafdastfeiwgaLLHGARLVLFP--PESPTPEEIGRVVREHGVTTLWlTAPlfhavadrgldqlRGVRQLLAGGDvlsp 740
Cdd:PRK00174  310 -------------LANGATTLMFEgvPNYPDPGRFWEVIDKHKVTIFY-TAP-------------TAIRALMKEGD---- 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  741 KHVARVllGLPALRLINGYG--------------------PTENT---TFTTCHdvsrgMGT---GSVPIgKPIANTH-- 792
Cdd:PRK00174  359 EHPKKY--DLSSLRLLGSVGepinpeawewyykvvggercPIVDTwwqTETGGI-----MITplpGATPL-KPGSATRpl 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  793 ----VYLLDEQMNPVPPNAVGELF--TGGDGLARGYHERPdqtaERFVPDPFSGVPGarLYRTGDLARYLPNGDMEFLGR 866
Cdd:PRK00174  431 pgiqPAVVDEEGNPLEGGEGGNLVikDPWPGMMRTIYGDH----ERFVKTYFSTFKG--MYFTGDGARRDEDGYYWITGR 504

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  867 RDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRfSELRKFLLQRL---------PD 937
Cdd:PRK00174  505 VDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPS-DELRKELRNWVrkeigpiakPD 583

                         570       580
                  ....*....|....*....|....*.
gi 260177242  938 HMIPAavvalDKLPLVPSGKLDRRAL 963
Cdd:PRK00174  584 VIQFA-----PGLPKTRSGKIMRRIL 604
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 2000-2431 3.21e-21

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 99.95  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2000 SPGSVALCYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAA 2079
Cdd:PRK07514   15 DRDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2080 VLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVSLDGDGkdaDGNVVIHGRRALADLADgnLPRAAGphNMAYVIFTSGS 2159
Cdd:PRK07514   95 FIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADG---TGSLLEAAAAAPDDFET--VPRGAD--DLAAILYTSGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2160 TGTPKGVVERHSqviNLIEwvNRTYLV-----GPSDRLLFVtspsfdLSVYDVFGM-------LAAGGSIHIASEDDlrs 2227
Cdd:PRK07514  168 TGRSKGAMLSHG---NLLS--NALTLVdywrfTPDDVLIHA------LPIFHTHGLfvatnvaLLAGASMIFLPKFD--- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 PERLAAELGRGTI-----TFWDSapaALQQlvPYFDRiEDGSQLRLaFLSGDwVPigMLDELRRAFPnvKLVGLG----- 2297
Cdd:PRK07514  234 PDAVLALMPRATVmmgvpTFYTR---LLQE--PRLTR-EAAAHMRL-FISGS-AP--LLAETHREFQ--ERTGHAilery 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2298 GATEaTVWSnyfevdgidprwTSIPY---------GRPIQNARYYVLDR-SGNPCPIGVTGDLYIGGTCVSFGYYADPSQ 2367
Cdd:PRK07514  302 GMTE-TNMN------------TSNPYdgerragtvGFPLPGVSLRVTDPeTGAELPPGEIGMIEVKGPNVFKGYWRMPEK 368

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242 2368 TAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK07514  369 TAEEFRADGF--------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPG 424
PRK07529 PRK07529
AMP-binding domain protein; Validated
 474-963 4.71e-21

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 100.41  E-value: 4.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVAL--------DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKA 545
Cdd:PRK07529   27 TYELLSRAAARHPDAPALsflldadpLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  546 GGAyVPLDPAYPSERLAFLAHDAGVQIVLSAAG---------AEERLGEGP----WTVVRLDEDLGRP------------ 600
Cdd:PRK07529  107 GIA-NPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwqkVAEVLAALPelrtVVEVDLARYLPGPkrlavplirrka 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  601 --------DERDAAPND------NVSAENLAYVMYTSGSTGKPKGVAVTHRN-VVRLVRGSSFATFGPDQVFLMMAPaaf 665
Cdd:PRK07529  186 harildfdAELARQPGDrlfsgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNeVANAWLGALLLGLGPGDTVFCGLP--- 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  666 dasTFEIWG-------ALLHGARLVLfppesPTP---------EEIGRVVREHGVTTLWLTAPLFHAVADRGLD--QLRG 727
Cdd:PRK07529  263 ---LFHVNAllvtglaPLARGAHVVL-----ATPqgyrgpgviANFWKIVERYRINFLSGVPTVYAALLQVPVDghDISS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  728 VRQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSVPIGKPIANTHVYLLDEQ---MNPVP 804
Cdd:PRK07529  335 LRYALCGAAPL-PVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVILDDAgryLRDCA 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  805 PNAVGELFTGGDGLARGYHErPDQTAERFVPDpfsgvpgaRLYRTGDLARYLPNGDMEFLGRRDGQVkIR-GFRIELAEV 883
Cdd:PRK07529  414 VDEVGVLCIAGPNVFSGYLE-AAHNKGLWLED--------GWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAI 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  884 EAALLQHPALREAVVIAREDRPGDKRLVAYV-VGREAEVPRfSELRKFLLQRLPDHM-IPAAVVALDKLPLVPSGKLDRR 961
Cdd:PRK07529  484 EEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATE-AELLAFARDHIAERAaVPKHVRILDALPKTAVGKIFKP 562


                  ..
gi 260177242  962 AL 963
Cdd:PRK07529  563 AL 564
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 482-965 6.98e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 99.30  E-value: 6.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDEDLGRPDERDAAPNDNVSAEnlaYVMYTSGSTGKPKGV--------- 632
Cdd:PRK13383  125 AAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGR---IVLLTSGTTGKPKGVprapqlrsa 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  633 ---AVTHRNVVRLVRGSSFATFGPdqvflMMAPAAFDASTFEIwgaLLHGARLVLFPPESPTPEEIGRVVREHGVTTLWL 709
Cdd:PRK13383  202 vgvWVTILDRTRLRTGSRISVAMP-----MFHGLGLGMLMLTI---ALGGTVLTHRHFDAEAALAQASLHRADAFTAVPV 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  710 TAPLFHAVAD--RGLDQLRGVRQLLAGGDVLSPKhVARVLLGLPALRLINGYGPTEnttfttchdvsRGMGTGSVP---- 783
Cdd:PRK13383  274 VLARILELPPrvRARNPLPQLRVVMSSGDRLDPT-LGQRFMDTYGDILYNGYGSTE-----------VGIGALATPadlr 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  784 -----IGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHErpdqTAERFVPDPFSGvpgarlyrTGDLARYLPN 858
Cdd:PRK13383  342 dapetVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDGMTS--------TGDMGYLDNA 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  859 GDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDH 938
Cdd:PRK13383  410 GRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRF 489

                         490       500
                  ....*....|....*....|....*..
gi 260177242  939 MIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK13383  490 EQPRDINIVSSIPRNPTGKVLRKELPG 516
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 615-958 1.08e-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: 96.03  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG-SSFATFGPDQVFLMMAPaafdasTFEIWG-------ALLHGARLVlfP 686
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAwADCADLTEDDRYLIINP------FFHTFGykagivaCLLTGATVV--P 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  687 PESPTPEEIGRVVREHGVTTLWLTAPLFH---AVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTE 763
Cdd:cd17638    73 VAVFDVDAILEAIERERITVLPGPPTLFQsllDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  764 NTTFTTCHDvSRGMGTGSVPIGKPIANTHVYLLDEqmnpvppnavGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpg 843
Cdd:cd17638   153 AGVATMCRP-GDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW----- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  844 arlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPR 923
Cdd:cd17638   217 ---LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLT 293

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 260177242  924 FSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKL 958
Cdd:cd17638   294 EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 2015-2430 1.14e-20

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: 98.72  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVP----LDPRWPLERVAAvlGTTRPVCIV 2090
Cdd:cd05970    49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqLTAKDIVYRIES--ADIKMIVAI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2091 TDERHLGAVEIAARQLGIEHVVSLDGDgKDADGNVVIHgrrALADLADGNLPRAAGP-----HNMAYVIFTSGSTGTPKG 2165
Cdd:cd05970   127 AEDNIPEEIEKAAPECPSKPKLVWVGD-PVPEGWIDFR---KLIKNASPDFERPTANsypcgEDILLVYFSSGTTGMPKM 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2166 VVERHS----QVINLIEWVNrtylVGPSDRLLFVTSPSFDLSVY-DVFGMLAAGGSIHIASEDDLrSPERLAAELGRGTI 2240
Cdd:cd05970   203 VEHDFTyplgHIVTAKYWQN----VREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYDKF-DPKALLEKLSKYGV 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 TFWDSAPAALQQLVPYFDRIEDGSQLRLAFLSGDwvPIGM-LDELRRAFPNVKLVGLGGATEATVWSNYFEvdGIDPRWT 2319
Cdd:cd05970   278 TTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGE--ALNPeVFNTFKEKTGIKLMEGFGQTETTLTIATFP--WMEPKPG 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2320 SIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYI---GGTCVSF--GYYADPSQTAERFvpdpFSGepgarLYRTGDLARF 2394
Cdd:cd05970   354 SM--GKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGLfgGYYKDAEKTAEVW----HDG-----YYHTGDAAWM 422

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 260177242 2395 FRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05970   423 DEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHP 458
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1989-2431 1.42e-20

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 98.42  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALCY-DGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVP 2067
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVtADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2068 LDPRWPL--ERVAAVLGTTRPVCIVTDERHLGAVEiAARQLGIehVVSLDGDGKDADGNVVIHGRRALADLADGNLPRAA 2145
Cdd:PRK05852   98 LDPALPIaeQRVRSQAAGARVVLIDADGPHDRAEP-TTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2146 GPHNmAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVtspsfdLSVYDVFGMLAAGGSIhIASEDDL 2225
Cdd:PRK05852  175 RPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAV------MPLYHGHGLIAALLAT-LASGGAV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2226 RSPERlaaelGRGTI-TFWD---SAPAALQQLVPYFDRI-------EDGSQLR--LAFLSGDWVPI--GMLDELRRAFpN 2290
Cdd:PRK05852  247 LLPAR-----GRFSAhTFWDdikAVGATWYTAVPTIHQIlleraatEPSGRKPaaLRFIRSCSAPLtaETAQALQTEF-A 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2291 VKLVGLGGATEATVWSNYFEVDGI----DPRWTSIPYGRPiQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPS 2366
Cdd:PRK05852  321 APVVCAFGMTEATHQVTTTQIEGIgqteNPVVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242 2367 QTAERFVPDPFsgepgarlyRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK05852  400 ITAANFTDGWL---------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPN 455
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 2015-2433 2.40e-20

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: 96.78  E-value: 2.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRG-LGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:cd05958    12 TYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALCAH 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RhLGAVEiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagphNMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd05958    92 A-LTASD------------------------------------------------DICILAFTSGTTGAPKATMHFHRDP 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLIEWVNRTYLvGPSDRLLFVTSP----SFDLSVYDVFgMLAAGGSIHIASEddlRSPERLAAELGRGTITFWDSAPAA 2249
Cdd:cd05958   123 LASADRYAVNVL-RLREDDRFVGSPplafTFGLGGVLLF-PFGVGASGVLLEE---ATPDLLLSAIARYKPTVLFTAPTA 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2250 LQQLVPYFDRIE-DGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEAtvWSNYFEVDGIDPRWTSIpyGRPIQ 2328
Cdd:cd05958   198 YRAMLAHPDAAGpDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEM--FHIFISARPGDARPGAT--GKPVP 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2329 NARYYVLDRSGNPCPIGVTGDLYIGGTcVSFGYYADPSQTaerfvpDPFSGEPGArlyrTGDLarFFR--DGNIEFLGRA 2406
Cdd:cd05958   273 GYEAKVVDDEGNPVPDGTIGRLAVRGP-TGCRYLADKRQR------TYVQGGWNI----TGDT--YSRdpDGYFRHQGRS 339

                         410       420
                  ....*....|....*....|....*..
gi 260177242 2407 DSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:cd05958   340 DDMIVSGGYNIAPPEVEDVLLQHPAVA 366
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 2014-2433 2.76e-20

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: 96.59  E-value: 2.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRL-GWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPlervaavlgttrpvcivtd 2092
Cdd:cd05941    12 ITYADLVARAARLaNRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYP------------------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 erhlgaveiaARQLgiEHVVSldgdgkDADGNVVIhgrraladladgnlpraagphNMAYVIFTSGSTGTPKGVVERH-- 2170
Cdd:cd05941    73 ----------LAEL--EYVIT------DSEPSLVL---------------------DPALILYTSGTTGRPKGVVLTHan 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2171 --SQVINLIEWVNRTylvgPSDRLLFVtspsfdLSVYDVFGM-------LAAGGSIHIASEDDlrsPERLAAELGRGTIT 2241
Cdd:cd05941   114 laANVRALVDAWRWT----EDDVLLHV------LPLHHVHGLvnallcpLFAGASVEFLPKFD---PKEVAISRLMPSIT 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2242 FWDSAPAALQQLVPYFDRIEDGSQ---------LRLaFLSGDW-VPIGMLDELRRAFPNVkLVGLGGATEATV-WSNyfE 2310
Cdd:cd05941   181 VFMGVPTIYTRLLQYYEAHFTDPQfaraaaaerLRL-MVSGSAaLPVPTLEEWEAITGHT-LLERYGMTEIGMaLSN--P 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2311 VDGiDPRWTSIpyGRPIQNARYYVLDRSGN-PCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTG 2389
Cdd:cd05941   257 LDG-ERRPGTV--GMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTG 325

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 260177242 2390 DLARFFRDGNIEFLGR-ADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:cd05941   326 DLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVS 370
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
614-963 2.91e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 95.11  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  614 ENLAYVMYTSGSTGKPKGVAVTHRNVvrlvRGSSFATF----GPDQVFLMMaPAAFDASTFEIWGALLHGAR-LVLFPPE 688
Cdd:PRK07824   35 DDVALVVATSGTTGTPKGAMLTAAAL----TASADATHdrlgGPGQWLLAL-PAHHIAGLQVLVRSVIAGSEpVELDVSA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  689 SPTPEEIGRVVREHG-------VTTLWLTAPLFHAVADRGLDQLRGVrqLLAGGDVLSPKHVARVLLGLPALRLingYGP 761
Cdd:PRK07824  110 GFDPTALPRAVAELGggrrytsLVPMQLAKALDDPAATAALAELDAV--LVGGGPAPAPVLDAAAAAGINVVRT---YGM 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  762 TEnttftTChdvsrgmgTGSVPIGKPIANTHVYLLDeqmnpvppnavGELFTGGDGLARGYHERPDqtaerfvPDPFSGv 841
Cdd:PRK07824  185 SE-----TS--------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFAE- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  842 PGarLYRTGDLARyLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEV 921
Cdd:PRK07824  233 PG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 260177242  922 PRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK07824  310 PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 5-438 5.53e-20

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: 95.13  E-value: 5.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    5 LPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGVT 84
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   85 DGSSWDEP--TAAAWLQAEAARPFDLRAGALRVRALRRAPDQWQILFA-FHHIVCDGWSAMIVAAEFAELCAADVEGRAA 161
Cdd:cd19533    82 DLSGDPDPegAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  162 TLTPisrgFRDYLvwhrDLLASDDA---SALVREWAAMVGDLDVSTPldLPTDLPRRA-QQRYHVRQHFRDLGADLMDRV 237
Cdd:cd19533   162 PPAP----FGSFL----DLVEEEQAyrqSERFERDRAFWTEQFEDLP--EPVSLARRApGRSLAFLRRTAELPPELTRTL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  238 RESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDA-------AATPRAII 310
Cdd:cd19533   232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPqqtfaelVAQVSREL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  311 R-----------ELRNALRVTAKLQsvPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSfneairpegfghmlrwsrgplgf 379
Cdd:cd19533   312 RsllrhqryryeDLRRDLGLTGELH--PLFGPTVNYMPFDYGLDFGGVVGLTHNLSS----------------------- 366

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  380 evevpselGSQLDLEVRCYDFF-SSSVRTCWRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19533   367 --------GPTNDLSIFVYDRDdESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
PRK09274 PRK09274
peptide synthase; Provisional
 482-898 5.70e-20

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 96.51  E-value: 5.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVAL------DAGSNV----VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVP 551
Cdd:PRK09274   16 AQERPDQLAVavpggrGADGKLaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  552 LDPAYPSERL----------AF----LAHDAGVQIVLSAAGAEERLGEGP---WTVVRLDEDLGRPDERDAAPNDnVSAE 614
Cdd:PRK09274   96 VDPGMGIKNLkqclaeaqpdAFigipKAHLARRLFGWGKPSVRRLVTVGGrllWGGTTLATLLRDGAAAPFPMAD-LAPD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRN---VVRLVRgssfATFGpdqvflmMAPAAFDASTFEIWG--ALLHGARLVLfPPES 689
Cdd:PRK09274  175 DMAAILFTSGSTGTPKGVVYTHGMfeaQIEALR----EDYG-------IEPGEIDLPTFPLFAlfGPALGMTSVI-PDMD 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 PT------PEEIGRVVREHGVTTLWLTAPLFHAVADRGLD---QLRGVRQLLAGGDVLSPKHVARVLLGLPA-LRLINGY 759
Cdd:PRK09274  243 PTrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEAngiKLPSLRRVISAGAPVPIAVIERFRAMLPPdAEILTPY 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  760 GPTE----------NTTFTTCHDVSRGMGTGsvpIGKPIANTHVYLLD---------EQMNPVPPNAVGELFTGGDGLAR 820
Cdd:PRK09274  323 GATEalpissiesrEILFATRAATDNGAGIC---VGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTR 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  821 GYHERPDQTAERFVPDPFSGVpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPAL-REAVV 898
Cdd:PRK09274  400 SYYNRPEATRLAKIPDGQGDV----WHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkRSALV 474
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 2001-2430 7.43e-20

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 96.00  E-value: 7.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAV 2080
Cdd:PRK07786   31 PDAPALRFLGNT-TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTTRPVCIVTdERHLGAVEIAARQL--GIEHVVSLdgdGKDADGNVVihGRRALADLADGNLPRAAGPHNM-AYVIFTS 2157
Cdd:PRK07786  110 VSDCGAHVVVT-EAALAPVATAVRDIvpLLSTVVVA---GGSSDDSVL--GYEDLLAEAGPAHAPVDIPNDSpALIMYTS 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2158 GSTGTPKGVVERHS----QVINLIewvnRTYLVGPSDRLLFVTSPSFDLS-VYDVFGMLAAGGS--IHIASEDDlrsPER 2230
Cdd:PRK07786  184 GTTGRPKGAVLTHAnltgQAMTCL----RTNGADINSDVGFVGVPLFHIAgIGSMLPGLLLGAPtvIYPLGAFD---PGQ 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2231 LAAELGRGTITFWDSAPAALQQLVPyfDRIEDGSQLRLAFLSGDWVPIG--MLDELRRAFPNVKLVGLGGATEATVWSNY 2308
Cdd:PRK07786  257 LLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDLALRVLSWGAAPASdtLLRQMAATFPEAQILAAFGQTEMSPVTCM 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2309 FEVDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlyRT 2388
Cdd:PRK07786  335 LLGEDAIRKLGSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF---------HS 403

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 260177242 2389 GDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK07786  404 GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHP 445
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 769-1043 7.84e-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: 92.51  E-value: 7.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TCHDVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGVPGARLYR 848
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  849 TGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGR-EAEVPRFSEL 927
Cdd:COG3433    81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAvAALDGLAAAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  928 RKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLSGRSGPFVAPEG-----HPEEVLARIWERVLRV--DAVG 1000
Cdd:COG3433   161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaletaLTEEELRADVAELLGVdpEEID 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 260177242 1001 REDNFFELGGDSILAIQVVAGAREVDLKLTVRQIFTHPTLSSL 1043
Cdd:COG3433   241 PDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAW 283
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 31-439 1.11e-19

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: 94.63  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   31 LVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSA--VDFGVTDGSSWDEPTAAAWLQAEAARPFDL 108
Cdd:cd19534    26 VLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLEVVDLSSLAQAAAIEALAAEAQSSLDL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  109 RAGALrVRA--LRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADVEGRAATLTPiSRGFRDYLVWHRDLLASDDA 186
Cdd:cd19534   106 EEGPL-LAAalFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPLPS-KTSFQTWAELLAEYAQSPAL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  187 SALVREWAamvgDLDVSTPLDLPTDLPRRAQQRyhVRQHFRdLGADLMDR-VRESARAEGVTTYTVLLAAYQVLLTRLSS 265
Cdd:cd19534   184 LEELAYWR----ELPAADYWGLPKDPEQTYGDA--RTVSFT-LDEEETEAlLQEANAAYRTEINDLLLAALALAFQDWTG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  266 QRPFLV---GcgvSGR---------TRTwqlgvVGHMAGIVPVPARIDAAATPRAIIRELRNALRvtaklqSVP------ 327
Cdd:cd19534   257 RAPPAIfleG---HGReeidpgldlSRT-----VGWFTSMYPVVLDLEASEDLGDTLKRVKEQLR------RIPnkgigy 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  328 -LSR-LAEQCRVPKSPGRMPlvqavfqEIrSFNEAirpEGFGHMLRwsrgPLGFEVEVPSELGSQLDLEVRCY---DFFS 402
Cdd:cd19534   323 gILRyLTPEGTKRLAFHPQP-------EI-SFNYL---GQFDQGER----DDALFVSAVGGGGSDIGPDTPRFallDINA 387

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 260177242  403 SSVRTC----WRYDPDLFLPETVERWADYYAALLRELVGDL 439
Cdd:cd19534   388 VVEGGQlvitVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 2015-2431 1.14e-19

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 95.26  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDEr 2094
Cdd:PRK09088   24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDD- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2095 hlgaveiaarqlgieHVVSLDGDGKDADGnvvihgRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVV--ERHSQ 2172
Cdd:PRK09088  103 ---------------AVAAGRTDVEDLAA------FIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMlsERNLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2173 --VINLiewvNRTYLVGPSDRLLfVTSPSFDLS--VYDVFGMLAAGGSIHIAsedDLRSPERLAAELGRGT--ITFWDSA 2246
Cdd:PRK09088  162 qtAHNF----GVLGRVDAHSSFL-CDAPMFHIIglITSVRPVLAVGGSILVS---NGFEPKRTLGRLGDPAlgITHYFCV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2247 PAALQQL--VPYFdrieDGSQLR--LAFLSGDwVPIGMLDELRRAFPNVKLVGLGGATEA-TVWSNYFEVDGIDPRWTSI 2321
Cdd:PRK09088  234 PQMAQAFraQPGF----DAAALRhlTALFTGG-APHAAEDILGWLDDGIPMVDGFGMSEAgTVFGMSVDCDVIRAKAGAA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2322 pyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIE 2401
Cdd:PRK09088  309 --GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW--------FRTGDIARRDADGFFW 378

                         410       420       430
                  ....*....|....*....|....*....|
gi 260177242 2402 FLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK09088  379 VVDRKKDMFISGGENVYPAEIEAVLADHPG 408
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 614-960 2.05e-19

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: 92.32  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  614 ENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG--SSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFpPESPT 691
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG-GENTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  692 PEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLRGVRQL---LAGGDVLSPKHVaRVLLGLPALRLINGYGPTEnTTFT 768
Cdd:cd17635    80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLrliGYGGSRAIAADV-RFIEATGLTNTAQVYGLSE-TGTA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TCHDVSRGMG-TGSVpiGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarly 847
Cdd:cd17635   158 LCLPTDDDSIeINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  848 RTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVV-GREAEVPRFSE 926
Cdd:cd17635   227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVaSAELDENAIRA 306

                         330       340       350
                  ....*....|....*....|....*....|....
gi 260177242  927 LRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDR 960
Cdd:cd17635   307 LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 1984-2431 2.44e-19

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 94.23  E-value: 2.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1984 ARERCIHELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGG 2063
Cdd:PRK08316    8 ARRQTIGDILRRSARRYPDKTALVFGDRS-WTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2064 AYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVSLD-GDGKDADGnvvihGRRALADLADGNLP 2142
Cdd:PRK08316   87 VHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLvLGGREAPG-----GWLDFADWAEAGSV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2143 RAAGPH----NMAYVIFTSGSTGTPKGVVERHSQVINliewvnrTYL-------VGPSDRLLFvTSPSFDLSVYDVFGM- 2210
Cdd:PRK08316  162 AEPDVEladdDLAQILYTSGTESLPKGAMLTHRALIA-------EYVscivagdMSADDIPLH-ALPLYHCAQLDVFLGp 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2211 -LAAGGSIHIASEDDlrsPERLAAELGRGTITFWDSAPAALQQLV--PYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRA 2287
Cdd:PRK08316  234 yLYVGATNVILDAPD---PELILRTIEAERITSFFAPPTVWISLLrhPDFDT-RDLSSLRKGYYGASIMPVEVLKELRER 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2288 FPNVKLVGLGGATE----ATVWSNyfevDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYA 2363
Cdd:PRK08316  310 LPGLRFYNCYGQTEiaplATVLGP----EEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWD 383

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 2364 DPSQTAERFVPDPFsgepgarlyRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK08316  384 DPEKTAEAFRGGWF---------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPA 442
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2014-2430 2.61e-19

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: 93.35  E-value: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDe 2093
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlgaveiaarqlgiehvvsLDGDGKDADGNVVIhgrraladladgnlpraagphnmayvIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd05973    80 --------------------AANRHKLDSDPFVM--------------------------MFTSGTTGLPKGVPVPLRAL 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLIEWVNRTYLVGPSDRLLFVTSPSFDLSVY-DVFGMLAAG-GSIHIASEDDLRSPERLAAELGrgtITFWDSAPAALQ 2251
Cdd:cd05973   114 AAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYyAITGPLALGhPTILLEGGFSVESTWRVIERLG---VTNLAGSPTAYR 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2252 QLVPYFDRIEDGSQLRLAFLSGDWVPIGmlDELRRAFPnvklVGLG-------GATEATVWSNYFEVDGIDPRWTSIpyG 2324
Cdd:cd05973   191 LLMAAGAEVPARPKGRLRRVSSAGEPLT--PEVIRWFD----AALGvpihdhyGQTELGMVLANHHALEHPVHAGSA--G 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2325 RPIQNARYYVLDRSGNPCPIGVTGDLYI---GGTCVSFGYYADPSQTAerfvpdpfsgePGARLYRTGDLARFFRDGNIE 2401
Cdd:cd05973   263 RAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMWFRGYQLPDTPA-----------IDGGYYLTGDTVEFDPDGSFS 331

                         410       420
                  ....*....|....*....|....*....
gi 260177242 2402 FLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05973   332 FIGRADDVITMSGYRIGPFDVESALIEHP 360
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 2014-2431 3.00e-19

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: 93.57  E-value: 3.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGayvpldprwplerVAAVLGTTrpvcivtde 2093
Cdd:cd05940     4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA-------------VAALINYN--------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlgaveiaARQLGIEHVVSLDgdgkdadgnvvihgrRALADLADgnlpraagphnMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd05940    62 ---------LRGESLAHCLNVS---------------SAKHLVVD-----------AALYIYTSGTTGLPKAAIISHRRA 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLIEWVNRTYLVGPSDRlLFVTSPSF--DLSVYDVFGMLAAGGSIHIAseddlrspERLAAElgrgtiTFWDSAPAALQ 2251
Cdd:cd05940   107 WRGGAFFAGSGGALPSDV-LYTCLPLYhsTALIVGWSACLASGATLVIR--------KKFSAS------NFWDDIRKYQA 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2252 QLVPYFDRI------------EDGSQLRLAF---LSGD-WvpigmlDELRRAFPNVKLVGLGGATEATVWS-NYFEVDGI 2314
Cdd:cd05940   172 TIFQYIGELcryllnqppkptERKHKVRMIFgngLRPDiW------EEFKERFGVPRIAEFYAATEGNSGFiNFFGKPGA 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2315 DPRWTSI-----PY---------GRPIQNARYYVLdrsgnPCPIGVTGdLYIG--GTCVSFGYYADPSQTAERFVPDPFs 2378
Cdd:cd05940   246 IGRNPSLlrkvaPLalvkydlesGEPIRDAEGRCI-----KVPRGEPG-LLISriNPLEPFDGYTDPAATEKKILRDVF- 318

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2379 gEPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05940   319 -KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPG 370
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 499-938 8.89e-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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 92.14  E-value: 8.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  499 SYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAG 578
Cdd:cd05910     4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGIPK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  579 AEErlgegpwtvvrldedlgrpderDAApndnvsaenlayVMYTSGSTGKPKGVAVTHRNV---VRLVRgssfATFGPdq 655
Cdd:cd05910    84 ADE----------------------PAA------------ILFTSGSTGTPKGVVYRHGTFaaqIDALR----QLYGI-- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  656 vflmmAPAAFDASTFEIWGalLHGARLVL---FPPESPT------PEEIGRVVREHGVTTLWLTAPLFHAVADRGLD--- 723
Cdd:cd05910   124 -----RPGEVDLATFPLFA--LFGPALGLtsvIPDMDPTrparadPQKLVGAIRQYGVSIVFGSPALLERVARYCAQhgi 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  724 QLRGVRQLLAGGDVLSPKHVARVLLGL-PALRLINGYGPTE----------NTTFTTCHDVSRGMGTGsvpIGKPIANTH 792
Cdd:cd05910   197 TLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEalpvssigsrELLATTTAATSGGAGTC---VGRPIPGVR 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  793 VYLLD---------EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGVpgarLYRTGDLARYLPNGDMEF 863
Cdd:cd05910   274 VRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGF----WHRMGDLGYLDDEGRLWF 349

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  864 LGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAReDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDH 938
Cdd:cd05910   350 CGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 614-915 9.55e-19

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 92.94  E-value: 9.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  614 ENLAYVMYTSGSTGKPKGVAVTHRN-VVRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPP-ESPT 691
Cdd:PLN02860  172 DDAVLICFTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKfDAKA 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  692 PEEigrVVREHGVTTLwLTAP-----LFHAVADRGLDQLR-GVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTE-- 763
Cdd:PLN02860  252 ALQ---AIKQHNVTSM-ITVPammadLISLTRKSMTWKVFpSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEac 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  764 -NTTFTTCHDVSRGMGT-----------------GSVPIGKPIAntHVYLldeQMNPVPPNAVGELFTGGDGLARGYHER 825
Cdd:PLN02860  328 sSLTFMTLHDPTLESPKqtlqtvnqtksssvhqpQGVCVGKPAP--HVEL---KIGLDESSRVGRILTRGPHVMLGYWGQ 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  826 PDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREdrp 905
Cdd:PLN02860  403 NSETASVLSNDGW--------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP--- 471

                         330
                  ....*....|
gi 260177242  906 gDKRLVAYVV 915
Cdd:PLN02860  472 -DSRLTEMVV 480
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 1949-2431 9.74e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 92.80  E-value: 9.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1949 AIADDPDLPTGDLPLlsaherrqvvadwNDTARAYARERcihelfessversPGSVALCYDGvPPLTYSDLNGRANRLGW 2028
Cdd:PRK06178   21 GIPREPEYPHGERPL-------------TEYLRAWARER-------------PQRPAIIFYG-HVITYAELDELSDRFAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2029 LLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGI 2108
Cdd:PRK06178   74 LLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2109 EHVV------------------SLDGDGKDADGnvVIHGRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERH 2170
Cdd:PRK06178  154 RHVIvtsladvlpaeptlplpdSLRAPRLAAAG--AIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2171 SQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDvFGMLA---AGGSIHIASEDD----LRSPERLAAELGRGTItfw 2243
Cdd:PRK06178  232 RDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGEN-FGLLFplfSGATLVLLARWDavafMAAVERYRVTRTVMLV--- 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2244 DSAPAALQQlvPYFDRIeDGSQLRLAFLSGDwvpIGMLD-ELRRAFP----NVKLVGLGGATE---ATVWSNYFEVDGID 2315
Cdd:PRK06178  308 DNAVELMDH--PRFAEY-DLSSLRQVRVVSF---VKKLNpDYRQRWRaltgSVLAEAAWGMTEthtCDTFTAGFQDDDFD 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2316 PRWTSIPYGRPIQNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVpDPFsgepgarlYRTGDLARF 2394
Cdd:PRK06178  382 LLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-DGW--------LHTGDIGKI 452

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 260177242 2395 FRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK06178  453 DEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPA 489
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 2014-2430 2.95e-18

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: 90.23  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPrwplervaavlgttrpvCIVTDE 2093
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP-----------------MLKERE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlgaveiaarqlgIEHVVsldgdgKDADGNVVIhgrrALADLADgnlpraagphnMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd05935    65 --------------LEYIL------NDSGAKVAV----VGSELDD-----------LALIPYTSGTTGLPKGCMHTHFSA 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLIEWVNRTYLVGPSDRLLfVTSPSFDLS--VYDVFGMLAAGGSIHIASEDDlrsPERLAAELGRGTITFWDSAPAALQ 2251
Cdd:cd05935   110 AANALQSAVWTGLTPSDVIL-ACLPLFHVTgfVGSLNTAVYVGGTYVLMARWD---RETALELIEKYKVTFWTNIPTMLV 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2252 QLV--PYFdRIEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEATVWSNyfevdgIDP--RWTSIPYGRPI 2327
Cdd:cd05935   186 DLLatPEF-KTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTH------TNPplRPKLQCLGIP* 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2328 QNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPfsgepGARLYRTGDLARFFRDGNIEFLGRA 2406
Cdd:cd05935   258 FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK-----GRRFFRTGDLGYMDEEGYFFFVDRV 332

                         410       420
                  ....*....|....*....|....
gi 260177242 2407 DSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05935   333 KRMINVSGFKVWPAEVEAKLYKHP 356
PRK13382 PRK13382
bile acid CoA ligase;
477-966 4.36e-18

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 90.59  E-value: 4.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  477 LFEEEARRVPDAVAL--DAGSnvVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDP 554
Cdd:PRK13382   48 GFAIAAQRCPDRPGLidELGT--LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  555 AYPSERLAFLAHDAGVQIVLS----AAGAEERLGEGPWTVVRLDedlgRPDERDAAPNDNVSAENLA-----------YV 619
Cdd:PRK13382  126 SFAGPALAEVVTREGVDTVIYdeefSATVDRALADCPQATRIVA----WTDEDHDLTVEVLIAAHAGqrpeptgrkgrVI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  620 MYTSGSTGKPKGVavthrnvvrlvRGSSFATFGPDQVFL----MMA--PAAFDASTFEIWG------ALLHGARLVL--- 684
Cdd:PRK13382  202 LLTSGTTGTPKGA-----------RRSGPGGIGTLKAILdrtpWRAeePTVIVAPMFHAWGfsqlvlAASLACTIVTrrr 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  685 FPPESPTpeeigRVVREHGVTTLWLTAPLFHAVAD---RGLDQL--RGVRQLLAGGDVLSPKHVARVLLGLPALrLINGY 759
Cdd:PRK13382  271 FDPEATL-----DLIDRHRATGLAVVPVMFDRIMDlpaEVRNRYsgRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNY 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  760 GPTENTTFTTC--HDVSRGMGTGsvpiGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQ-TAERFVPd 836
Cdd:PRK13382  345 NATEAGMIATAtpADLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKdFHDGFMA- 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  837 pfsgvpgarlyrTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVG 916
Cdd:PRK13382  420 ------------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL 487

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242  917 REAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAP 966
Cdd:PRK13382  488 KPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 615-963 5.17e-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: 88.31  E-value: 5.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRNVVRLVR-GSSFATFGPDQVFLMMAPAAFDASTFEIWGALLH-GARLVLFPP---ES 689
Cdd:cd05944     3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWmLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLAsGAHVVLAGPagyRN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 PTP-EEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTTFT 768
Cdd:cd05944    83 PGLfDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TCHDVSRGMGTGSVPIGKPIANTHVYLLDEQMN---PVPPNAVGELFTGGDGLARGY----HERPDQTAERFVpdpfsgv 841
Cdd:cd05944   163 AVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRllrDCAPDEVGEICVAGPGVFGGYlyteGNKNAFVADGWL------- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  842 pgarlyRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEV 921
Cdd:cd05944   236 ------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 260177242  922 PRFSELRKFLLQRLPDH-MIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05944   310 VEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 1962-2433 5.30e-18

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 90.50  E-value: 5.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1962 PLLSAHERRQVVAdwndtaRAYARERCIHELFESSVERSPGSVALC-----YDGVPPLTYSDLNGRANRLGWLLRGLGAG 2036
Cdd:PRK13295    5 AVLLPPRRAASIA------AGHWHDRTINDDLDACVASCPDKTAVTavrlgTGAPRRFTYRELAALVDRVAVGLARLGVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2037 PEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRP-VCIVTDE-RHLGAVEIAAR------QLgi 2108
Cdd:PRK13295   79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESkVLVVPKTfRGFDHAAMARRlrpelpAL-- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2109 EHVVSLDGDGKDADGNVVIHGRRALADLADGNLPR-AAGPHNMAYVIFTSGSTGTPKGVVERHSQVI-NLIEWVNRTYLv 2186
Cdd:PRK13295  157 RHVVVVGGDGADSFEALLITPAWEQEPDAPAILARlRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMaNIVPYAERLGL- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2187 gPSDRLLFVTSPSFDLSVYdVFGM---LAAGGSihiASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFD-RIED 2262
Cdd:PRK13295  236 -GADDVILMASPMAHQTGF-MYGLmmpVMLGAT---AVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKeSGRP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2263 GSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATE---ATVwsnyfEVDGIDPRWTSIPYGRPIQNARYYVLDRSG 2339
Cdd:PRK13295  311 VSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTEngaVTL-----TKLDDPDERASTTDGCPLPGVEVRVVDADG 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2340 NPCPIGVTGDLYIGGTCVSFGYYADPSQTAerfvpDPFSGepgarLYRTGDLARFFRDGNIEFLGRAdSQVKIRG-YRIE 2418
Cdd:PRK13295  385 APLPAGQIGRLQVRGCSNFGGYLKRPQLNG-----TDADG-----WFDTGDLARIDADGYIRISGRS-KDVIIRGgENIP 453

                         490
                  ....*....|....*
gi 260177242 2419 CGEVEVALAQHPGAQ 2433
Cdd:PRK13295  454 VVEIEALLYRHPAIA 468
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 2014-2431 5.31e-18

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: 89.99  E-value: 5.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:cd05904    33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHLGAVEIAARQlgiehVVSLDGDGKDADGNVVihgrraLADLADGNLPRAA--GPHNMAYVIFTSGSTGTPKGVVERHS 2171
Cdd:cd05904   113 ELAEKLASLALP-----VVLLDSAEFDSLSFSD------LLFEADEAEPPVVviKQDDVAALLYSSGTTGRSKGVMLTHR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2172 QVINLIE-WVNRTYLVGPSDRLLFVTSPSFDLSVYDVF--GMLAAGGSIHIASEDDLRSperLAAELGRGTITFWDSAPA 2248
Cdd:cd05904   182 NLIAMVAqFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFalGLLRLGATVVVMPRFDLEE---LLAAIERYKVTHLPVVPP 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2249 ALQQLVPyfDRIEDGSQLR-LAFLSGDWVPIG--MLDELRRAFPNVKLVGLGGATEAT-VWSNYFEVDGIDPRWTSIpyG 2324
Cdd:cd05904   259 IVLALVK--SPIVDKYDLSsLRQIMSGAAPLGkeLIEAFRAKFPNVDLGQGYGMTESTgVVAMCFAPEKDRAKYGSV--G 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2325 RPIQNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFL 2403
Cdd:cd05904   335 RLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW--------LHTGDLCYIDEDGYLFIV 406

                         410       420
                  ....*....|....*....|....*...
gi 260177242 2404 GRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05904   407 DRLKELIKYKGFQVAPAELEALLLSHPE 434
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 1987-2431 6.65e-18

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: 89.49  E-value: 6.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1987 RCIHELFESSVERSPGSVALCY-DGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAY 2065
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2066 VPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHgrraladladgnlPRAA 2145
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIE-------------DPPR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2146 GPHNMAYVIFTSGSTGTPKGVV--ERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASED 2223
Cdd:cd05923   148 EPEQPAFVFYTSGTTGLPKGAVipQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2224 DlrSPERLAAELGRGTITFWDSAPAALQQLVPYFDRI-EDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKlVGLGGATEA 2302
Cdd:cd05923   228 F--DPADALKLIEQERVTSLFATPTHLDALAAAAEFAgLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK-VNIYGTTEA 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2303 TVwSNYFEvdgiDPRWTSIpyGRPIQNARYYVLDRSGNP---CPIGVTGDLYI--GGTCVSFGYYADPSQTAERFVpdpf 2377
Cdd:cd05923   305 MN-SLYMR----DARTGTE--MRPGFFSEVRIVRIGGSPdeaLANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ---- 373

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 260177242 2378 sgepgARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05923   374 -----DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPG 422
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 478-941 9.48e-18

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 89.93  E-value: 9.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDpayP 557
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN---T 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  558 SERLAFLAH-----DAGVQIV---LSAAGAEER---LGEGPWTVVRLDEDLGRPDERDAA------PNDN------VSAE 614
Cdd:PRK08279  120 QQRGAVLAHslnlvDAKHLIVgeeLVEAFEEARadlARPPRLWVAGGDTLDDPEGYEDLAaaaagaPTTNpasrsgVTAK 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRNVvrLVRGSSFA---TFGPDQVFLMMAP----AAFDAStfeiWG-ALLHGARLVL-- 684
Cdd:PRK08279  200 DTAFYIYTSGTTGLPKAAVMSHMRW--LKAMGGFGgllRLTPDDVLYCCLPlyhnTGGTVA----WSsVLAAGATLALrr 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  685 ------FPPEsptpeeigrvVREHGVTTL---------WLTAPlfHAVADRGlDQLRgvrqlLAGGDVLSP----KHVAR 745
Cdd:PRK08279  274 kfsasrFWDD----------VRRYRATAFqyigelcryLLNQP--PKPTDRD-HRLR-----LMIGNGLRPdiwdEFQQR 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  746 vlLGLPalRLINGYGPTE-NTTFTTCHDVSRGMGTGSVPIGKPIA--------NTHVYLLDEQMNPVPPNAVGELFTGGD 816
Cdd:PRK08279  336 --FGIP--RILEFYAASEgNVGFINVFNFDGTVGRVPLWLAHPYAivkydvdtGEPVRDADGRCIKVKPGEVGLLIGRIT 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  817 GLAR--GYhERPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALR 894
Cdd:PRK08279  412 DRGPfdGY-TDPEASEKKILRDVFK--KGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVE 488

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242  895 EAVV----IARED-RPGdkrLVAYVVGREAEVpRFSELRKFLLQRLPDHMIP 941
Cdd:PRK08279  489 EAVVygveVPGTDgRAG---MAAIVLADGAEF-DLAALAAHLYERLPAYAVP 536
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 486-957 1.00e-17

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: 90.02  E-value: 1.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  486 PDAVALDAGSN----VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPS--- 558
Cdd:cd05943    83 DDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVpgv 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  559 -ERLA-----FLAHDAGVQ-------------------------IVLSAAGAEERL-GEGPWTVVRLDEDLGRPDerdAA 606
Cdd:cd05943   163 lDRFGqiepkVLFAVDAYTyngkrhdvrekvaelvkglpsllavVVVPYTVAAGQPdLSKIAKALTLEDFLATGA---AG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  607 PND--NVSAENLAYVMYTSGSTGKPK-------GVAVTHRNVVRLvrgssFATFGPDQVFL-------MMapaafdastf 670
Cdd:cd05943   240 ELEfePLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHIL-----HCDLRPGDRLFyyttcgwMM---------- 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  671 eiW----GALLHGARLVLF--PPESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQ-----LRGVRQLLAGGDVLS 739
Cdd:cd05943   305 --WnwlvSGLAVGATIVLYdgSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPaethdLSSLRTILSTGSPLK 382

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  740 P-------KHV-ARVLLGLpalrlINGygpteNTTFTTCH-------DVSRGmgtgsvPIGKPIANTHVYLLDEQMNPVP 804
Cdd:cd05943   383 PesfdyvyDHIkPDVLLAS-----ISG-----GTDIISCFvggnpllPVYRG------EIQCRGLGMAVEAFDEEGKPVW 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  805 pNAVGELF--TGGDGLARGYHERPDqtAERFVPDPFSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAE 882
Cdd:cd05943   447 -GEKGELVctKPFPSMPVGFWNDPD--GSRYRAAYFAKYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAE 521

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  883 VEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVprFS-ELRKFLLQRL-----PDHmIPAAVVALDKLPLVPSG 956
Cdd:cd05943   522 IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVE--LDdELRKRIRSTIrsalsPRH-VPAKIIAVPDIPRTLSG 598


                  .
gi 260177242  957 K 957
Cdd:cd05943   599 K 599
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 1991-2431 2.88e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 87.73  E-value: 2.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALcYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP 2070
Cdd:PRK06188   16 HLLVSALKRYPDRPAL-VLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 RWPLERVAAVLGTTRP-VCIVTDERHLG-AVEIAARQLGIEHVVSLD--GDGKDadgnvvihgrraLADLADGNLPR--- 2143
Cdd:PRK06188   95 LGSLDDHAYVLEDAGIsTLIVDPAPFVErALALLARVPSLKHVLTLGpvPDGVD------------LLAAAAKFGPAplv 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2144 -AAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTsPSFDLSVYDVFGMLAAGGSIHIASE 2222
Cdd:PRK06188  163 aAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCT-PLSHAGGAFFLPTLLRGGTVIVLAK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2223 DDlrsPERL--AAELGRGTITFwdsapaalqqLVP---YfdRIEDGSQLRLAFLSG-DWVPIGM-------LDELRRAFP 2289
Cdd:PRK06188  242 FD---PAEVlrAIEEQRITATF----------LVPtmiY--ALLDHPDLRTRDLSSlETVYYGAspmspvrLAEAIERFG 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2290 NVkLVGLGGATEATVWSNYF---EVDGIDP-RWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADP 2365
Cdd:PRK06188  307 PI-FAQYYGQTEAPMVITYLrkrDHDPDDPkRLTSC--GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRP 383

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 2366 SQTAERFvpdpfsgePGARLyRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK06188  384 EETAEAF--------RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPA 440
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1065-1494 3.30e-17

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: 86.66  E-value: 3.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1065 PLTPIQR--WFL-SGEPAAPHhFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSGGPVPYEV 1141
Cdd:cd19539     3 PLSFAQErlWFIdQGEDGGPA-YNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1142 VDLSELPGEERRAALEARAAEAQASLDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEG 1221
Cdd:cd19539    82 RDLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDD-HVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1222 EIVRLPSKTTSLR---RWGERLLAtvDEVVAAELPFW-EALDGQGVRPLPrGCEPAEDREGDAQTVEVWLGGPETEALLG 1297
Cdd:cd19539   161 PAAPLPELRQQYKeyaAWQREALA--APRAAELLDFWrRRLRGAEPTALP-TDRPRPAGFPYPGADLRFELDAELVAALR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1298 RVGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREElfPDIEvaRTVGWFTTIHPVVLPGRPQSagarlkAVKE 1377
Cdd:cd19539   238 ELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFE--STVGFFVNLLPLRVDVSDCA------TFRD 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1378 AIRRVPKHGIGYGILRYLGSDEVVTRL------ARLPAPEVAFNYLGRLDRALPKDGPFVMAPEAAGPSVSPRGkrshaL 1451
Cdd:cd19539   308 LIARVRKALVDAQRHQELPFQQLVAELpvdrdaGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFD-----L 382

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 260177242 1452 QTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIA 1494
Cdd:cd19539   383 NLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLA 425
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 1999-2430 3.55e-17

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 87.25  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1999 RSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVA 2078
Cdd:PRK06145   14 RTPDRAALVYRD-QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2079 AVLGTTRPVCIVTDErhlgavEIAArQLGIEHVVSLDGDGKDADGNVVIHGRRALADLAdgnlprAAGPHNMAYVIFTSG 2158
Cdd:PRK06145   93 YILGDAGAKLLLVDE------EFDA-IVALETPKIVIDAAAQADSRRLAQGGLEIPPQA------AVAPTDLVRLMYTSG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2159 STGTPKGVVERHSQVinliEW--VNRTYLVG--PSDRLLfVTSPSFDLSVYDVFGM--LAAGGSIHIASEDDlrsPERLA 2232
Cdd:PRK06145  160 TTDRPKGVMHSYGNL----HWksIDHVIALGltASERLL-VVGPLYHVGAFDLPGIavLWVGGTLRIHREFD---PEAVL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2233 AELGRGTITFWDSAPAALQQL--VPYFDRIEDGSqLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEA----TVWS 2306
Cdd:PRK06145  232 AAIERHRLTCAWMAPVMLSRVltVPDRDRFDLDS-LAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETcsgdTLME 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2307 NYFEVDGIDPRwtsipyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarly 2386
Cdd:PRK06145  311 AGREIEKIGST------GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------- 375

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 260177242 2387 RTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK06145  376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELP 419
PRK07529 PRK07529
AMP-binding domain protein; Validated
 1990-2430 3.86e-17

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 88.09  E-value: 3.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1990 HELFESSVERSPGSVALCY--DGVP-----PLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTG 2062
Cdd:PRK07529   28 YELLSRAAARHPDAPALSFllDADPldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2063 GAyVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGA-----VEIAARQL-GIEHVVSLDGDG------------KDADGN 2124
Cdd:PRK07529  108 IA-NPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTdiwqkVAEVLAALpELRTVVEVDLARylpgpkrlavplIRRKAH 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2125 VVIHGRRALADLADGNL---PRAAGPHNMAYVIFTSGSTGTPKGVVERHS-QVINliEWV-NRTYLVGPSDRLLfvtsps 2199
Cdd:PRK07529  187 ARILDFDAELARQPGDRlfsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGnEVAN--AWLgALLLGLGPGDTVF------ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2200 FDLSVYDVFG-------MLAAGGSIHIASEDDLRSPE---RLAAELGRGTITFWDSAPAALQQL--VPYFDRieDGSQLR 2267
Cdd:PRK07529  259 CGLPLFHVNAllvtglaPLARGAHVVLATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALlqVPVDGH--DISSLR 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2268 LAFLSGDWVPIgmldELRRAFPN---VKLVGLGGATEATVWSNYFEVDG-IDPRWTSIPYgrPIQNARYYVLDRSGN--- 2340
Cdd:PRK07529  337 YALCGAAPLPV----EVFRRFEAatgVRIVEGYGLTEATCVSSVNPPDGeRRIGSVGLRL--PYQRVRVVILDDAGRylr 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2341 PCPIGVTGDLYIGGTCVsFGYYADPSQTAERFVPDpfsgepgaRLYRTGDLARFFRDGNIEFLGRADSQVkIR-GYRIEC 2419
Cdd:PRK07529  411 DCAVDEVGVLCIAGPNV-FSGYLEAAHNKGLWLED--------GWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDP 480

                         490
                  ....*....|.
gi 260177242 2420 GEVEVALAQHP 2430
Cdd:PRK07529  481 AAIEEALLRHP 491
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 584-891 4.76e-17

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 87.86  E-value: 4.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  584 GEGPWTVVRLD--EDLGRPDERDAapnDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG--SSFATFGPDQVFLM 659
Cdd:PLN02387  221 GSSNWTVSSFSevEKLGKENPVDP---DLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGvmTVVPKLGKNDVYLA 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  660 MAPAAF------DASTFEIWGALLHGARLVLFPPES--------------PT-----PEEIGRV---VREHGVTTLWLTA 711
Cdd:PLN02387  298 YLPLAHilelaaESVMAAVGAAIGYGSPLTLTDTSNkikkgtkgdasalkPTlmtavPAILDRVrdgVRKKVDAKGGLAK 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  712 PLFHAVADRGLDQLRG----------------------------VRQLLAGGDVLSP--KHVARVLLGLPalrLINGYGP 761
Cdd:PLN02387  378 KLFDIAYKRRLAAIEGswfgawglekllwdalvfkkiravlggrIRFMLSGGAPLSGdtQRFINICLGAP---IGQGYGL 454

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  762 TEN---TTFTTCHDVSRGMgtgsvpIGKPIANTHVYLLD-EQMN------PVPPnavGELFTGGDGLARGYHERPDQTAE 831
Cdd:PLN02387  455 TETcagATFSEWDDTSVGR------VGPPLPCCYVKLVSwEEGGylisdkPMPR---GEIVIGGPSVTLGYFKNQEKTDE 525

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260177242  832 RFVPDPfsgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIR-GFRIELAEVEAALLQHP 891
Cdd:PLN02387  526 VYKVDE----RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1564-1953 5.14e-17

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: 85.70  E-value: 5.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1564 LALEGALDFDRLQQAWDETLGAHPALRASFlwegVPEPLQVVRRLVRIPTERIDARSMAVdgdawiveraRDERRRGFAL 1643
Cdd:cd19537    30 CRLSGDVDRDRLASAWNTVLARHRILRSRY----VPRDGGLRRSYSSSPPRVQRVDTLDV----------WKEINRPFDL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1644 DAAPAMRLLLvrtgDRSHRLIwTFHHILLDGWSVPLVLEEVFKRYSGGMQHeaahrTAPRPHRDYVAWLRGADaQSVERF 1723
Cdd:cd19537    96 EREDPIRVFI----SPDTLLV-VMSHIICDLTTLQLLLREVSAAYNGKLLP-----PVRREYLDSTAWSRPAS-PEDLDF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1724 WRRELGGfreVTPLGIDRPPAGqraSSYR--RFERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFG 1801
Cdd:cd19537   165 WSEYLSG---LPLLNLPRRTSS---KSYRgtSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1802 ETVSGRSAPLEgiERMVGLFINTVPMRAVVDPERP--IGEWLTELqgRRAERtayehASLAQVQAWSEvphgsaLFESLI 1879
Cdd:cd19537   239 APYLNRTSEED--METVGLFLEPLPIRIRFPSSSDasAADFLRAV--RRSSQ-----AALAHAIPWHQ------LLEHLG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1880 VVENYPVAPAF---------SGDELSVRLVGGDEQTNYP--------VTLVALPGRRLTLRLLYEAERIPDGAAEGVLSH 1942
Cdd:cd19537   304 LPPDSPNHPLFdvmvtfhddRGVSLALPIPGVEPLYTWAegakfplmFEFTALSDDSLLLRLEYDTDCFSEEEIDRIESL 383

                         410
                  ....*....|.
gi 260177242 1943 LESLLCAIADD 1953
Cdd:cd19537   384 ILAALELLVEG 394
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 502-866 6.91e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 86.92  E-value: 6.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  502 ELNRRADKLAHMLRLKGVgTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPS---ERLAFLAHDAGVQIVLSAAG 578
Cdd:PRK05850   40 QLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  579 AEERL--------GEGPWTVVRLDE-DLGRPDERDAAPNDnvsAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFA 649
Cdd:PRK05850  119 VVDDVteyvapqpGQSAPPVIEVDLlDLDSPRGSDARPRD---LPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSD 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  650 TFGPDQVFlmmAPAafdASTFEIWGALLH--------------GARLVLFPPES--PTPEEIGRVVREHGVTtlWLTAPL 713
Cdd:PRK05850  196 YFGDTGGV---PPP---DTTVVSWLPFYHdmglvlgvcapilgGCPAVLTSPVAflQRPARWMQLLASNPHA--FSAAPN 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FH---AV-----AD-RGLDqLRGVRQLLAGGDVLSPKHVARVL-----LGLPALRLINGYGPTENTTF-----------T 768
Cdd:PRK05850  268 FAfelAVrktsdDDmAGLD-LGGVLGIISGSERVHPATLKRFAdrfapFNLRETAIRPSYGLAEATVYvatrepgqppeS 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TCHD--------VSR---GMGTGSVPIGKPIANThVYLLD-EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERF--- 833
Cdd:PRK05850  347 VRFDyeklsaghAKRcetGGGTPLVSYGSPRSPT-VRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgat 425

                         410       420       430
                  ....*....|....*....|....*....|...
gi 260177242  834 VPDPFSGVPGARLYRTGDLArYLPNGDMEFLGR 866
Cdd:PRK05850  426 LVDPSPGTPEGPWLRTGDLG-FISEGELFIVGR 457
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 619-963 8.76e-17

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: 86.37  E-value: 8.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNVVR--LVRGSSFATFGPDQVFLMM-----APAAFdASTFEIW--GALLHGARLVLFPPES 689
Cdd:cd05928   179 IYFTSGTTGSPKMAEHSHSSLGLglKVNGRYWLDLTASDIMWNTsdtgwIKSAW-SSLFEPWiqGACVFVHHLPRFDPLV 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 ptpeeIGRVVREHGVTTLWLTAPLFHAVADRGLD--QLRGVRQLLAGGDVLSPKHVA--RVLLGLpalRLINGYGPTEnt 765
Cdd:cd05928   258 -----ILKTLSSYPITTFCGAPTVYRMLVQQDLSsyKFPSLQHCVTGGEPLNPEVLEkwKAQTGL---DIYEGYGQTE-- 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  766 TFTTChDVSRGMGTGSVPIGKPIANTHVYLLDEQMNPVPPNAVGELF-----TGGDGLARGYHERPDQTAERFVPDpfsg 840
Cdd:cd05928   328 TGLIC-ANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGirvkpIRPFGLFSGYVDNPEKTAATIRGD---- 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  841 vpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVgreaE 920
Cdd:cd05928   403 -----FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVV----L 473

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242  921 VPRF-SELRKFLLQRLPDHM--------IPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05928   474 APQFlSHDPEQLTKELQQHVksvtapykYPRKVEFVQELPKTVTGKIQRNEL 525
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
472-963 9.64e-17

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 86.47  E-value: 9.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  472 RCLHHLFEEEARRVPDAVALDAGSNVVSYGELNRRADKLA-HMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYV 550
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAaYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  551 PLDPAYPSERLAFLAHDAGVQIVLS----AAGAEERLGEGPWTVV---RLDEDLGRPDE--------------------- 602
Cdd:PRK08751  105 NVNPLYTPRELKHQLIDSGASVLVVidnfGTTVQQVIADTPVKQVittGLGDMLGFPKAalvnfvvkyvkklvpeyring 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  603 ----RDA--------APNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV-------RLVRGSSFATFGPDQVFLMMAPA 663
Cdd:PRK08751  185 airfREAlalgrkhsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqqahQWLAGTGKLEEGCEVVITALPLY 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  664 AFDAST-----FEIWGALLHgarLVLFPPESPT-PEEIGRV--VREHGVTTLW---LTAPlfhavadrGLDQL--RGVRQ 730
Cdd:PRK08751  265 HIFALTanglvFMKIGGCNH---LISNPRDMPGfVKELKKTrfTAFTGVNTLFnglLNTP--------GFDQIdfSSLKM 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  731 LLAGGDVLSpKHVARVLLGLPALRLINGYGPTENTTFTTCHDVSRGMGTGSvpIGKPIANTHVYLLDEQMNPVPPNAVGE 810
Cdd:PRK08751  334 TLGGGMAVQ-RSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGS--IGLPIPSTDACIKDDAGTVLAIGEIGE 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  811 LFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQH 890
Cdd:PRK08751  411 LCIKGPQVMKGYWKRPEETAKVMDADGW--------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242  891 PALRE-AVVIAREDRPGDkrLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PRK08751  483 PGVLEvAAVGVPDEKSGE--IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2147-2433 9.94e-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: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 84.25  E-value: 9.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2147 PHNMAYVIFTSGSTGTPKGVVERHSQVINliewvnRTYLVGpsDRLLFVTSPSFDLSV--YDVFGM----LAA---GGSI 2217
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVN------NGYFIG--ERLGLTEQDRLCIPVplFHCFGSvlgvLAClthGATM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2218 HIASE-----DDLRSPERLAAELGRGTITFWDsapAALQQlvPYFDRiEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVK 2292
Cdd:cd05917    73 VFPSPsfdplAVLEAIEKEKCTALHGVPTMFI---AELEH--PDFDK-FDLSSLRTGIMAGAPCPPELMKRVIEVM-NMK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2293 LVGLG-GATEAT-VWSNYFEVDGIDPRWTSIpyGRPIQNARYYVLDRSGNP-CPIGVTGDLYIGGTCVSFGYYADPSQTA 2369
Cdd:cd05917   146 DVTIAyGMTETSpVSTQTRTDDSIEKRVNTV--GRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVMKGYWNDPEKTA 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242 2370 ERFVPDpfsgepgaRLYRTGDLARFFRDGNIEFLGRADSQVkIRG-YRIECGEVEVALAQHPGAQ 2433
Cdd:cd05917   224 EAIDGD--------GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVS 279
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 474-974 2.30e-16

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 85.56  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  474 LHHLFEEEARRVPDAVA---LD-----AGSNV-VSYGELNRRADKL-AHMLRLKGVGTetRVGLCLERSVELVVGILGVL 543
Cdd:PRK12476   36 LISLIERNIANVGDTVAyryLDhshsaAGCAVeLTWTQLGVRLRAVgARLQQVAGPGD--RVAILAPQGIDYVAGFFAAI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  544 KAGGAYVPL-DPAYP--SERLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLDedlgRP------DERDAAPNDNVSAE 614
Cdd:PRK12476  114 KAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLR----RPrviaidAIPDSAGESFVPVE 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 ----NLAYVMYTSGSTGKPKGVAVTHR----NVVRLV----------RGSSFATFGPDQVFLM-------------MAPA 663
Cdd:PRK12476  190 ldtdDVSHLQYTSGSTRPPVGVEITHRavgtNLVQMIlsidlldrntHGVSWLPLYHDMGLSMigfpavygghstlMSPT 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  664 AFDASTFEIWGALLHGARlvlfppesptpeeIGRVVRehgvttlwlTAPLF--HAVADRGLDQ------LRGVrQLLAGG 735
Cdd:PRK12476  270 AFVRRPQRWIKALSEGSR-------------TGRVVT---------AAPNFayEWAAQRGLPAegddidLSNV-VLIIGS 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  736 DVLSPKHV-----ARVLLGLPALRLINGYGPTENTTF--TTCHDVS--------RGMGTG---SVPIGKPIANTHV---- 793
Cdd:PRK12476  327 EPVSIDAVttfnkAFAPYGLPRTAFKPSYGIAEATLFvaTIAPDAEpsvvyldrEQLGAGravRVAADAPNAVAHVscgq 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  794 -------YLLDEQM-NPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFSGVP----------GARLYRTGDLARY 855
Cdd:PRK12476  407 varsqwaVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRLAegshadgaadDGTWLRTGDLGVY 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  856 LpNGDMEFLGRRDGQVKIRGFRIELAEVEA-ALLQHPALREAVVIAREdRPGDKRLVAYVV-------GREAEVPRFSEL 927
Cdd:PRK12476  487 L-DGELYITGRIADLIVIDGRNHYPQDIEAtVAEASPMVRRGYVTAFT-VPAEDNERLVIVaeraagtSRADPAPAIDAI 564

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242  928 RKFLLQRlpdHMIPAA---VVALDKLPLVPSGKLDRRALPAPTLSGRSGP 974
Cdd:PRK12476  565 RAAVSRR---HGLAVAdvrLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 1986-2431 2.40e-16

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 85.20  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1986 ERCIHELFESSVERSPGSVaLCYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAY 2065
Cdd:PRK06155   20 ERTLPAMLARQAERYPDRP-LLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2066 VPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVE-IAARQLGIEHVVSLDGDGkdadGNVVIHGRRA--LADLADGNLP 2142
Cdd:PRK06155   99 VPINTALRGPQLEHILRNSGARLLVVEAALLAALEaADPGDLPLPAVWLLDAPA----SVSVPAGWSTapLPPLDAPAPA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2143 RAAGPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDrLLFVTSPSFDLSVYDVF-GMLAAGGSIHIAS 2221
Cdd:PRK06155  175 AAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-VLYTTLPLFHTNALNAFfQALLAGATYVLEP 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2222 EddlRSPERLAAELGR--GTITFWDSAPAALQQLVPYFDRiEDGSQLRLAFLSGdwVPIGMLDELRRAFpNVKLVGLGGA 2299
Cdd:PRK06155  254 R---FSASGFWPAVRRhgATVTYLLGAMVSILLSQPARES-DRAHRVRVALGPG--VPAALHAAFRERF-GVDLLDGYGS 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2300 TEATVwsnYFEVDGIDPRWTSIPYGRPIQNARyyVLDRSGNPCPIGVTGDLYIGGT---CVSFGYYADPSQTAERFVPDP 2376
Cdd:PRK06155  327 TETNF---VIAVTHGSQRPGSMGRLAPGFEAR--VVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLW 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260177242 2377 FsgepgarlyRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK06155  402 F---------HTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPA 447
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1975-2431 2.66e-16

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 84.80  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1975 DWNDTARA------YARERCIHELFESSVERSPGSVALCYDGVPPLTYSDLNGRANRLG-WLLrGLGAGPEERVVVWMDR 2047
Cdd:PRK06087    5 TFNEQRRAayrqqgYWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLAnWLL-AKGIEPGDRVAFQLPG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2048 APELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERH------LGAVEIAARQLGIEHVVSLDGDGKDa 2121
Cdd:PRK06087   84 WCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtrpvDLILPLQNQLPQLQQIVGVDKLAPA- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2122 dgnvviHGRRALADLADGNLPRAAGP----HNMAYVIFTSGSTGTPKGVVERHsqviNLIEWVNRTYLVG---PSDRLLF 2194
Cdd:PRK06087  163 ------TSSLSLSQIIADYEPLTTAItthgDELAAVLFTSGTEGLPKGVMLTH----NNILASERAYCARlnlTWQDVFM 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2195 VTSP-----SFDLSVydVFGMLAAGGSIhiaSEDDLRsPERLAAELGRGTITFWDSAPAALQQLVPYFDRIE-DGSQLRL 2268
Cdd:PRK06087  233 MPAPlghatGFLHGV--TAPFLIGARSV---LLDIFT-PDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPaDLSALRF 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2269 AFLSGDWVPIGMLDELRRAfpNVKLVGLGGATEAtvwSNYFEVDGIDP-RWTSIPYGRPIQNARYYVLDRSGNPCPIGVT 2347
Cdd:PRK06087  307 FLCGGTTIPKKVARECQQR--GIKLLSVYGSTES---SPHAVVNLDDPlSRFMHTDGYAAAGVEIKVVDEARKTLPPGCE 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2348 GDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRaDSQVKIR-GYRIECGEVEVAL 2426
Cdd:PRK06087  382 GEEASRGPNVFMGYLDEPELTARALDEEGW--------YYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDIL 452


                  ....*
gi 260177242 2427 AQHPG 2431
Cdd:PRK06087  453 LQHPK 457
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 2014-2430 2.91e-16

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: 84.33  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVtde 2093
Cdd:cd17640     6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlgaveiaarqlgiehvvsLDGDGKDadgnvvihgrraladladgnlpraagphnMAYVIFTSGSTGTPKGVVERH--- 2170
Cdd:cd17640    83 --------------------VENDSDD-----------------------------LATIIYTSGTTGNPKGVMLTHanl 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2171 -SQVINLIEWVNrtylVGPSDRLLFVTSP--SFDLSV-YDVFgmlAAGGSIHIAS----EDDLR--SPERLAAeLGRgti 2240
Cdd:cd17640   114 lHQIRSLSDIVP----PQPGDRFLSILPIwhSYERSAeYFIF---ACGCSQAYTSirtlKDDLKrvKPHYIVS-VPR--- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 tFWDSAPAALQqlvpyfDRIEDGS----QLRLAFLSGDWVPIG------MLDELRRAFP--NVKLVGLGGATEATVwsny 2308
Cdd:cd17640   183 -LWESLYSGIQ------KQVSKSSpikqFLFLFFLSGGIFKFGisgggaLPPHVDTFFEaiGIEVLNGYGLTETSP---- 251

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2309 fevdGIDPRWTSIPY----GRPIQNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepga 2383
Cdd:cd17640   252 ----VVSARRLKCNVrgsvGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------ 321

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 260177242 2384 rlYRTGDLARFFRDGNIEFLGRA-DSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd17640   322 --FNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSP 367
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 1985-2433 3.24e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 84.82  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1985 RERCIHELFESSVERSPGSVALCY-DGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGG 2063
Cdd:PRK12583   16 LTQTIGDAFDATVARFPDREALVVrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2064 AYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLG----------AVEIAARQLG---------IEHVVSLDGDgkDADGN 2124
Cdd:PRK12583   96 ILVNINPAYRASELEYALGQSGVRWVICADAFKTsdyhamlqelLPGLAEGQPGalacerlpeLRGVVSLAPA--PPPGF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2125 VVIHGRRALAD-LADGNLPRAAG------PHNMAYvifTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLfVTS 2197
Cdd:PRK12583  174 LAWHELQARGEtVSREALAERQAsldrddPINIQY---TSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC-VPV 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2198 PsfdlsVYDVFGM-------LAAGGSIHIASED-----DLRSPERLAAELGRGTITFWdsapaaLQQLV-PYFDRIeDGS 2264
Cdd:PRK12583  250 P-----LYHCFGMvlanlgcMTVGACLVYPNEAfdplaTLQAVEEERCTALYGVPTMF------IAELDhPQRGNF-DLS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2265 QLRLAFLSGDWVPIGMLdelRRAFPNVKL--VGLG-GATEATVWSNYFEV-DGIDPRWTSIPYGRPIQNARyyVLDRSGN 2340
Cdd:PRK12583  318 SLRTGIMAGAPCPIEVM---RRVMDEMHMaeVQIAyGMTETSPVSLQTTAaDDLERRVETVGRTQPHLEVK--VVDPDGA 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2341 PCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECG 2420
Cdd:PRK12583  393 TVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW--------MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPR 464

                         490
                  ....*....|...
gi 260177242 2421 EVEVALAQHPGAQ 2433
Cdd:PRK12583  465 EIEEFLFTHPAVA 477
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
2014-2442 4.80e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 83.76  E-value: 4.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRG-LGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRW-PLERVAAVLGTTRPVCIVT 2091
Cdd:PRK06839   28 MTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLtENELIFQLKDSGTTVLFVE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2092 DERHLGAVEIAARqLGIEHVVSLDGDGKDADgnvvihgrRALADLADGNLPRAagphnmaYVI-FTSGSTGTPKGVVerH 2170
Cdd:PRK06839  108 KTFQNMALSMQKV-SYVQRVISITSLKEIED--------RKIDNFVEKNESAS-------FIIcYTSGTTGKPKGAV--L 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2171 SQVINLIEWVNRTYLVG-PSDRLLFVTSPSFDLSVYDVFGM--LAAGGSIHIASEDDLRSPERLAaELGRGTITFwdSAP 2247
Cdd:PRK06839  170 TQENMFWNALNNTFAIDlTMHDRSIVLLPLFHIGGIGLFAFptLFAGGVIIVPRKFEPTKALSMI-EKHKVTVVM--GVP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2248 AALQQLVPYFDRIE-DGSQLRLAFLSGDWVPIGMLDELR-RAFPNVKLVGLGgATEATVwsnyFEVDGIDPRWTSIPYGR 2325
Cdd:PRK06839  247 TIHQALINCSKFETtNLQSVRWFYNGGAPCPEELMREFIdRGFLFGQGFGMT-ETSPTV----FMLSEEDARRKVGSIGK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2326 PIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSgepgarlyrTGDLARFFRDGNIEFLGR 2405
Cdd:PRK06839  322 PVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC---------TGDLARVDEDGFVYIVGR 392

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 260177242 2406 ADSQVKIRGYRIECGEVEVALAQHPGAQRGRGSGGPE 2442
Cdd:PRK06839  393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQH 429
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1064-1495 5.34e-16

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: 83.02  E-value: 5.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1064 MPLTPIQRWFLSG---EPAAPHHFNQAVLL--------ALRDAWvpkhvdaavGAVIRHHDALRLRFVaedgmWRARGMP 1132
Cdd:cd19543     2 YPLSPMQEGMLFHsllDPGSGAYVEQMVITlegpldpdRFRAAW---------QAVVDRHPILRTSFV-----WEGLGEP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1133 -----SGGPVPYEVVDLSELPGEERRAALEARAAE-AQASLDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGI 1206
Cdd:cd19543    68 lqvvlKDRKLPWRELDLSHLSEAEQEAELEALAEEdRERGFDLARAPLMRLTLIRLGDDR-YRLVWSFHHILLDGWSLPI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1207 LLADLATAHRQLVEGEIVRLPsKTTSLR---RWgerlLATVDEvvAAELPFW-EALDGQGVR-PLPRGCEPAEDREGDAQ 1281
Cdd:cd19543   147 LLKELFAIYAALGEGQPPSLP-PVRPYRdyiAW----LQRQDK--EAAEAYWrEYLAGFEEPtPLPKELPADADGSYEPG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1282 TVEVWLGGPETEALLgRVGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREELFPDIEvaRTVGWF-TTIhPVV 1360
Cdd:cd19543   220 EVSFELSAELTARLQ-ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIE--TMVGLFiNTL-PVR 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1361 LPGRP-QSAGARLKAVKEAIRRVPKHGigygilrYLGSDEvVTRLARLPAPE----VAF-NYlgrldralPKDGPFVMAP 1434
Cdd:cd19543   296 VRLDPdQTVLELLKDLQAQQLELREHE-------YVPLYE-IQAWSEGKQALfdhlLVFeNY--------PVDESLEEEQ 359

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242 1435 EAAGPSVSP---RGKRSHALqTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAH 1495
Cdd:cd19543   360 DEDGLRITDvsaEEQTNYPL-TVVAIPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2014-2434 5.37e-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: 83.28  E-value: 5.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRwplervaavlgttrpvcivTDE 2093
Cdd:cd05910     3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG-------------------MGR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHLGAVEIaarqlgiehvvsldgdgkDADGNVVIhgrraladladgNLPRAAGPhnmAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd05910    64 KNLKQCLQ------------------EAEPDAFI------------GIPKADEP---AAILFTSGSTGTPKGVVYRHGTF 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLIEWVNRTYLVGPSDRLLfvtsPSFDLsvydvFGML-AAGGSIHIASEDDLRSPERL-------AAELGRGTITFwdS 2245
Cdd:cd05910   111 AAQIDALRQLYGIRPGEVDL----ATFPL-----FALFgPALGLTSVIPDMDPTRPARAdpqklvgAIRQYGVSIVF--G 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2246 APAALQQLVPYFDRIEDG-SQLRLAFLSGDWVPIGMLDELRRAF-PNVKLVGLGGATEATVWSNyfeVDGIDPRWTSIPY 2323
Cdd:cd05910   180 SPALLERVARYCAQHGITlPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEALPVSS---IGSRELLATTTAA 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2324 ---------GRPIQNARYYVLDRSGNP---------CPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFSGepgaRL 2385
Cdd:cd05910   257 tsggagtcvGRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEG----FW 332

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 260177242 2386 YRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd05910   333 HRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR 381
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 491-900 1.62e-15

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 82.85  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  491 LDAGSNVVSYGELN--RRADKLAHML---------------------RLKGVGT--------ETRVGLCLERSVELVVGI 539
Cdd:PRK07769   17 FPPNTNLVRHVERWakVRGDKLAYRFldfsterdgvardltwsqfgaRNRAVGArlqqvtkpGDRVAILAPQNLDYLIAF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  540 LGVLKAGGAYVPL-DPAYP--SERLAFLAHDAGVQIVLSAAGAEERLGEgpwtVVRldedlGRP-DER------DAAPND 609
Cdd:PRK07769   97 FGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRK----FFR-----ARPaKERprviavDAVPDE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  610 --------NVSAENLAYVMYTSGSTGKPKGVAVTHR----NVVRLV---------RGSSFATFGPDQVFLM--------- 659
Cdd:PRK07769  168 vgatwvppEANEDTIAYLQYTSGSTRIPAGVQITHLnlptNVLQVIdalegqegdRGVSWLPFFHDMGLITvllpallgh 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  660 ----MAPAAFdastfeiwgallhgarlVLFPpesptpeeiGRVVRE-----HGVTTLWLTAPLF---HAvADRGLDQ--- 724
Cdd:PRK07769  248 yitfMSPAAF-----------------VRRP---------GRWIRElarkpGGTGGTFSAAPNFafeHA-AARGLPKdge 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  725 ----LRGVRQLLAGGDVLSPKHVARVL-----LGLPALRLINGYGPTENTTF--TTCHD-------VSRG-MGTGS---V 782
Cdd:PRK07769  301 ppldLSNVKGLLNGSEPVSPASMRKFNeafapYGLPPTAIKPSYGMAEATLFvsTTPMDeeptviyVDRDeLNAGRfveV 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  783 PIGKPIANTHV-----------YLLD-EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERF--------VPDPFSGVP 842
Cdd:PRK07769  381 PADAPNAVAQVsagkvgvsewaVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlSESHAEGAP 460

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242  843 -GARLYRTGDLARYLpNGDMEFLGRRDGQVKIRGFR-----IELAEVEAAllqhPALREAVVIA 900
Cdd:PRK07769  461 dDALWVRTGDYGVYF-DGELYITGRVKDLVIIDGRNhypqdLEYTAQEAT----KALRTGYVAA 519
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 1997-2431 2.01e-15

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: 82.22  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1997 VERSPGSVALCYDGVPP-----LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTG-------GA 2064
Cdd:cd05966    63 LKERGDKVAIIWEGDEPdqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavhsvvfAG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2065 YVPldprwplERVAAVLGTTRPVCIVT-DERHLG------------AVEIAArqlGIEHVVSLDGDGKDADGNvviHGR- 2130
Cdd:cd05966   143 FSA-------ESLADRINDAQCKLVITaDGGYRGgkviplkeivdeALEKCP---SVEKVLVVKRTGGEVPMT---EGRd 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2131 ----RALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVerHSQVinliewvnrTYLVGPSDRLLFVtspsFDLSVYD 2206
Cdd:cd05966   210 lwwhDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVV--HTTG---------GYLLYAATTFKYV----FDYHPDD 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2207 VF-----------------GMLAAGG-SIHIASEDDLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRIE---DGSQ 2265
Cdd:cd05966   275 IYwctadigwitghsyivyGPLANGAtTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVkkhDLSS 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2266 LRLaflsgdwvpIGMldelrrafpnvklVGLGGATEATVWsnYFEVDG------IDPRW---------TSIPY------- 2323
Cdd:cd05966   355 LRV---------LGS-------------VGEPINPEAWMW--YYEVIGkercpiVDTWWqtetggimiTPLPGatplkpg 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2324 --GRPIQNARYYVLDRSGNPCPIGVTGDLyiggtCVSF-------GYYADPsqtaERFVPDPFSGEPGarLYRTGDLARF 2394
Cdd:cd05966   411 saTRPFFGIEPAILDEEGNEVEGEVEGYL-----VIKRpwpgmarTIYGDH----ERYEDTYFSKFPG--YYFTGDGARR 479

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 260177242 2395 FRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05966   480 DEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 614-969 2.40e-15

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 81.79  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  614 ENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRgSSFATFGPDQVFLMMA--PaAFDASTFEIWG--ALLHGARlVLFPPES 689
Cdd:PRK06334  183 EDVAVILFTSGTEKLPKGVPLTHANLLANQR-ACLKFFSPKEDDVMMSflP-PFHAYGFNSCTlfPLLSGVP-VVFAYNP 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 PTPEEIGRVVREHGVTTLWLTAPLFHAV---ADRGLDQLRGVRQLLAGGDVLSPKHVARVLLGLPALRLINGYGPTENTT 766
Cdd:PRK06334  260 LYPKKIVEMIDEAKVTFLGSTPVFFDYIlktAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSP 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  767 FTTCHDVSRGMGTGSVpiGKPIANTHVYLLDEQMN-PVPPNAVGELFTGGDGLARGY-HERPDQTaerfvpdpFSGVPGA 844
Cdd:PRK06334  340 VITINTVNSPKHESCV--GMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYlGEDFGQG--------FVELGGE 409

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  845 RLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQH---PALREAVVIAREDRPGDKRLVAYVVGREAEV 921
Cdd:PRK06334  410 TWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPLVVCGLPGEKVRLCLFTTFPTSI 489

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 260177242  922 PRFSELRKFLlqRLPDHMIPAAVVALDKLPLVPSGKLDRRALPAPTLS 969
Cdd:PRK06334  490 SEVNDILKNS--KTSSILKISYHHQVESIPMLGTGKPDYCSLNALAKS 535
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 481-965 2.48e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 81.65  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  481 EARRVPDAVALDAGSNVVSYGELNRRADKLAHMLR-LKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSE 559
Cdd:PRK07867   12 LPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  560 RLAFLAHDAGVQIVLSAAGAEERLGEGPWTVVRLD------EDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVA 633
Cdd:PRK07867   92 ALARDIAHADCQLVLTESAHAELLDGLDPGVRVINvdspawADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  634 VTHRNVVrlVRGSSFAT---FGPDQVFLMMAPAAFDASTFEIWG-ALLHGARLVL--------FPPEsptpeeigrvVRE 701
Cdd:PRK07867  172 CTHRKVA--SAGVMLAQrfgLGPDDVCYVSMPLFHSNAVMAGWAvALAAGASIALrrkfsasgFLPD----------VRR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  702 HGVTTL-WLTAPLFHAVA-----DRGLDQLRgvrqlLAGGDVLSPKHVARVLLGLpALRLINGYGPTENTTfttchDVSR 775
Cdd:PRK07867  240 YGATYAnYVGKPLSYVLAtperpDDADNPLR-----IVYGNEGAPGDIARFARRF-GCVVVDGFGSTEGGV-----AITR 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  776 GMGTGSVPIGKPIANTHVylLD-EQMNPVPP------------NAVGELF-TGGDGLARGYHERPDQTAERFVpdpfSGV 841
Cdd:PRK07867  309 TPDTPPGALGPLPPGVAI--VDpDTGTECPPaedadgrllnadEAIGELVnTAGPGGFEGYYNDPEADAERMR----GGV 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  842 pgarlYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEV 921
Cdd:PRK07867  383 -----YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAK 457

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 260177242  922 PRFSELRKFLLQR--LPDHMIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK07867  458 FDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 469-866 2.76e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 82.02  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  469 PRERCLHHLFEEEARRVPDAVAL-----DAGS-NVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGV 542
Cdd:PRK12582   46 PYPRSIPHLLAKWAAEAPDRPWLaqrepGHGQwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  543 LKAGGAYVPLDPAYP--SERLAFLAHDAGV---QIVL-------SAAGAEERLGEGPWTVV----------RLDEDLGRP 600
Cdd:PRK12582  126 MQAGVPAAPVSPAYSlmSHDHAKLKHLFDLvkpRVVFaqsgapfARALAALDLLDVTVVHVtgpgegiasiAFADLAATP 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  601 -DERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHR----NVVRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGA 675
Cdd:PRK12582  206 pTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRmmcaNIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNG 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  676 LLHGARLVLFPPESPTPEEIGRVVRE-HGVT-TLWLTAPLFHAVADRGLDQ--------LRGVRQLLAGGDVLSPKHVAR 745
Cdd:PRK12582  286 LLWGGGTLYIDDGKPLPGMFEETIRNlREISpTVYGNVPAGYAMLAEAMEKddalrrsfFKNLRLMAYGGATLSDDLYER 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  746 vllgLPALR---------LINGYGPTENT-TFTTCHDVSRGMGTgsvpIGKPIANTHVYLldeqmnpVPPNAVGELFTGG 815
Cdd:PRK12582  366 ----MQALAvrttghripFYTGYGATETApTTTGTHWDTERVGL----IGLPLPGVELKL-------APVGDKYEVRVKG 430

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  816 DGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYL----PNGDMEFLGR 866
Cdd:PRK12582  431 PNVTPGYHKDPELTAAAFDEEGF--------YRLGDAARFVdpddPEKGLIFDGR 477
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 5-439 2.83e-15

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: 80.43  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    5 LPLSEGQRSLWLAQelAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALR--LVVRPDNEGLVQSLADVSAVDFG 82
Cdd:cd19542     2 YPCTPMQEGMLLSQ--LRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRtvFVESSAEGTFLQVVLKSLDPPIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   83 VTDGsswDEPTAAAWLQAEAARPFDLRAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVaaeFAELCAAdVEGRAAT 162
Cdd:cd19542    80 EVET---DEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPII---LRDLAAA-YNGQLLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  163 LTPisrGFRDYLvwhrDLLASDDASALVREWAAMVGDldvSTPLDLPTDLPRRAQQRYhVRQHFRDLgadlmDRVRESAR 242
Cdd:cd19542   153 PAP---PFSDYI----SYLQSQSQEESLQYWRKYLQG---ASPCAFPSLSPKRPAERS-LSSTRRSL-----AKLEAFCA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  243 AEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRT---RTWQlGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRV 319
Cdd:cd19542   217 SLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpvPGID-DIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  320 TAKLQSVPLSRLAEQCRVPKSPGRMP-LVQavFQEIRSFNEAIRPEGFGHMLRWSRG----PLGFEVEVPselGSQLDLE 394
Cdd:cd19542   296 SLPHQHLSLREIQRALGLWPSGTLFNtLVS--YQNFEASPESELSGSSVFELSAAEDpteyPVAVEVEPS---GDSLKVS 370

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 260177242  395 VrcydffsssvrtcwRYDPDLFLPETVERWADYYAALLRELVGDL 439
Cdd:cd19542   371 L--------------AYSTSVLSEEQAEELLEQFDDILEALLANP 401
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 2033-2431 3.20e-15

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 81.38  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2033 LGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDER------HLGAVEIAARQL 2106
Cdd:PLN02860   52 LGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcsswyeELQNDRLPSLMW 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2107 gieHVVSldgdgkDADGNVVIHG-----------RRALADLadgNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVIn 2175
Cdd:PLN02860  132 ---QVFL------ESPSSSVFIFlnsflttemlkQRALGTT---ELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALI- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2176 lIEWVNRTYLVG-PSDRLLFVTSPSFDLS-VYDVFGMLAAGGSiHI--------ASEDDLRSPErlaaelgrgtITFWDS 2245
Cdd:PLN02860  199 -VQSLAKIAIVGyGEDDVYLHTAPLCHIGgLSSALAMLMVGAC-HVllpkfdakAALQAIKQHN----------VTSMIT 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2246 APAALQQLVPYfDRIEDGSQLRLAFLS----GDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSNYFEVDgiDPRWTSi 2321
Cdd:PLN02860  267 VPAMMADLISL-TRKSMTWKVFPSVRKilngGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLH--DPTLES- 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2322 pygrPIQNARYYVLDRS-----------GNPCP-----IGVTGDLYIG-----GTCVSFGYYADPSQTAERFVPDPFsge 2380
Cdd:PLN02860  343 ----PKQTLQTVNQTKSssvhqpqgvcvGKPAPhvelkIGLDESSRVGriltrGPHVMLGYWGQNSETASVLSNDGW--- 415

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 260177242 2381 pgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PLN02860  416 -----LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
PLN02654 PLN02654
acetate-CoA ligase
 498-963 3.36e-15

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 81.87  E-value: 3.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAA 577
Cdd:PLN02654  121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 GA-------------EERLGEGPWTVVRLD-------------EDLGRPDERDAAPNDNVS------------AENLAYV 619
Cdd:PLN02654  201 AVkrgpktinlkdivDAALDESAKNGVSVGicltyenqlamkrEDTKWQEGRDVWWQDVVPnyptkcevewvdAEDPLFL 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  620 MYTSGSTGKPKGVAVTHRNVVrLVRGSSFA---TFGPDQVFLMMAPAAF-DASTFEIWGALLHGARLVLFP--PESPTPE 693
Cdd:PLN02654  281 LYTSGSTGKPKGVLHTTGGYM-VYTATTFKyafDYKPTDVYWCTADCGWiTGHSYVTYGPMLNGATVLVFEgaPNYPDSG 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  694 EIGRVVREHGVTTLWlTAPLFhavadrgldqlrgVRQLLAGGDVLSPKHVARvllglpALRLINGYG-PTENTTFTTCHD 772
Cdd:PLN02654  360 RCWDIVDKYKVTIFY-TAPTL-------------VRSLMRDGDEYVTRHSRK------SLRVLGSVGePINPSAWRWFFN 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  773 VsrgMGTGSVPIG----------------------KPIANTHVY------LLDEQMNPVPPNAVGELFTGGD--GLAR-- 820
Cdd:PLN02654  420 V---VGDSRCPISdtwwqtetggfmitplpgawpqKPGSATFPFfgvqpvIVDEKGKEIEGECSGYLCVKKSwpGAFRtl 496

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  821 -GYHERPDQTAERfvpdPFSGvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVI 899
Cdd:PLN02654  497 yGDHERYETTYFK----PFAG-----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVV 567

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  900 AREDRPGDKRLVAYVVGREAeVPRFSELRKFLLQRLPDHMipAAVVALDK------LPLVPSGKLDRRAL 963
Cdd:PLN02654  568 GIEHEVKGQGIYAFVTLVEG-VPYSEELRKSLILTVRNQI--GAFAAPDKihwapgLPKTRSGKIMRRIL 634
PRK08315 PRK08315
AMP-binding domain protein; Validated
 465-957 6.65e-15

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 80.63  E-value: 6.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  465 ASDYP-RERCLHHLFEEEARRVPDAVAL-DAGSNV-VSYGELNRRADKLA-HMLRLkGVGTETRVGLCLERSVELVVGIL 540
Cdd:PRK08315    8 PTDVPlLEQTIGQLLDRTAARYPDREALvYRDQGLrWTYREFNEEVDALAkGLLAL-GIEKGDRVGIWAPNVPEWVLTQF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  541 GVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAG-------------------------AEERLgegPW--TVVRL 593
Cdd:PRK08315   87 ATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelapelatcepgqlQSARL---PElrRVIFL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  594 DED-------------LGR--PDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV-------RLVRgssfatF 651
Cdd:PRK08315  164 GDEkhpgmlnfdellaLGRavDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngyfigEAMK------L 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  652 GP-DQV---------FLM-MAPAAfdastfeiwgALLHGARLVlFPPESPTPEEIGRVVRE------HGVTTLW---LTA 711
Cdd:PRK08315  238 TEeDRLcipvplyhcFGMvLGNLA----------CVTHGATMV-YPGEGFDPLATLAAVEEerctalYGVPTMFiaeLDH 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  712 PLFhavADRGLDQLR-GVrqlLAGG--------DVLSPKHVARVLLGlpalrlingYGPTEN---TTFTTCHD-VSRGMG 778
Cdd:PRK08315  307 PDF---ARFDLSSLRtGI---MAGSpcpievmkRVIDKMHMSEVTIA---------YGMTETspvSTQTRTDDpLEKRVT 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  779 TgsvpIGKPIANTHVYLLDEQMN-PVPPNAVGELFTGGDGLARGYHERPDQTAErfVPDPfsgvpgARLYRTGDLARYLP 857
Cdd:PRK08315  372 T----VGRALPHLEVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDA------DGWMHTGDLAVMDE 439

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  858 NGDMEFLGRrdgqVK---IRGFR-IELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQ 933
Cdd:PRK08315  440 EGYVNIVGR----IKdmiIRGGEnIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRG 515

                         570       580
                  ....*....|....*....|....
gi 260177242  934 RLPDHMIPAAVVALDKLPLVPSGK 957
Cdd:PRK08315  516 KIAHYKIPRYIRFVDEFPMTVTGK 539
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 2015-2431 9.85e-15

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: 79.60  E-value: 9.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDER 2094
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2095 HLGAVEIAARQLG-IEHVVSLDgdgkDADGNVVIHGRRALA--DLADGNLPRAAGP---HNMAYVI-FTSGSTGTPKGVV 2167
Cdd:cd12119   107 FLPLLEAIAPRLPtVEHVVVMT----DDAAMPEPAGVGVLAyeELLAAESPEYDWPdfdENTAAAIcYTSGTTGNPKGVV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2168 ERHSQVI--NLIEWVNRTYLVGPSDRLLFVTsPSFDLSVYDV-FGMLAAGGSIHIASEDDlrSPERLAAELGRGTITFWD 2244
Cdd:cd12119   183 YSHRSLVlhAMAALLTDGLGLSESDVVLPVV-PMFHVNAWGLpYAAAMVGAKLVLPGPYL--DPASLAELIEREGVTFAA 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2245 SAPAALQQLVPYFDRIE-DGSQLRLAFLSGDWVPIGMLDELRRAFpnVKLVGLGGATEA----------TVWSNYFEVDG 2313
Cdd:cd12119   260 GVPTVWQGLLDHLEANGrDLSSLRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGMTETsplgtvarppSEHSNLSEDEQ 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2314 IDPRWTSipyGRPIQNARYYVLDRSGNPCPI-GVT-GDLYIGGTCVSFGYYADPsQTAERFVPDPFsgepgarlYRTGDL 2391
Cdd:cd12119   338 LALRAKQ---GRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKND-EESEALTEDGW--------LRTGDV 405

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 260177242 2392 ARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd12119   406 ATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPA 445
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 482-935 1.70e-14

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 78.76  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERL 561
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  562 AFLAHDAGVQIVLSAAgaeerlGEGPWTVVRLDedlgRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRN--- 638
Cdd:PRK09029   93 EELLPSLTLDFALVLE------GENTFSALTSL----HLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhla 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  639 ----VVRLVRgssfatFGPDQVFLMMAPaAFDASTFEI-WGALLHGARLvlfppesptpeeigrVVREHGvttlwltaPL 713
Cdd:PRK09029  163 saegVLSLMP------FTAQDSWLLSLP-LFHVSGQGIvWRWLYAGATL---------------VVRDKQ--------PL 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  714 FHAVAD------------RGLDQLRgvrqllaggDVLSPKHvarVLLG---LPA----------LRLINGYGPTENTTfT 768
Cdd:PRK09029  213 EQALAGcthaslvptqlwRLLDNRS---------EPLSLKA---VLLGgaaIPVelteqaeqqgIRCWCGYGLTEMAS-T 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TChdVSRGMGTGSVpiGKPIANTHVYLLDeqmnpvppnavGELFTGGDGLARGY-HERpdqtaeRFVPdpfsgvpgarL- 846
Cdd:PRK09029  280 VC--AKRADGLAGV--GSPLPGREVKLVD-----------GEIWLRGASLALGYwRQG------QLVP----------Lv 328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  847 -----YRTGDLARyLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAyVVGREAEV 921
Cdd:PRK09029  329 ndegwFATRDRGE-WQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVESDSEA 406

                         490
                  ....*....|....
gi 260177242  922 PRfSELRKFLLQRL 935
Cdd:PRK09029  407 AV-VNLAEWLQDKL 419
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 499-899 1.86e-14

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: 79.05  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  499 SYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSA-- 576
Cdd:cd05932     8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGkl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  577 ---AGAEERLGEGPWTVVRLDEDLGR------------PDERDAAPNDnvsAENLAYVMYTSGSTGKPKGVAVTHRNVV- 640
Cdd:cd05932    88 ddwKAMAPGVPEGLISISLPPPSAANcqyqwddliaqhPPLEERPTRF---PEQLATLIYTSGTTGQPKGVMLTFGSFAw 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  641 RLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPT-PEEIGR--------VVR-----EHGVTT 706
Cdd:cd05932   165 AAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTfVEDVQRarptlffsVPRlwtkfQQGVQD 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  707 --------LWLTAPLFHAVADR------GLDQlrgVRQLLAGGDVLSPK--HVARVlLGLPalrLINGYGPTENTTFTT- 769
Cdd:cd05932   245 kipqqklnLLLKIPVVNSLVKRkvlkglGLDQ---CRLAGCGSAPVPPAllEWYRS-LGLN---ILEAYGMTENFAYSHl 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  770 CHDVSRGMGTgsvpIGKPIANTHVYLLDEqmnpvppnavGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRT 849
Cdd:cd05932   318 NYPGRDKIGT----VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF--------LRT 375

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 260177242  850 GDLARYLPNGDMEFLGRRDGQVKI-RGFRIELAEVEAALLQHPALREAVVI 899
Cdd:cd05932   376 GDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 525-965 1.90e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 78.92  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  525 VGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAGAEERL-GEGPWTVVRLDEDLGR---- 599
Cdd:PRK13388   55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLdGLDLPGVRVLDVDTPAyael 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  600 -PDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRgSSFATFG--PDQVFLMMAPAAFDASTFEIWG-A 675
Cdd:PRK13388  135 vAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGR-ALTERFGltRDDVCYVSMPLFHSNAVMAGWApA 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  676 LLHGARLVLFPPESPT---PEeigrvVREHGVTTL-WLTAPLFHAVA-----DRGLDQLRgvrqlLAGGDVLSPKHVARV 746
Cdd:PRK13388  214 VASGAAVALPAKFSASgflDD-----VRRYGATYFnYVGKPLAYILAtperpDDADNPLR-----VAFGNEASPRDIAEF 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  747 LLGLPAlRLINGYGPTENTTFttchdVSRGMGTGSVPIGKPIANTHVYLLDE-QMNPV-----------PPNAVGELF-T 813
Cdd:PRK13388  284 SRRFGC-QVEDGYGSSEGAVI-----VVREPGTPPGSIGRGAPGVAIYNPETlTECAVarfdahgallnADEAIGELVnT 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  814 GGDGLARGYHERPDQTAERFvpdpfsgvpgaR--LYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHP 891
Cdd:PRK13388  358 AGAGFFEGYYNNPEATAERM-----------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHP 426

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  892 ALREAVVIARED-RPGDKRLVAYVVGREAevpRFS--ELRKFLL--QRLPDHMIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK13388  427 AINRVAVYAVPDeRVGDQVMAALVLRDGA---TFDpdAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 6-331 2.78e-14

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: 77.74  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    6 PLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALR--LVVRPDNEGLvQSLADVSAVDFGV 83
Cdd:cd19547     3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRtgFTWRDRAEPL-QYVRDDLAPPWAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDgssWDEPTAAAWLQAEAARPFDLRAGAL--------RVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAAD 155
Cdd:cd19547    82 LD---WSGEDPDRRAELLERLLADDRAAGLsladcplyRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  156 VEGRAATLTPIsRGFRDYLVWHRDLLASDDASAlvREWAAMVGDLDVSTPLDLPTDlprrAQQRYHVRQHfrDLGADLMD 235
Cdd:cd19547   159 AHGREPQLSPC-RPYRDYVRWIRARTAQSEESE--RFWREYLRDLTPSPFSTAPAD----REGEFDTVVH--EFPEQLTR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  236 RVRESARAEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRtwQLGVVGHMAGI----VPVPARIDAAATPRAIIR 311
Cdd:cd19547   230 LVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPP--ELEGSEHMVGIfintIPLRIRLDPDQTVTGLLE 307

                         330       340
                  ....*....|....*....|
gi 260177242  312 ELRNALRVTAKLQSVPLSRL 331
Cdd:cd19547   308 TIHRDLATTAAHGHVPLAQI 327
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 2013-2430 2.82e-14

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: 77.87  E-value: 2.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2013 PLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTD 2092
Cdd:cd05914     7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ErhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraladladgnlpraagPHNMAYVIFTSGSTGTPKGVVERHSQ 2172
Cdd:cd05914    87 D-----------------------------------------------------EDDVALINYTSGTTGNSKGVMLTYRN 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2173 VINLIEWVNRTYLVGPSDRLLFVtspsfdLSVYDVFGM-----LAAGGSIHIASEDDLRSPERLAAELGRGTITFWDSAP 2247
Cdd:cd05914   114 IVSNVDGVKEVVLLGKGDKILSI------LPLHHIYPLtftllLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGVPVP 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2248 AALqqlvpyFDRIEDGSQLRLAFLSGDW---VPIGMLDELRRAFP--------NVKLVGLGGATEATVWSNYFEVDGI-- 2314
Cdd:cd05914   188 LVI------EKIFKMDIIPKLTLKKFKFklaKKINNRKIRKLAFKkvheafggNIKEFVIGGAKINPDVEEFLRTIGFpy 261

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2315 ---------DPRWTSIPYGRPIQNARYYVLD----RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgep 2381
Cdd:cd05914   262 tigygmtetAPIISYSPPNRIRLGSAGKVIDgvevRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW---- 337

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242 2382 garlYRTGDLARFFRDGNIEFLGRADSQ-VKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05914   338 ----FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMP 383
PRK09274 PRK09274
peptide synthase; Provisional
 2002-2434 3.61e-14

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 78.02  E-value: 3.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2002 GSVALCYDgvpPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVL 2081
Cdd:PRK09274   33 ADGKLAYD---ELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2082 GTTRP-VCIVTDERHLgaveiaARQL------GIEHVVSLDGdgKDADGNVVIhgRRALADLADGNLP-RAAGPHNMAYV 2153
Cdd:PRK09274  110 AEAQPdAFIGIPKAHL------ARRLfgwgkpSVRRLVTVGG--RLLWGGTTL--ATLLRDGAAAPFPmADLAPDDMAAI 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2154 IFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLfVTSPSFDLsvydvFGMLAAGGSI-------HIASEDdlr 2226
Cdd:PRK09274  180 LFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL-PTFPLFAL-----FGPALGMTSVipdmdptRPATVD--- 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2227 sPERLAAELGRGTITFWDSAPAALQQLVPYfdRIEDGSQL---RLAFLSGDWVPIGMLDELRRAFPN-VKLVGLGGATEA 2302
Cdd:PRK09274  251 -PAKLFAAIERYGVTNLFGSPALLERLGRY--GEANGIKLpslRRVISAGAPVPIAVIERFRAMLPPdAEILTPYGATEA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2303 ----TVWSNyfEV-DGIDPRWTS---IPYGRPIQNARYYVLDRSGNP---------CPIGVTGDLYIGGTCVSFGYYADP 2365
Cdd:PRK09274  328 lpisSIESR--EIlFATRAATDNgagICVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVAGPMVTRSYYNRP 405

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2366 SQTAERFVPDpfsGEPGARlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:PRK09274  406 EATRLAKIPD---GQGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKR 470
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 882-957 3.64e-14

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: 69.50  E-value: 3.64e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242   882 EVEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGK 957
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1063-1227 3.74e-14

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: 77.40  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1063 EMPLTPIQR--WFLS-GEPAAPHhFNQAVLLALRDAWvpkHVDA---AVGAVIRHHDALRLRFVAEDGMWRARGMPSGgP 1136
Cdd:cd19531     1 PLPLSFAQQrlWFLDqLEPGSAA-YNIPGALRLRGPL---DVAAlerALNELVARHEALRTTFVEVDGEPVQVILPPL-P 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1137 VPYEVVDLSELPGEERRAALEAR-AAEAQASLDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAH 1215
Cdd:cd19531    76 LPLPVVDLSGLPEAEREAEAQRLaREEARRPFDLARGPLLRATLLRLGEDE-HVLLLTMHHIVSDGWSMGVLLRELAALY 154

                         170
                  ....*....|..
gi 260177242 1216 RQLVEGEIVRLP 1227
Cdd:cd19531   155 AAFLAGRPSPLP 166
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 498-962 7.72e-14

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 76.96  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQI----- 572
Cdd:PRK07768   30 HTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIgmiga 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  573 ---VLSAA--GAEERLGEGPWTVVRLDEDLGRpderDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGss 647
Cdd:PRK07768  110 kavVVGEPflAAAPVLEEKGIRVLTVADLLAA----DPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEA-- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  648 fatfgpdqvflMMAPAAFDASTFEI--WGALLH--------------GARLVLFPP----ESPT--PEEIGrvvREHGVT 705
Cdd:PRK07768  184 -----------MFVAAEFDVETDVMvsWLPLFHdmgmvgfltvpmyfGAELVKVTPmdflRDPLlwAELIS---KYRGTM 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  706 TLW------LTAPLFHAVADRGLDQLRGVRQLLAGGDVLSPKHVARVL-----LGLPALRLINGYGPTENTTFTTCHDVS 774
Cdd:PRK07768  250 TAApnfayaLLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLdagarFGLRPEAILPAYGMAEATLAVSFSPCG 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  775 RGMGTGSV-----------------------PIGKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGLARGYherpdQTAE 831
Cdd:PRK07768  330 AGLVVDEVdadllaalrravpatkgntrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMD 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  832 RFVPdpfsGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIA-REDRPGDKRL 910
Cdd:PRK07768  405 GFIP----AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAvRLDAGHSREG 480

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260177242  911 VAYVV-----GREAEVPRfseLRKFLLQRLPDH--MIPAAVVALDK--LPLVPSGKLDRRA 962
Cdd:PRK07768  481 FAVAVesnafEDPAEVRR---IRHQVAHEVVAEvgVRPRNVVVLGPgsIPKTPSGKLRRAN 538
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 2014-2430 1.21e-13

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 76.69  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHLGA-VEIAARQLGIEHVVSLDGDGKDAD------GNVVIHGRRALADLADGN--LPRAAGPHNMAYVIFTSGSTGTPK 2164
Cdd:PLN02387  187 KQLKKlIDISSQLETVKRVIYMDDEGVDSDsslsgsSNWTVSSFSEVEKLGKENpvDPDLPSPNDIAVIMYTSGSTGLPK 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2165 GVVERHSQVINLIEWVnRTYL--VGPSDRLL--FVTSPSFDLSVYDVfgMLAAGGSIHIASEDDLRSperLAAELGRGTI 2240
Cdd:PLN02387  267 GVMMTHGNIVATVAGV-MTVVpkLGKNDVYLayLPLAHILELAAESV--MAAVGAAIGYGSPLTLTD---TSNKIKKGTK 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2241 --------TFWDSAPAALqqlvpyfDRIEDG------------SQL-------RLAFLSGDWVPIGMLDEL---RRAFPN 2290
Cdd:PLN02387  341 gdasalkpTLMTAVPAIL-------DRVRDGvrkkvdakgglaKKLfdiaykrRLAAIEGSWFGAWGLEKLlwdALVFKK 413

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2291 VKLVgLGGATEatvwsnyFEVDGIDP------RWTSIPYGRPIQNAryYVLD-----------------RSGNPCPIGVT 2347
Cdd:PLN02387  414 IRAV-LGGRIR-------FMLSGGAPlsgdtqRFINICLGAPIGQG--YGLTetcagatfsewddtsvgRVGPPLPCCYV 483

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2348 -------------------GDLYIGGTCVSFGYYADPSQTAERFVPDpfsgEPGARLYRTGDLARFFRDGNIEFLGRADS 2408
Cdd:PLN02387  484 klvsweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVD----ERGMRWFYTGDIGQFHPDGCLEIIDRKKD 559

                         490       500
                  ....*....|....*....|...
gi 260177242 2409 QVKIR-GYRIECGEVEVALAQHP 2430
Cdd:PLN02387  560 IVKLQhGEYVSLGKVEAALSVSP 582
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 498-936 1.26e-13

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: 76.34  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  498 VSYGELNRRADKLAHMLRLKG-VGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLA---------FLAHD 567
Cdd:cd17632    68 ITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLApilaeteprLLAVS 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  568 A-----GVQIVLSA----------------------AGAEERLGEGPWTVVRLDEDLGRPDERDAAPND--NVSAENLAY 618
Cdd:cd17632   148 AehldlAVEAVLEGgtpprlvvfdhrpevdahraalESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFrpEPDDDPLAL 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNVVRLVRGsSFATFGPDQ---VFLMMAPAAFDASTFEIWGALLHGArLVLFPPESPT---- 691
Cdd:cd17632   228 LIYTSGSTGTPKGAMYTERLVATFWLK-VSSIQDIRPpasITLNFMPMSHIAGRISLYGTLARGG-TAYFAAASDMstlf 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  692 -------PEEIGRVVR-------EHGVTTLWLTAPLFHAVADRG------LDQLRGVRQLLA--GGDVLSPKHVARV--L 747
Cdd:cd17632   306 ddlalvrPTELFLVPRvcdmlfqRYQAELDRRSVAGADAETLAErvkaelRERVLGGRLLAAvcGSAPLSAEMKAFMesL 385

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  748 LGLPalrLINGYGPTEnttfttchdvsrgmgTGSVPIGKPIANTHVylLDEQMNPVP---------PNAVGELFTGGDGL 818
Cdd:cd17632   386 LDLD---LHDGYGSTE---------------AGAVILDGVIVRPPV--LDYKLVDVPelgyfrtdrPHPRGELLVKTDTL 445

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  819 ARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKI-RGFRIELAEVEAALLQHPALRE-- 895
Cdd:cd17632   446 FPGYYKRPEVTAEVFDEDGF--------YRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQif 517

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260177242  896 -----------AVVIARED---RPGDKRLVAYV------VGREAEVPRFSELRKFLLQRLP 936
Cdd:cd17632   518 vygnserayllAVVVPTQDalaGEDTARLRAALaeslqrIAREAGLQSYEIPRDFLIETEP 578
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 482-958 1.44e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 75.82  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPD--AVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSE 559
Cdd:PRK13390    7 AQIAPDrpAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  560 RLAFLAHDAGVQIVLSAAGAEERLGE-GPWTVVRLD-----EDLGRPDERDAAPNDNVSAENLAYVM-YTSGSTGKPKGV 632
Cdd:PRK13390   87 EADYIVGDSGARVLVASAALDGLAAKvGADLPLRLSfggeiDGFGSFEAALAGAGPRLTEQPCGAVMlYSSGTTGFPKGI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  633 A--VTHRNV-------VRLVRGssFATFGPDQVFLMMAPAaFDASTFEiWGALLH--GARLVLfpPESPTPEEIGRVVRE 701
Cdd:PRK13390  167 QpdLPGRDVdapgdpiVAIARA--FYDISESDIYYSSAPI-YHAAPLR-WCSMVHalGGTVVL--AKRFDAQATLGHVER 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  702 HGVTTLWLTAPLFhavadrgldqlrgVRQLLAGGDVlspkhvaRVLLGLPALR----------------LINGYGPT--E 763
Cdd:PRK13390  241 YRITVTQMVPTMF-------------VRLLKLDADV-------RTRYDVSSLRavihaaapcpvdvkhaMIDWLGPIvyE 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  764 NTTFTTCHdvsrGMGTGSVP--------IGKPIANThVYLLDEQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVP 835
Cdd:PRK13390  301 YYSSTEAH----GMTFIDSPdwlahpgsVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHP 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  836 -DPFsgvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIARED-RPGDK----- 908
Cdd:PRK13390  376 aHPF-------WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpEMGEQvkavi 448

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242  909 RLVAYVVGREaEVPRfsELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKL 958
Cdd:PRK13390  449 QLVEGIRGSD-ELAR--ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 2149-2431 2.16e-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: 73.59  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2149 NMAYVIFTSGSTGTPKGVVERHSQVINLIEwVNRTYLVGPSDRLLFVTSP-SFDLSVYDVFGMLAAGGSIHIASEDDLRS 2227
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFV-CNEDLFNISGEDAILAPGPlSHSLFLYGAISALYLGGTFIGQRKFNPKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 PERLaaeLGRGTITFWDSAPAALQQLVPYfDRIEdgSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVWSn 2307
Cdd:cd17633    80 WIRK---INQYNATVIYLVPTMLQALART-LEPE--SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFIT- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2308 YFEVDGIDPRWTSipyGRPIQNARYYVLDRSGnpcpiGVTGDLYIGGTCVSFGYYADPSQTAERFvpdpfsgepgarlYR 2387
Cdd:cd17633   153 YNFNQESRPPNSV---GRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-------------MS 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 260177242 2388 TGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17633   212 VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPG 255
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 467-867 4.09e-13

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 75.14  E-value: 4.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  467 DYPRERCLHHLFEEEARRVPDAVALdaGSNV-----------VSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVEL 535
Cdd:PLN02736   39 DHPEIGTLHDNFVYAVETFRDYKYL--GTRIrvdgtvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEW 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  536 VVgilgVLKAGGAY----VPL-----------------------DPAYPSERLAFLAHDAGVQIVLSAAGAEERLGEGPW 588
Cdd:PLN02736  117 LI----VDHACSAYsyvsVPLydtlgpdavkfivnhaevaaifcVPQTLNTLLSCLSEIPSVRLIVVVGGADEPLPSLPS 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  589 T----VVRLD--EDLGRPDERDAAPNDNvsaENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVFLMMA 661
Cdd:PLN02736  193 GtgveIVTYSklLAQGRSSPQPFRPPKP---EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTkFYPSDVHISYL 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  662 PAAFDASTFEIWGALLHGARLVLFPPE-----------SPT-----PEEIGRV-------VREHGVttlwLTAPLFHA-- 716
Cdd:PLN02736  270 PLAHIYERVNQIVMLHYGVAVGFYQGDnlklmddlaalRPTifcsvPRLYNRIydgitnaVKESGG----LKERLFNAay 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  717 --------------------VADRGLDQLRG-VRQLLAGGDVLSPK--HVARVLLGlpaLRLINGYGPTENT-TFTTCHD 772
Cdd:PLN02736  346 nakkqalengknpspmwdrlVFNKIKAKLGGrVRFMSSGASPLSPDvmEFLRICFG---GRVLEGYGMTETScVISGMDE 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  773 VSRGMGTgsvpIGKPIANTHVYLLD-EQMN------PVPPnavGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgar 845
Cdd:PLN02736  423 GDNLSGH----VGSPNPACEVKLVDvPEMNytsedqPYPR---GEICVRGPIIFKGYYKDEVQTREVIDEDGW------- 488

                         490       500
                  ....*....|....*....|..
gi 260177242  846 lYRTGDLARYLPNGDMEFLGRR 867
Cdd:PLN02736  489 -LHTGDIGLWLPGGRLKIIDRK 509
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 621-963 4.32e-13

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 74.67  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  621 YTSGSTGKPKGVAVTHR----NVVRLVRGSSFATFgpdQVFLMMAPAAFDASTFEIWGALLHGARLVLFppESPTPEEIG 696
Cdd:PLN03102  193 YTSGTTADPKGVVISHRgaylSTLSAIIGWEMGTC---PVYLWTLPMFHCNGWTFTWGTAARGGTSVCM--RHVTAPEIY 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  697 RVVREHGVTTLWLTAPLFHAVAD-RGLDQ--LRGVRQLLAGGDvlSP-----KHVARVllglpALRLINGYGPTENT--- 765
Cdd:PLN03102  268 KNIEMHNVTHMCCVPTVFNILLKgNSLDLspRSGPVHVLTGGS--PPpaalvKKVQRL-----GFQVMHAYGLTEATgpv 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  766 TFTTCHDV-SRGMGTGSVPIGKPIANTHVYLLD------EQMNPVPPNA--VGELFTGGDGLARGYHERPDQTAERFVPD 836
Cdd:PLN03102  341 LFCEWQDEwNRLPENQQMELKARQGVSILGLADvdvknkETQESVPRDGktMGEIVIKGSSIMKGYLKNPKATSEAFKHG 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  837 PFSgvpgarlyrTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYVVG 916
Cdd:PLN03102  421 WLN---------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL 491

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  917 REAE----------VPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:PLN03102  492 EKGEttkedrvdklVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 466-866 5.14e-13

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 74.53  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  466 SDYPRerCLHHLFEEEARRVPDAVAL-----DAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGIL 540
Cdd:PRK08180   35 GDYPR--RLTDRLVHWAQEAPDRVFLaergaDGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLAL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  541 GVLKAGGAYVPLDPAY--PSERLAFLAH--------------------------DAGVQIVLSAAGAEERlgegpwTVVR 592
Cdd:PRK08180  113 AAMYAGVPYAPVSPAYslVSQDFGKLRHvlelltpglvfaddgaafaralaavvPADVEVVAVRGAVPGR------AATP 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  593 LDEDLGRPDERDAAP-NDNVSAENLAYVMYTSGSTGKPKGVAVTHRN--VVRLVRGSSFATFGPDQ-VFLMMAP--AAFD 666
Cdd:PRK08180  187 FAALLATPPTAAVDAaHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMlcANQQMLAQTFPFLAEEPpVLVDWLPwnHTFG 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  667 AS-TFEIwgALLHGARLVLfPPESPTPEEIGRVVR--EHGVTTLWLTAPL-FHAVAD--RGLDQLR-----GVRQLLAGG 735
Cdd:PRK08180  267 GNhNLGI--VLYNGGTLYI-DDGKPTPGGFDETLRnlREISPTVYFNVPKgWEMLVPalERDAALRrrffsRLKLLFYAG 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  736 DVLSP------KHVARVLLGLPaLRLINGYGPTENT-TFTTCHDVSRGMGtgsvPIGKPIANTHVYLldeqmnpVPPNAV 808
Cdd:PRK08180  344 AALSQdvwdrlDRVAEATCGER-IRMMTGLGMTETApSATFTTGPLSRAG----NIGLPAPGCEVKL-------VPVGGK 411

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242  809 GELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDME----FLGR 866
Cdd:PRK08180  412 LEVRVKGPNVTPGYWRAPELTAEAFDEEGY--------YRSGDAVRFVDPADPErglmFDGR 465
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 2014-2431 6.95e-13

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: 74.27  E-value: 6.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTG-------GAYVP------LDPRWPLERVAAV 2080
Cdd:cd05967    83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAAkelasrIDDAKPKLIVTAS 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2081 LGTT--RPVCIVT--DErhlgAVEIAARQlgIEHVVSLDGDGKDADgnVVIHGRralaDLADGNLPRAAGPHNMA----- 2151
Cdd:cd05967   163 CGIEpgKVVPYKPllDK----ALELSGHK--PHHVLVLNRPQVPAD--LTKPGR----DLDWSELLAKAEPVDCVpvaat 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2152 ---YVIFTSGSTGTPKGVVERHSQVINLIEWVNRT-YLVGPSDrLLFVTSpsfDLS-----VYDVFGMLAAGGSIHIASE 2222
Cdd:cd05967   231 dplYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNiYGIKPGD-VWWAAS---DVGwvvghSYIVYGPLLHGATTVLYEG 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2223 DDLRSPE-----RLAAELGRGTItFwdSAPAALQQLV---PYFDRIE--DGSQLRLAFLSGDWVPIGMLDELRRAFpNVK 2292
Cdd:cd05967   307 KPVGTPDpgafwRVIEKYQVNAL-F--TAPTAIRAIRkedPDGKYIKkyDLSSLRTLFLAGERLDPPTLEWAENTL-GVP 382

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2293 LVGLGGATEaTVW---SNYFEVDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGG----TCVSfGYYADP 2365
Cdd:cd05967   383 VIDHWWQTE-TGWpitANPVGLEPLPIKAGSP--GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLplppGCLL-TLWKND 458

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 2366 sqtaERFVPDPFSGEPGarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05967   459 ----ERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPA 518
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 2151-2434 1.16e-12

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: 71.59  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 AYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLfVTSPSFDLS-VYDVFGMLAAGGSIHIASEDDLrspe 2229
Cdd:cd17630     3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGgLAILVRSLLAGAELVLLERNQA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 rLAAELGRGTITFWDSAPAALQQLVPYFDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGlgGATEA----TVW 2305
Cdd:cd17630    78 -LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTY--GMTETasqvATK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2306 SNYFEVDGIDprwtsipyGRPIQNARYYVLDRsgnpcpigvtGDLYIGGTCVSFGYYADPSqtaerfvPDPFSGEPgarL 2385
Cdd:cd17630   155 RPDGFGRGGV--------GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQL-------VPEFNEDG---W 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 260177242 2386 YRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:cd17630   207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD 255
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 2015-2433 1.17e-12

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 73.09  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDER 2094
Cdd:PLN02330   57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2095 HLGAVE------IAARQLGIEHVVSLDG--DGKDADGNVVIHGRRALADLAdgNLPraagphnmayviFTSGSTGTPKGV 2166
Cdd:PLN02330  137 NYGKVKglglpvIVLGEEKIEGAVNWKEllEAADRAGDTSDNEEILQTDLC--ALP------------FSSGTTGISKGV 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2167 VERHSQVI-NLiewVNRTYLVGPSDRLLFVT---SPSFdlSVYDVFGMLAA----GGSIHIASEDDLRSperLAAELGRG 2238
Cdd:PLN02330  203 MLTHRNLVaNL---CSSLFSVGPEMIGQVVTlglIPFF--HIYGITGICCAtlrnKGKVVVMSRFELRT---FLNALITQ 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2239 TITFWDSAPAALQQLV--PYFDRIeDGSQLRLAFLSGDWVPIG--MLDELRRAFPNVKLVGLGGATEATVWS----NYFE 2310
Cdd:PLN02330  275 EVSFAPIVPPIILNLVknPIVEEF-DLSKLKLQAIMTAAAPLApeLLTAFEAKFPGVQVQEAYGLTEHSCITlthgDPEK 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2311 VDGIDPRwTSIPYGRPIQNARYYVLDrSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGD 2390
Cdd:PLN02330  354 GHGIAKK-NSVGFILPNLEVKFIDPD-TGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW--------LHTGD 423

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 260177242 2391 LARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:PLN02330  424 IGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE 466
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
491-973 1.61e-12

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 72.89  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  491 LDAGSNVVSYGELNRRADKLAHMLR-LKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAG 569
Cdd:PRK05620   32 GGAEQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  570 VQIVLSAAGAEERLGE------GPWTVVRLDEDLGRPDERDAAPN----------DNVSAE---------NLAYVMYTSG 624
Cdd:PRK05620  112 DEVIVADPRLAEQLGEilkecpCVRAVVFIGPSDADSAAAHMPEGikvysyeallDGRSTVydwpeldetTAAAICYSTG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  625 STGKPKGVAVTHRNV----VRLVRGSSFATFGpDQVFLMMAPAAFDAStfeiWG----ALLHGARLVlFPPESPTPEEIG 696
Cdd:PRK05620  192 TTGAPKGVVYSHRSLylqsLSLRTTDSLAVTH-GESFLCCVPIYHVLS----WGvplaAFMSGTPLV-FPGPDLSAPTLA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  697 RVVRE------HGVTTLWLTAPLFHAvadRGLDQLRGVRQLLAGGDVLSPkhvarVLLGLPALR----LINGYGPTENTT 766
Cdd:PRK05620  266 KIIATamprvaHGVPTLWIQLMVHYL---KNPPERMSLQEIYVGGSAVPP-----ILIKAWEERygvdVVHVWGMTETSP 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  767 FTTchdVSRG-------------MGTGSVPIGKP--IANThvyllDEQMNPVPPNAvGELFTGGDGLARGYHERPDQT-- 829
Cdd:PRK05620  338 VGT---VARPpsgvsgearwayrVSQGRFPASLEyrIVND-----GQVMESTDRNE-GEIQVRGNWVTASYYHSPTEEgg 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  830 --AERF----VPDPFSGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIARED 903
Cdd:PRK05620  409 gaASTFrgedVEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPD 488

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  904 RPGDKRLVAYVV---GREAEVPRFSELRKFLLQRLPDHMIP-----------AAVVALDKLPL---VPSGKLDRRALPAP 966
Cdd:PRK05620  489 DKWGERPLAVTVlapGIEPTRETAERLRDQLRDRLPNWMLPeywtfvdeidkTSVGKFDKKDLrqhLADGDFEIIKLKGP 568


                  ....*..
gi 260177242  967 TLSGRSG 973
Cdd:PRK05620  569 GESGESD 575
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 2147-2435 1.79e-12

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: 72.36  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2147 PHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSP--SFDLSVYDVFGMLAAGGSIHIASEDD 2224
Cdd:cd05909   146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTGCLWLPLLSGIKVVFHPNPLD 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2225 LRSPERLAAELGrgtITFWDSAPAALQQlvpYFDRI--EDGSQLRLAFLSGDWVPigmlDELRRAFPN---VKLVGLGGA 2299
Cdd:cd05909   226 YKKIPELIYDKK---ATILLGTPTFLRG---YARAAhpEDFSSLRLVVAGAEKLK----DTLRQEFQEkfgIRILEGYGT 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2300 TEAT-VWSnyFEVDGIDPRWTSIpyGRPIQNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAErfvpdpf 2377
Cdd:cd05909   296 TECSpVIS--VNTPQSPNKEGTV--GRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF------- 364

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 2378 sgEPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQRG 2435
Cdd:cd05909   365 --AFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNE 420
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 2053-2431 2.09e-12

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 72.57  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2053 VALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEiaarQLGIEhVVSLDGDGKDADGNVVIHGRRA 2132
Cdd:PLN02574  107 VIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLS----PLGVP-VIGVPENYDFDSKRIEFPKFYE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2133 LADLADGNLPRAA-GPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNR----TYLVGPSDRLLFVTSPSFD---LSV 2204
Cdd:PLN02574  182 LIKEDFDFVPKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDNVYLAALPMFHiygLSL 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2205 YdVFGMLAAGGSIHIASEDDLRSperLAAELGRGTITFWDSAPAALQQLVPYFDRIEDGSQLRLAFLSGDWVPIG--MLD 2282
Cdd:PLN02574  262 F-VVGLLSLGSTIVVMRRFDASD---MVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSgkFIQ 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2283 ELRRAFPNVKLVGLGGATEAT-VWSNYFEVDGIDpRWTSIPYGRPiqNARYYVLDRSGNPC-PIGVTGDLYIGGTCVSFG 2360
Cdd:PLN02574  338 DFVQTLPHVDFIQGYGMTESTaVGTRGFNTEKLS-KYSSVGLLAP--NMQAKVVDWSTGCLlPPGNCGELWIQGPGVMKG 414

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260177242 2361 YYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PLN02574  415 YLNNPKATQSTIDKDGW--------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPE 477
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 482-866 2.33e-12

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: 72.46  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  482 ARRVPDAVALDA-----GSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:cd05921     5 ARQAPDRTWLAEregngGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 P--SERLAFLAH--------------------------DAGVQIVLSAAGAEERlgegpwTVVRLDEDLGRPDERDAAPN 608
Cdd:cd05921    85 SlmSQDLAKLKHlfellkpglvfaqdaapfaralaaifPLGTPLVVSRNAVAGR------GAISFAELAATPPTAAVDAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  609 -DNVSAENLAYVMYTSGSTGKPKGVAVTHRNV--VRLVRGSSFATFGPD-QVFLMMAPAAFDASTFEIWGALLHGARLVL 684
Cdd:cd05921   159 fAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLcaNQAMLEQTYPFFGEEpPVLVDWLPWNHTFGGNHNFNLVLYNGGTLY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  685 FPPESPTPEEIGRVVR--EHGVTTLWLTAPLFHAV---ADRGLDQLRG-----VRQLLAGGDVLSP-----------KHV 743
Cdd:cd05921   239 IDDGKPMPGGFEETLRnlREISPTVYFNVPAGWEMlvaALEKDEALRRrffkrLKLMFYAGAGLSQdvwdrlqalavATV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  744 ARvllglpALRLINGYGPTENT-TFTTCHDVSRGMGTgsvpIGKPIANTHVYLldeqmnpVPPNAVGELFTGGDGLARGY 822
Cdd:cd05921   319 GE------RIPMMAGLGATETApTATFTHWPTERSGL----IGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGY 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 260177242  823 HERPDQTAERFVPDPFsgvpgarlYRTGDLARYL----PNGDMEFLGR 866
Cdd:cd05921   382 WRQPELTAQAFDEEGF--------YCLGDAAKLAdpddPAKGLVFDGR 421
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1537-1858 2.76e-12

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: 71.37  E-value: 2.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1537 PLTPLQegilfHALL-------EPGG--SHYCVQLDLAlegALDFDRLQQAWDETLGAHPALRASFLWEGvpepLQVVrr 1607
Cdd:cd19535     3 PLTDVQ-----YAYWigrqddqELGGvgCHAYLEFDGE---DLDPDRLERAWNKLIARHPMLRAVFLDDG----TQQI-- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1608 LVRIPTERI---DARSMAVDGDAWIVERARDE---RRrgFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVL 1681
Cdd:cd19535    69 LPEVPWYGItvhDLRGLSEEEAEAALEELRERlshRV--LDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1682 EEVFKRYSGGmqhEAAHRTAPRPHRDYVAWLRGADAQSVER---FWRRELggfrEVTPLGIDRP----PAGQRASSYRRF 1754
Cdd:cd19535   147 RELAALYEDP---GEPLPPLELSFRDYLLAEQALRETAYERaraYWQERL----PTLPPAPQLPlakdPEEIKEPRFTRR 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1755 ERALDEHTTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLFINTVPMRAVVDPE 1834
Cdd:cd19535   220 EHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEG 299

                         330       340
                  ....*....|....*....|....
gi 260177242 1835 RPIGEWLTELQGRraERTAYEHAS 1858
Cdd:cd19535   300 QSFLERARRLQQQ--LWEDLDHSS 321
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 2153-2433 3.01e-12

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: 70.75  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2153 VIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSP-SFDLSVYDVFGMLAAGGSIHIASEDDLRSPERL 2231
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPaTHIGGLWWILTCLIHGGLCVTGGENTTYKSLFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2232 AAELGRGTITFWdsAPAALQQLVP-YFDRIEDGSQLRLAFLSGDWvPIGMLDELRRAFPNVKLVGLGGATEATvwsnyfe 2310
Cdd:cd17635    86 ILTTNAVTTTCL--VPTLLSKLVSeLKSANATVPSLRLIGYGGSR-AIAADVRFIEATGLTNTAQVYGLSETG------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2311 vdgidpRWTSIPY----------GRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsge 2380
Cdd:cd17635   156 ------TALCLPTdddsieinavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--- 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2381 pgarlyRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:cd17635   227 ------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQ 273
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 1987-2431 3.44e-12

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 71.98  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1987 RCIHELFESSVERSPGSVAL-CYDGVppLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAY 2065
Cdd:PRK07059   23 PSLADLLEESFRQYADRPAFiCMGKA--ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2066 VPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVV--SLdGDGKDADGNVV---------------IH 2128
Cdd:PRK07059  101 VNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVvaSM-GDLLGFKGHIVnfvvrrvkkmvpawsLP 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2129 GRRALAD-LADGN----LPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVI-NLIE---WVNRTYLVGPS-DRLLFVTS- 2197
Cdd:PRK07059  180 GHVRFNDaLAEGArqtfKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQmeaWLQPAFEKKPRpDQLNFVCAl 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2198 P---SFDLSVYDVFGMLAAGGSIHIASEDDLRSperLAAELGRGTITfwdSAPA------ALQQlVPYFDRIeDGSQLRL 2268
Cdd:PRK07059  260 PlyhIFALTVCGLLGMRTGGRNILIPNPRDIPG---FIKELKKYQVH---IFPAvntlynALLN-NPDFDKL-DFSKLIV 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2269 AFLSGDWV--PIGMLDELRRAFPNVKLVGLGgATEATVWSNYFEVDGIdprwtSIPYGRPIQNARYYVLDRSGNPCPIGV 2346
Cdd:PRK07059  332 ANGGGMAVqrPVAERWLEMTGCPITEGYGLS-ETSPVATCNPVDATEF-----SGTIGLPLPSTEVSIRDDDGNDLPLGE 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2347 TGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVAL 2426
Cdd:PRK07059  406 PGEICIRGPQVMAGYWNRPDETAKVMTADGF--------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477


                  ....*
gi 260177242 2427 AQHPG 2431
Cdd:PRK07059  478 ASHPG 482
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2147-2430 3.87e-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: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2147 PHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTsPSFDL--SVYDVFGMLAAGGSIHIASEDD 2224
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGL-PLFHVngSVVTLLTPLASGAHVVLAGPAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2225 LRSP---ERLAAELGRGTITFWDSAPAALQQLVPYFDRiEDGSQLRLAFLSGDWVPIgmldELRRAFPN---VKLVGLGG 2298
Cdd:cd05944    80 YRNPglfDNFWKLVERYRITSLSTVPTVYAALLQVPVN-ADISSLRFAMSGAAPLPV----ELRARFEDatgLPVVEGYG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2299 ATEATVWSNYFEVDGiDPRWTSIPYGRPIQNARYYVLDRSGN---PCPIGVTGDLYIGGTCVsFGYYADPSQTAERFVPD 2375
Cdd:cd05944   155 LTEATCLVAVNPPDG-PKRPGSVGLRLPYARVRIKVLDGVGRllrDCAPDEVGEICVAGPGV-FGGYLYTEGNKNAFVAD 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260177242 2376 PFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05944   233 GW--------LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHP 279
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 2014-2430 5.01e-12

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: 70.67  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPldprwplervaavlGTTRpvcivtde 2093
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP--------------ATTL-------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhLGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHgrraladladgnlpraagphnmayviFTSGSTGTPKGVVerHSQV 2173
Cdd:cd05974    59 --LTPDDLRDRVDRGGAVYAAVDENTHADDPMLLY--------------------------FTSGTTSKPKLVE--HTHR 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLIEWVNRTYLVG--PSDRLLFVTSPSFDLSVYD-VFGMLAAGGSIHIASEDDLrSPERLAAELGRGTITFWDSAPAAL 2250
Cdd:cd05974   109 SYPVGHLSTMYWIGlkPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARF-DAKRVLAALVRYGVTTLCAPPTVW 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2251 QQLVPYfDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEATVWSnyfevdGIDPRWTSIP--YGRPIQ 2328
Cdd:cd05974   188 RMLIQQ-DLASFDVKLREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALV------GNSPGQPVKAgsMGRPLP 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2329 NARYYVLDRSGNPCPIG----VTGDLYIGGtcVSFGYYADPSQTAERFvpdpfsgepGARLYRTGDLARFFRDGNIEFLG 2404
Cdd:cd05974   260 GYRVALLDPDGAPATEGevalDLGDTRPVG--LMKGYAGDPDKTAHAM---------RGGYYRTGDIAMRDEDGYLTYVG 328

                         410       420
                  ....*....|....*....|....*.
gi 260177242 2405 RADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05974   329 RADDVFKSSDYRISPFELESVLIEHP 354
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 502-965 5.33e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 70.45  E-value: 5.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  502 ELNRRADKLAHMLRLKGvGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLsaagaee 581
Cdd:PRK08308   13 DFDLRLQRYEEMEQFQE-AAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLL------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  582 rLGEGPWTVVRLDedlgrpderdaapndNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRgSSFATFGPDQVF--LM 659
Cdd:PRK08308   85 -YGESDFTKLEAV---------------NYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIE-AYNEALNCEQDEtpIV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  660 MAPAAFdaSTFEIWG---ALLHGARLVLFppESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLRGVRQLLAGgd 736
Cdd:PRK08308  148 ACPVTH--SYGLICGvlaALTRGSKPVII--TNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHAVMTSG-- 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  737 VLSPKHVARVLLGLpALRLINGYGPTENTTFTTCHDVsrgmgTGSVPIGKPIAntHVylldeQMNpvppnavgelfTGGD 816
Cdd:PRK08308  222 TPLPEAWFYKLRER-TTYMMQQYGCSEAGCVSICPDM-----KSHLDLGNPLP--HV-----SVS-----------AGSD 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  817 glargyHERPDQTAERFvpdpfsgvpGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREA 896
Cdd:PRK08308  278 ------ENAPEEIVVKM---------GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEA 342

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  897 VVIAREDRPGDKRLVAYVVGREAEVPrfSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK08308  343 VVYRGKDPVAGERVKAKVISHEEIDP--VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 2005-2431 5.51e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 70.79  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2005 ALCYDGVPpLTYSDLNGRANRLGWLLRGLGagpeeRVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTT 2084
Cdd:PRK07787   18 AVRIGGRV-LSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2085 RPVCIvtderhLGAVEIAARqlGIEHVvsldgdgkdadgNVVIHGRRALAdladgnlPRAAGPHNMAYVIFTSGSTGTPK 2164
Cdd:PRK07787   92 GAQAW------LGPAPDDPA--GLPHV------------PVRLHARSWHR-------YPEPDPDAPALIVYTSGTTGPPK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2165 GVV-ERHSQVINL------IEWVnrtylvgpSDRLLFVTSPSFDLS--VYDVFGMLAAGGS-IHIASEddlrSPERLAAE 2234
Cdd:PRK07787  145 GVVlSRRAIAADLdalaeaWQWT--------ADDVLVHGLPLFHVHglVLGVLGPLRIGNRfVHTGRP----TPEAYAQA 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2235 L-GRGTITFwdSAPAALQQLVPYFDRIEDGSQLRLaFLSGDW-VPIGMLDELRRAfPNVKLVGLGGATEaTVWSNYFEVD 2312
Cdd:PRK07787  213 LsEGGTLYF--GVPTVWSRIAADPEAARALRGARL-LVSGSAaLPVPVFDRLAAL-TGHRPVERYGMTE-TLITLSTRAD 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2313 GiDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGV--TGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGD 2390
Cdd:PRK07787  288 G-ERRPGWV--GLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW--------FRTGD 356

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 260177242 2391 LARFFRDGNIEFLGRADSQ-VKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK07787  357 VAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPG 398
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 614-958 6.05e-12

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 70.89  E-value: 6.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  614 ENLAYVM-YTSGSTGKPKGVAVTHRNVVRlvrgSSFATFGPDqvflMMAPAAFDA-----STFEI--WG----ALLHGAR 681
Cdd:PRK07008  175 ENQASSLcYTSGTTGNPKGALYSHRSTVL----HAYGAALPD----AMGLSARDAvlpvvPMFHVnaWGlpysAPLTGAK 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  682 LVLfppesPTPEEIGRVVRE----------HGVTTLWLTapLFHAVADRGLdQLRGVRQLLAGGDVLSPKHVaRVLLGLP 751
Cdd:PRK07008  247 LVL-----PGPDLDGKSLYElieaervtfsAGVPTVWLG--LLNHMREAGL-RFSTLRRTVIGGSACPPAMI-RTFEDEY 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  752 ALRLINGYGPTENTTF-TTC----------HDVSRGMGTGSvpiGKPIANTHVYLLDEQMNPVPPNAVgelfTGGDGLAR 820
Cdd:PRK07008  318 GVEVIHAWGMTEMSPLgTLCklkwkhsqlpLDEQRKLLEKQ---GRVIYGVDMKIVGDDGRELPWDGK----AFGDLQVR 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  821 GyherPDQTAERFVPDPFSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIA 900
Cdd:PRK07008  391 G----PWVIDRYFRGDASPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA 464

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  901 REDRPGDKRLVAYVVGRE-AEVPRfSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKL 958
Cdd:PRK07008  465 CAHPKWDERPLLVVVKRPgAEVTR-EELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 2014-2376 7.71e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 70.49  E-value: 7.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:PRK13391   25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHLGAVEIAARQL-GIEHVVSLDGDGkDADGNVVIhgRRALADLADGNLPRAAGPHNMAYvifTSGSTGTPKGVV----- 2167
Cdd:PRK13391  105 AKLDVARALLKQCpGVRHRLVLDGDG-ELEGFVGY--AEAVAGLPATPIADESLGTDMLY---SSGTTGRPKGIKrplpe 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2168 ERHSQVINLIEWVNRTYLVGPSDRLL-----FVTSPSFDLSVydvfgMLAAGGSIHIASEDDlrsPERLAAELGRGTITF 2242
Cdd:PRK13391  179 QPPDTPLPLTAFLQRLWGFRSDMVYLspaplYHSAPQRAVML-----VIRLGGTVIVMEHFD---AEQYLALIEEYGVTH 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2243 wdsapaalQQLVP-YFDRI----------EDGSQLRLAFLSGDWVPigmldelrrafPNVK---LVGLG-------GATE 2301
Cdd:PRK13391  251 --------TQLVPtMFSRMlklpeevrdkYDLSSLEVAIHAAAPCP-----------PQVKeqmIDWWGpiiheyyAATE 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2302 ATVWSnyfevdGIDPR-WTSIP--YGRPIQnARYYVLDRSGNPCPIGVTGDLYI-GGTcvSFGYYADPSQTAERFVPDP 2376
Cdd:PRK13391  312 GLGFT------ACDSEeWLAHPgtVGRAMF-GDLHILDDDGAELPPGEPGTIWFeGGR--PFEYLNDPAKTAEARHPDG 381
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1989-2434 8.76e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 70.19  E-value: 8.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALCY-DGVppLTYSDLNGRANRLGWLLRGLGAGPEeRVVVWMDRAPELVVALLGILKTGGAYVP 2067
Cdd:PRK07638    3 ITKEYKKHASLQPNKIAIKEnDRV--LTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2068 LDPRWPLERVAAVLGTTRPVCIVTDERHLGaveiaarqlgiehvvsldgDGKDADGNVVI--HGRRALADLADGNLPRAA 2145
Cdd:PRK07638   80 LDIKWKQDELKERLAISNADMIVTERYKLN-------------------DLPDEEGRVIEidEWKRMIEKYLPTYAPIEN 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2146 GPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIaseddL 2225
Cdd:PRK07638  141 VQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL-----M 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2226 R--SPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEdgSQLRLAFLSGDWvPIGMLDELRRAFPNVKLVGLGGATEAT 2303
Cdd:PRK07638  216 RkfIPNQVLDKLETENISVMYTVPTMLESLYKENRVIE--NKMKIISSGAKW-EAEAKEKIKNIFPYAKLYEFYGASELS 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2304 VWSNYFEVDGIDPRwTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAerfvpdpfsgEPGA 2383
Cdd:PRK07638  293 FVTALVDEESERRP-NSV--GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAR----------ELNA 359

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 260177242 2384 RLYRT-GDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQR 2434
Cdd:PRK07638  360 DGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDE 411
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 2013-2430 1.08e-11

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: 69.93  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2013 PLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTD 2092
Cdd:cd05907     5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ErhlgaveiaarqlgiehvvsldgdgkdadgnvvihgrraLADLADgnlpraagphnmayVIFTSGSTGTPKGVVERH-- 2170
Cdd:cd05907    85 D---------------------------------------PDDLAT--------------IIYTSGTTGRPKGVMLSHrn 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2171 --SQVINLIEWVNrtylVGPSDRLLfvtspSF-DLS-----VYDVFGMLAAGGSIHIASeddlrSPERLAAELGRGTITF 2242
Cdd:cd05907   112 ilSNALALAERLP----ATEGDRHL-----SFlPLAhvferRAGLYVPLLAGARIYFAS-----SAETLLDDLSEVRPTV 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2243 WDSAP--------AALQQLVPYFDRIedgsQLRLAFL-SGDWVPIG---MLDELRRAFpnvklVGLG-------GATE-- 2301
Cdd:cd05907   178 FLAVPrvwekvyaAIKVKAVPGLKRK----LFDLAVGgRLRFAASGgapLPAELLHFF-----RALGipvyegyGLTEts 248

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2302 ATVWSNYFEvdgiDPRWTSIpyGRPIqnaryyvldrSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgep 2381
Cdd:cd05907   249 AVVTLNPPG----DNRIGTV--GKPL----------PGVEVRIADDGEILVRGPNVMLGYYKNPEATAEALDADGW---- 308

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 260177242 2382 garlYRTGDLARFFRDGNIEFLGRA-DSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05907   309 ----LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASP 354
PLN02479 PLN02479
acetate-CoA ligase
 800-965 1.10e-11

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 70.26  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  800 MNPVPPN--AVGELFTGGDGLARGYHERPDQTAERFvpdpfsgvpGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFR 877
Cdd:PLN02479  392 MKPVPADgkTMGEIVMRGNMVMKGYLKNPKANEEAF---------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGEN 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  878 IELAEVEAALLQHPALREAVVIAREDRPGDKRLVAYV-----VGREAEVPRFSELRKFLLQRLPDHMIPAAVVaLDKLPL 952
Cdd:PLN02479  463 ISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPK 541

                         170
                  ....*....|...
gi 260177242  953 VPSGKLDRRALPA 965
Cdd:PLN02479  542 TATGKIQKHVLRA 554
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 2015-2431 1.55e-11

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 69.68  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRP---VCIVT 2091
Cdd:PRK07470   34 TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGAramICHAD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2092 DERHLGAVEIAArqLGIEHVVSLDGDGKDADgnvvihgrraLADLADGNLPRAAGPHNMAY-----VIFTSGSTGTPKGV 2166
Cdd:PRK07470  114 FPEHAAAVRAAS--PDLTHVVAIGGARAGLD----------YEALVARHLGARVANAAVDHddpcwFFFTSGTTGRPKAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2167 VERHSQ---VINliewvNRTYLVGP----SDRLLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDdlRSPERLAAELGRGT 2239
Cdd:PRK07470  182 VLTHGQmafVIT-----NHLADLMPgtteQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSER--FDPAEVWALVERHR 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2240 ITFWDSAPAALQQLV--PYFDRIeDGSQLRLAFLSGdwVPIGMLDElRRAFPN-----VKLVGLGGATEA-TVWSNYF-- 2309
Cdd:PRK07470  255 VTNLFTVPTILKMLVehPAVDRY-DHSSLRYVIYAG--APMYRADQ-KRALAKlgkvlVQYFGLGEVTGNiTVLPPALhd 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2310 EVDGIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlyRTG 2389
Cdd:PRK07470  331 AEDGPDARIGTC--GFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF---------RTG 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 260177242 2390 DLARFFRDGNIEFLGRAdSQVKIR-GYRIECGEVEVALAQHPG 2431
Cdd:PRK07470  400 DLGHLDARGFLYITGRA-SDMYISgGSNVYPREIEEKLLTHPA 441
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 41-271 1.80e-11

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: 69.05  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   41 EAAIRRsmeaVLERRDALRLVVRPDneGLVQSLADVSAVDFGVTDGSSWDEPtaaawlqaeaarpfDLRAGALRVRA--- 117
Cdd:cd19535    43 ERAWNK----LIARHPMLRAVFLDD--GTQQILPEVPWYGITVHDLRGLSEE--------------EAEAALEELRErls 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  118 -LRRAPDQWQiLFAFH-----------HI-----VCDGWSAMIVAAEFAELcaadVEGRAATLTPISRGFRDYLVWHRDL 180
Cdd:cd19535   103 hRVLDVERGP-LFDIRlsllpegrtrlHLsidllVADALSLQILLRELAAL----YEDPGEPLPPLELSFRDYLLAEQAL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  181 LASDDASAlvRE-WAAMVGDLdvstPL--DLPT--DLPRRAQQRYHVRQHFrdLGADLMDRVRESARAEGVTTYTVLLAA 255
Cdd:cd19535   178 RETAYERA--RAyWQERLPTL----PPapQLPLakDPEEIKEPRFTRREHR--LSAEQWQRLKERARQHGVTPSMVLLTA 249

                         250
                  ....*....|....*.
gi 260177242  256 YQVLLTRLSSQRPFLV 271
Cdd:cd19535   250 YAEVLARWSGQPRFLL 265
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 2014-2394 2.06e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 69.30  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPL-----ERVAAVLGTTRPVC 2088
Cdd:PRK12582   81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRV 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2089 IVTDERHLGAVEIAARQLGIEHVVSLDGDGkdaDGNVVIHgrraLADLAdGNLPRAA--------GPHNMAYVIFTSGST 2160
Cdd:PRK12582  161 VFAQSGAPFARALAALDLLDVTVVHVTGPG---EGIASIA----FADLA-ATPPTAAvaaaiaaiTPDTVAKYLFTSGST 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2161 GTPKGVVERH----SQVINLIEWVNRTYLVGPSDRL-------LFVTSPSFDlsvydvfGMLAAGGSIHIaseDDLRSPE 2229
Cdd:PRK12582  233 GMPKAVINTQrmmcANIAMQEQLRPREPDPPPPVSLdwmpwnhTMGGNANFN-------GLLWGGGTLYI---DDGKPLP 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLAAElgrgTI--------TFWDSAPAALQQLVPYFDRieDgsqlrlaflsgdwvpigmlDELRRA-FPNVKLVGLGGAT 2300
Cdd:PRK12582  303 GMFEE----TIrnlreispTVYGNVPAGYAMLAEAMEK--D-------------------DALRRSfFKNLRLMAYGGAT 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2301 eatvWSN--YFEVDGIDPRWTS--IP----YG----RPIQNARYYVLDRSG-----------NPCPIGVTGDLYIGGTCV 2357
Cdd:PRK12582  358 ----LSDdlYERMQALAVRTTGhrIPfytgYGatetAPTTTGTHWDTERVGliglplpgvelKLAPVGDKYEVRVKGPNV 433

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 260177242 2358 SFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARF 2394
Cdd:PRK12582  434 TPGYHKDPELTAAAFDEEGF--------YRLGDAARF 462
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1065-1326 2.12e-11

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: 68.60  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1065 PLTPIQR--WFLS--GEPAAPHHFNQAVLL-------ALRdawvpkhvdAAVGAVIRHHDALRLRFVAEDGMWRARGMPS 1133
Cdd:cd19540     3 PLSFAQQrlWFLNrlDGPSAAYNIPLALRLtgaldvdALR---------AALADVVARHESLRTVFPEDDGGPYQVVLPA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1134 GG-PVPYEVVDLSE--LPGEERRAALEAraaeaqasLDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLAD 1210
Cdd:cd19540    74 AEaRPDLTVVDVTEdeLAARLAEAARRG--------FDLTAELPLRARLFRLGPDE-HVLVLVVHHIAADGWSMAPLARD 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1211 LATAHRQLVEGeivRLPSKTT--------SLrrWGERLLATVDE---VVAAELPFW-EALDGqgvrpLPRGCEPAEDR-- 1276
Cdd:cd19540   145 LATAYAARRAG---RAPDWAPlpvqyadyAL--WQRELLGDEDDpdsLAARQLAYWrETLAG-----LPEELELPTDRpr 214

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 1277 ------EGDAQTVEVwlgGPETEALLGRVGEAYRTRADEVILAALAGALTEWAGGE 1326
Cdd:cd19540   215 pavasyRGGTVEFTI---DAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGD 267
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 496-928 2.62e-11

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: 68.99  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  496 NVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLs 575
Cdd:cd17641    10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  576 aAGAEERLGE--------------------------GPWtVVRLDEDLGRPDERDAAPNDNVSA-------ENLAYVMYT 622
Cdd:cd17641    89 -AEDEEQVDKlleiadripsvryviycdprgmrkydDPR-LISFEDVVALGRALDRRDPGLYERevaagkgEDVAVLCTT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  623 SGSTGKPKGVAVTHRNVVRLVRGS-SFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTP----EEIG- 696
Cdd:cd17641   167 SGTTGKPKLAMLSHGNFLGHCAAYlAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPETMmedlREIGp 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  697 -------RV-------VREHGVTTLWLTAPLFHA---VADRGLDQ-LRGVRQLLAGGDV--LSPKHVARVL---LGLPAL 753
Cdd:cd17641   247 tfvllppRVwegiaadVRARMMDATPFKRFMFELgmkLGLRALDRgKRGRPVSLWLRLAswLADALLFRPLrdrLGFSRL 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  754 R-----------------------LINGYGPTENTTFTTCHDvsrgmgTGSVP---IGKPIANTHVYLlDEqmnpvppna 807
Cdd:cd17641   327 RsaatggaalgpdtfrffhaigvpLKQLYGQTELAGAYTVHR------DGDVDpdtVGVPFPGTEVRI-DE--------- 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  808 VGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGR-RDGQVKIRGFRIELAEVEAA 886
Cdd:cd17641   391 VGEILVRSPGVFVGYYKNPEATAEDFDEDGW--------LHTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFIENK 462

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 260177242  887 LLQHPALREAVVIAReDRPgdkRLVAYVVGREAEVPRFSELR 928
Cdd:cd17641   463 LKFSPYIAEAVVLGA-GRP---YLTAFICIDYAIVGKWAEQR 500
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 598-963 3.58e-11

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. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 68.23  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  598 GRPDERDAAPNDNVSAENLAYvmyTSGSTGKPKGVAVTHRNV---VRLVRGSSFATFGPDQVFLMMAPAAFDASTFEIWG 674
Cdd:cd05915   140 ALGEEADPVRVPERAACGMAY---TTGTTGLPKGVVYSHRALvlhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYA 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  675 ALLHGARLVLFPpESPTPEEIGRVVREHGVTTLWLTAPLFHAVADrGLDQLRG----VRQLLAGGDvlSPKHVARVLLGL 750
Cdd:cd05915   217 ATLVGAKQVLPG-PRLDPASLVELFDGEGVTFTAGVPTVWLALAD-YLESTGHrlktLRRLVVGGS--AAPRSLIARFER 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  751 PALRLINGYGptenttfttCHDVSrGMGTG--------------SVPIGKPIANTH----VYLLDEQMNPVPPNA--VGE 810
Cdd:cd05915   293 MGVEVRQGYG---------LTETS-PVVVQnfvkshleslseeeKLTLKAKTGLPIplvrLRVADEEGRPVPKDGkaLGE 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  811 LFTGGDGLARGYHERPDQTAerfvPDPFSGvpgaRLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQH 890
Cdd:cd05915   363 VQLKGPWITGGYYGNEEATR----SALTPD----GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGH 434

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242  891 PALREAVVIAREDRPGDKRLVAYVVGREAEVpRFSELRKFLLQRLPD-HMIPAAVVALDKLPLVPSGKLDRRAL 963
Cdd:cd05915   435 PKVKEAAVVAIPHPKWQERPLAVVVPRGEKP-TPEELNEHLLKAGFAkWQLPDAYVFAEEIPRTSAGKFLKRAL 507
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1987-2442 3.64e-11

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 68.36  E-value: 3.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1987 RCIHELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLG-WLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAY 2065
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYHSFG-KTITYREADQLVEQFAaYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2066 VPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVS-----LDGDGKDADGNVV-------------- 2126
Cdd:PRK08751  104 VNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITtglgdMLGFPKAALVNFVvkyvkklvpeyrin 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2127 --IHGRRALADLADGNLPRAA-GPHNMAYVIFTSGSTGTPKGVVERHSQVI-NLIE---WVNRTYLVGPSDRLLFVTSPs 2199
Cdd:PRK08751  184 gaIRFREALALGRKHSMPTLQiEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQahqWLAGTGKLEEGCEVVITALP- 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2200 fdlsVYDVFGMLA-------AGGSIHIASedDLRSPERLAAELGRGTITFWDSAPAALQQLV--PYFDRIeDGSQLRLAF 2270
Cdd:PRK08751  263 ----LYHIFALTAnglvfmkIGGCNHLIS--NPRDMPGFVKELKKTRFTAFTGVNTLFNGLLntPGFDQI-DFSSLKMTL 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2271 LSGDWVPIGMLDELRRAfPNVKLVGLGGATEATVWSNYFEVDgIDPRWTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDL 2350
Cdd:PRK08751  336 GGGMAVQRSVAERWKQV-TGLTLVEAYGLTETSPAACINPLT-LKEYNGSI--GLPIPSTDACIKDDAGTVLAIGEIGEL 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2351 YIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK08751  412 CIKGPQVMKGYWKRPEETAKVMDADGW--------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMP 483

                         490
                  ....*....|..
gi 260177242 2431 GAQRGRGSGGPE 2442
Cdd:PRK08751  484 GVLEVAAVGVPD 495
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1065-1552 5.12e-11

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: 68.73  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1065 PLTPIQRWFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDgmWRARGMPSGGPVPYEVVDL 1144
Cdd:COG1020    23 AQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGR--PVQVIQPVVAAPLPVVVLL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1145 SELPGEERRAALEARAAEAQASLDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIV 1224
Cdd:COG1020   101 VDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLL-LLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1225 RLPSKTTSL---RRWGERLLAtvDEVVAAELPFW--EALDGQGVRPLPRGCEPAEDREGDAQTVEVWLGGPETEALLgRV 1299
Cdd:COG1020   180 PLPPLPIQYadyALWQREWLQ--GEELARQLAYWrqQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALR-AL 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1300 GEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGReelfPDIEVARTVGWFTTIHPVVLPGRPQ-SAGARLKAVKEA 1378
Cdd:COG1020   257 ARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGR----PRPELEGLVGFFVNTLPLRVDLSGDpSFAELLARVRET 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1379 IRRVPKHgigygilRYLGSDEVVTRL------ARLPAPEVAFNYLGRLDRALpkdgpfvmapEAAGPSVSPRGKRSHA-- 1450
Cdd:COG1020   333 LLAAYAH-------QDLPFERLVEELqperdlSRNPLFQVMFVLQNAPADEL----------ELPGLTLEPLELDSGTak 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1451 --LQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAHAidvgseaswtpsDFPLARlephvLDALVDADR 1528
Cdd:COG1020   396 fdLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADP------------DQPLGD-----LPLLTAAER 458

                         490       500
                  ....*....|....*....|....*
gi 260177242 1529 ARPLDDL-YPLTPLQEGILFHALLE 1552
Cdd:COG1020   459 QQLLAEWnATAAPYPADATLHELFE 483
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1533-1828 6.74e-11

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: 67.12  E-value: 6.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1533 DDLYPLTPLQEGILFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFlwegvPEPLQVVRRLVRIP 1612
Cdd:cd19546     2 PDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF-----PGDGGDVHQRILDA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1613 TERIDARSMAVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGM 1692
Cdd:cd19546    77 DAARPELPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1693 QHEAAHRtAPRPHR--DYVAW----LRGADAQSV-----ERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEH 1761
Cdd:cd19546   157 EGRAPER-APLPLQfaDYALWerelLAGEDDRDSligdqIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAE 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242 1762 TTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGeTVSGRSAPLEGIERMVGLFINTVPMR 1828
Cdd:cd19546   236 VHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALR 301
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 2152-2431 1.15e-10

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: 65.87  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2152 YVIFTSGSTGTPKGVVERHSQV-------INL-------IEWVNRTYLVGPSDRLLFVTSPSFDLSVYDVFGMLAAGGSI 2217
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIfrmlmggADFgtgeftpSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2218 hIASEDDLRSPE--RLAAELGRGTITFWDSAPAAlqqlvPYFDRIEDG-----SQLRLAFLSGDWVPIGMLDELRRAFPN 2290
Cdd:cd05924    87 -VLPDDRFDPEEvwRTIEKHKVTSMTIVGDAMAR-----PLIDALRDAgpydlSSLFAISSGGALLSPEVKQGLLELVPN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2291 VKLVGLGGATEATVWSnYFEVDGidprwtSIPYGRPIQNA--RYYVLDRSGNPCPIGVTGDLYIGGT-CVSFGYYADPSQ 2367
Cdd:cd05924   161 ITLVDAFGSSETGFTG-SGHSAG------SGPETGPFTRAnpDTVVLDDDGRVVPPGSGGVGWIARRgHIPLGYYGDEAK 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242 2368 TAERFVPdpfsgEPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05924   234 TAETFPE-----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPA 292
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 1979-2431 1.38e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 66.49  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1979 TARAYARERCIHELFESSVERSPGSVALCyDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGI 2058
Cdd:PRK07788   41 LAADIRRYGPFAGLVAHAARRAPDRAALI-DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2059 LKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVVSLDGDGKDADGNvvihGRRALADLAD 2138
Cdd:PRK07788  120 GKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGS----TDETLDDLIA 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2139 GN----LPRAAGPHNMayVIFTSGSTGTPKGVVERH-------SQVINLIEWvnrtylvgPSDRLLFVTSPSFDLSVYDV 2207
Cdd:PRK07788  196 GSstapLPKPPKPGGI--VILTSGTTGTPKGAPRPEpsplaplAGLLSRVPF--------RAGETTLLPAPMFHATGWAH 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2208 FGMLAAGGSIHIaseddLR---SPERLAAELGRGTITFWDSAPAALQQLVPYFDRIE---DGSQLRLAFLSGDWVPIGML 2281
Cdd:PRK07788  266 LTLAMALGSTVV-----LRrrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLakyDTSSLKIIFVSGSALSPELA 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2282 DELRRAFPNVkLVGLGGATE---ATVwsnyfevdgIDPR-WTSIP--YGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGT 2355
Cdd:PRK07788  341 TRALEAFGPV-LYNLYGSTEvafATI---------ATPEdLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNG 410

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 2356 cVSFGYYADPSQtaerfvPDPFSGepgarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK07788  411 -FPFEGYTDGRD------KQIIDG-----LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPD 474
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 595-960 2.62e-10

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 65.17  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  595 EDLGR-P-----DERDAAPNDN--VSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLV----RGSSFATFGPDQVFLMMAP 662
Cdd:COG1541    56 EDLAKlPfttkeDLRDNYPFGLfaVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAelfaRSLRAAGVRPGDRVQNAFG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  663 aafdastFEIW--GALLH-GAR----LVLfpPESP-TPEEIGRVVREHGVTTLWLTAPLFHAVAD----RGLDqLR--GV 728
Cdd:COG1541   136 -------YGLFtgGLGLHyGAErlgaTVI--PAGGgNTERQLRLMQDFGPTVLVGTPSYLLYLAEvaeeEGID-PRdlSL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  729 RQLLAGGDVLSPKHVARV--LLGLPAlrlINGYGPTE--NTTFTTCHDvSRGMGtgsvpigkpIANTHVY--LLD-EQMN 801
Cdd:COG1541   206 KKGIFGGEPWSEEMRKEIeeRWGIKA---YDIYGLTEvgPGVAYECEA-QDGLH---------IWEDHFLveIIDpETGE 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  802 PVPPNAVGEL-FTggdGLARgyherpdqtaerfvpdpfSGVPGARlYRTGDLARYLPnGDME----------FLGRRDGQ 870
Cdd:COG1541   273 PVPEGEEGELvVT---TLTK------------------EAMPLIR-YRTGDLTRLLP-EPCPcgrthprigrILGRADDM 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  871 VKIRGFRIELAEVEAALLQHPALR-EAVVIAreDRPGDKRLVAYVVGREAEVPRfSELRKFLLQRLPDH-MIPAAVVald 948
Cdd:COG1541   330 LIIRGVNVFPSQIEEVLLRIPEVGpEYQIVV--DREGGLDELTVRVELAPGASL-EALAEAIAAALKAVlGLRAEVE--- 403

                         410
                  ....*....|..
gi 260177242  949 klpLVPSGKLDR 960
Cdd:COG1541   404 ---LVEPGSLPR 412
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 984-1042 3.32e-10

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: 57.57  E-value: 3.32e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242   984 EVLARIWERVLRVDA--VGREDNFFELGGDSILAIQVVAG-AREVDLKLTVRQIFTHPTLSS 1042
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARlEEEFGVEIPPSDLFEHPTLAE 62
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 497-898 5.98e-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: 64.30  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  497 VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPaypSERLAFLAHdagvqiVLSA 576
Cdd:cd05940     3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINY---NLRGESLAH------CLNV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  577 AGAEerlgegpwtVVRLDedlgrpderdaapndnvsaenLAYVMYTSGSTGKPKGVAVTHRNVVRLVR--GSSFATFGPD 654
Cdd:cd05940    74 SSAK---------HLVVD---------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAffAGSGGALPSD 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  655 QVFLMMAPAAFDASTFEIWGALLHGARLVLFPPESPTpeEIGRVVREHGVTTLWLTAPLFH---AVADRGLDQLRGVRQL 731
Cdd:cd05940   124 VLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSAS--NFWDDIRKYQATIFQYIGELCRyllNQPPKPTERKHKVRMI 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  732 LAGGdvLSP----KHVARvlLGLPalRLINGYGPTENTTFTTCHDVSRGMGTGSVPIGKPIANTHVYLLDEQ-------- 799
Cdd:cd05940   202 FGNG--LRPdiweEFKER--FGVP--RIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDLEsgepirda 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  800 ---MNPVPPNAVGELFTGGDGLAR--GYHErPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIR 874
Cdd:cd05940   276 egrCIKVPRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVFK--KGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK 352

                         410       420
                  ....*....|....*....|....
gi 260177242  875 GFRIELAEVEAALLQHPALREAVV 898
Cdd:cd05940   353 GENVSTTEVAAVLGAFPGVEEANV 376
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 1989-2442 7.38e-10

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 64.28  E-value: 7.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1989 IHELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPL 2068
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLG-KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2069 DPRWPLERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHV-VSLDGDGKDADGNVV--------------------I 2127
Cdd:PRK06710  105 NPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHViVTRIADFLPFPKNLLypfvqkkqsnlvvkvsesetI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2128 HGRRALADLADGNLPRAAGPHN-MAYVIFTSGSTGTPKGVVERHSQVI-NLIEWVNRTYLVGPSDRLLFVTSPSFdlsvy 2205
Cdd:PRK06710  185 HLWNSVEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVVLGVLPFF----- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2206 DVFGMLAA-------GGSIHIASEDDLRspeRLAAELGRGTITFWDSAPAALQQLV--PYFDRIeDGSQLRLAFLSGDWV 2276
Cdd:PRK06710  260 HVYGMTAVmnlsimqGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnsPLLKEY-DISSIRACISGSAPL 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2277 PIgmldELRRAFPNV---KLVGLGGATEAT-VWSNYFEVDGIDPRWTSIPYgrPIQNARYYVLDrSGNPCPIGVTGDLYI 2352
Cdd:PRK06710  336 PV----EVQEKFETVtggKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPW--PDTEAMIMSLE-TGEALPPGEIGEIVV 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2353 GGTCVSFGYYADPSQTAErFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGA 2432
Cdd:PRK06710  409 KGPQIMKGYWNKPEETAA-VLQDGW--------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKV 479

                         490
                  ....*....|
gi 260177242 2433 QRGRGSGGPE 2442
Cdd:PRK06710  480 QEVVTIGVPD 489
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 613-960 9.71e-10

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: 63.66  E-value: 9.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  613 AENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVFLMMAPAAFDAS--TFEIwGALLHGARLVLFPpes 689
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTeWKTKDRILSWMPLTHDMGliAFHL-APLIAGMNQYLMP--- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  690 pTPEEIGR------VVREHGVTTLwlTAPLF--HAVADRGLDQ------LRGVRQLLAGGDVLSPKHVARVLLGLPALRL 755
Cdd:cd05908   181 -TRLFIRRpilwlkKASEHKATIV--SSPNFgyKYFLKTLKPEkandwdLSSIRMILNGAEPIDYELCHEFLDHMSKYGL 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  756 -----INGYGPTENTT----------FTTCHDVSRGMGTGS---------------VPIGKPIANTHVYLLDEQMNPVPP 805
Cdd:cd05908   258 krnaiLPVYGLAEASVgaslpkaqspFKTITLGRRHVTHGEpepevdkkdsecltfVEVGKPIDETDIRICDEDNKILPD 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  806 NAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLArYLPNGDMEFLGRRDGQVKIRGFRIELAEVEA 885
Cdd:cd05908   338 GYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW--------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIER 408

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  886 ALLQ-HPALREAVVI--AREDRPGDKRLVAYVVGREAE---VPRFSELRKFLLQRLPDHMipAAVVALDKLPLVPSGKLD 959
Cdd:cd05908   409 IAEElEGVELGRVVAcgVNNSNTRNEEIFCFIEHRKSEddfYPLGKKIKKHLNKRGGWQI--NEVLPIRRIPKTTSGKVK 486


                  .
gi 260177242  960 R 960
Cdd:cd05908   487 R 487
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 2013-2427 1.14e-09

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: 63.83  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2013 PLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTD 2092
Cdd:cd05943    98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAV 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ERHL--GAV--------EIAARQLGIEHVVSLDGDGKDADGNVVIHGRRALadLADGNLPRAAGPHNMA--------YVI 2154
Cdd:cd05943   178 DAYTynGKRhdvrekvaELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALT--LEDFLATGAAGELEFEplpfdhplYIL 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2155 FTSGSTGTPKGVVerHSQVINLIEWVNRTYL---VGPSDRLLFVTSPSFDLSVYDVFGmLAAGGSIHIASEDDLRSPE-- 2229
Cdd:cd05943   256 YSSGTTGLPKCIV--HGAGGTLLQHLKEHILhcdLRPGDRLFYYTTCGWMMWNWLVSG-LAVGATIVLYDGSPFYPDTna 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 --RLAAELGrgtIT-FWDSAP--AALQQLVPYFDRIEDGSQLRLAFLSG--------DWVPigmldelRRAFPNVKLVGL 2296
Cdd:cd05943   333 lwDLADEEG---ITvFGTSAKylDALEKAGLKPAETHDLSSLRTILSTGsplkpesfDYVY-------DHIKPDVLLASI 402

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2297 GGATEatVWSNYFEVDGIDPRWTSipygrPIQnARYY-----VLDRSGNPCpIGVTGDLYI--GGTCVSFGYYADPSqtA 2369
Cdd:cd05943   403 SGGTD--IISCFVGGNPLLPVYRG-----EIQ-CRGLgmaveAFDEEGKPV-WGEKGELVCtkPFPSMPVGFWNDPD--G 471

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 2370 ERFVPDPFSGEPGarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRI----------ECGEVEVALA 2427
Cdd:cd05943   472 SRYRAAYFAKYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIgtaeiyrvveKIPEVEDSLV 537
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 2153-2431 1.15e-09

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: 62.52  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2153 VIFTSGSTGTPKGVVERHSQVINLI-EWVNRTYLVGpSDRLLFVtSPSFDLSVYD---VFGMLAAGGSIHIASEDDLRSP 2228
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHRQTLRAAaAWADCADLTE-DDRYLII-NPFFHTFGYKagiVACLLTGATVVPVAVFDVDAIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2229 ERLAAElgrgTITFWDSAPAALQQLVPYFDRIE-DGSQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEATVwsn 2307
Cdd:cd17638    83 EAIERE----RITVLPGPPTLFQSLLDHPGRKKfDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV--- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2308 yfevdgidprwtsIPYGRPIQNARyYVLDRSGNPCP-----IGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepg 2382
Cdd:cd17638   156 -------------ATMCRPGDDAE-TVATTCGRACPgfevrIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGW----- 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 260177242 2383 arlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17638   217 ---LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPG 262
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 2019-2430 1.18e-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: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2019 LNGRANRLGWLLRGLGA---------------GPEERVVVWMDRAPELVVALLGILKTGGAYVP----LDPRWPLERvaa 2079
Cdd:cd05928    33 VNGKGDEVKWSFRELGSlsrkaanvlsgacglQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPgtiqLTAKDILYR--- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2080 vLGTTRPVCIVTDERHLGAVEIAARQ---LGIEHVVSLdgdgkdadgnvviHGRRALADLaDGNLPRAAGPHN------- 2149
Cdd:cd05928   110 -LQASKAKCIVTSDELAPEVDSVASEcpsLKTKLLVSE-------------KSRDGWLNF-KELLNEASTEHHcvetgsq 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2150 --MAyVIFTSGSTGTPKgvVERHSQVINLIEW-VNRTYLVG--PSDRLLFVTSPSFDLSVY-DVFGMLAAGGSI---HIA 2220
Cdd:cd05928   175 epMA-IYFTSGTTGSPK--MAEHSHSSLGLGLkVNGRYWLDltASDIMWNTSDTGWIKSAWsSLFEPWIQGACVfvhHLP 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2221 SEDdlrsPERLAAELGRGTITFWDSAPAALQQLVPY-FDRIEDGSqLRLAFLSGDWVPIGMLDELRRafpnvkLVGLG-- 2297
Cdd:cd05928   252 RFD----PLVILKTLSSYPITTFCGAPTVYRMLVQQdLSSYKFPS-LQHCVTGGEPLNPEVLEKWKA------QTGLDiy 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2298 ---GATEATVWSNYFEVDGIDPRWtsipYGRPIQNARYYVLDRSGNPCPIGVTGDLYI-----GGTCVSFGYYADPSQTA 2369
Cdd:cd05928   321 egyGQTETGLICANFKGMKIKPGS----MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTA 396

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260177242 2370 ERFVPDpfsgepgarLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05928   397 ATIRGD---------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHP 448
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 2004-2430 1.29e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 63.62  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2004 VALCYDGVPP-----LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTG-------GAYVP--LD 2069
Cdd:PRK00174   84 VAIIWEGDDPgdsrkITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGFSAeaLA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2070 PRwpLERVAAVL----------GTTRPVCIVTDErhlgAVEIAArqlGIEHVVSLdgdgKDADGNVVIHGRR------AL 2133
Cdd:PRK00174  164 DR--IIDAGAKLvitadegvrgGKPIPLKANVDE----ALANCP---SVEKVIVV----RRTGGDVDWVEGRdlwwheLV 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2134 ADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVerHS------QVINLIEWV-----NRTYL----VGpsdrllFVTSP 2198
Cdd:PRK00174  231 AGASDECEPEPMDAEDPLFILYTSGSTGKPKGVL--HTtggylvYAAMTMKYVfdykdGDVYWctadVG------WVTGH 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2199 SfdlsvYDVFGMLAAGGSIhIASEDDLRSPERlaaelGRgtitFWD-----------SAPAALQQLVPYFDRI---EDGS 2264
Cdd:PRK00174  303 S-----YIVYGPLANGATT-LMFEGVPNYPDP-----GR----FWEvidkhkvtifyTAPTAIRALMKEGDEHpkkYDLS 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2265 QLRLAFLSGDwvPIGmldelrrafPnvklvglggatEATVWsnYFEVDG------IDPRW---------TSIP------- 2322
Cdd:PRK00174  368 SLRLLGSVGE--PIN---------P-----------EAWEW--YYKVVGgercpiVDTWWqtetggimiTPLPgatplkp 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2323 --YGRP---IQNAryyVLDRSGNPCPIGVTGDLYIGGtcvSF-----GYYADPsqtaERFVPDPFSGEPGarLYRTGDLA 2392
Cdd:PRK00174  424 gsATRPlpgIQPA---VVDEEGNPLEGGEGGNLVIKD---PWpgmmrTIYGDH----ERFVKTYFSTFKG--MYFTGDGA 491

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 260177242 2393 RFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK00174  492 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 529
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 26-438 2.17e-09

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: 62.32  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   26 VYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRL-VVRPDNEGLVQSLadVSAVDFGVTDGSSWDEPtaaawLQAEAAR 104
Cdd:cd19545    21 AYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTrIVQSDSGGLLQVV--VKESPISWTESTSLDEY-----LEEDRAA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  105 PFDLRAGALRVRALRRAPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAadveGRAATLTPISRGFRDYLVWHRDllasd 184
Cdd:cd19545    94 PMGLGGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ----GEPVPQPPPFSRFVKYLRQLDD----- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  185 daSALVREWAAMVGDLDVS--TPLDLPTDLPRRAQQRYHvrqhfrdlgadlmdRVRESARAE-GVTTYTVLLAAYQVLLT 261
Cdd:cd19545   165 --EAAAEFWRSYLAGLDPAvfPPLPSSRYQPRPDATLEH--------------SISLPSSASsGVTLATVLRAAWALVLS 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  262 RLSSQRPFLVGCGVSGRTrtwqLGV--VGHMAG--IVPVPARIDAAATpraiirelrnaLRVTAKLQSVPlSRLAEQcrv 337
Cdd:cd19545   229 RYTGSDDVVFGVTLSGRN----APVpgIEQIVGptIATVPLRVRIDPE-----------QSVEDFLQTVQ-KDLLDM--- 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  338 pkspgrMPLVQAVFQEIRSFNEAIRP-EGFGHML--------------RWSRGPLGFEVEVPSELGsqLDLEVRCYDffs 402
Cdd:cd19545   290 ------IPFEHTGLQNIRRLGPDARAaCNFQTLLvvqpalpsstseslELGIEEESEDLEDFSSYG--LTLECQLSG--- 358

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 260177242  403 SSVRTCWRYDPDLFLPETVERWADYYAALLRELVGD 438
Cdd:cd19545   359 SGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 499-941 2.48e-09

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: 62.45  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  499 SYGELNRRADKLAHMLR-LKGVGTETRVGLCLERSVELVVGILGVLKAGGAyvpldPAYPSERLAflahDAGVQIVLSAA 577
Cdd:cd05937     7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAFINYNLS----GDPLIHCLKLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  578 GAeerlgegpwTVVRLDEDlgrpderdaapndnvsaeNLAYVMYTSGSTGKPKGVAVTHRNVVR--LVRGSSFATFGPDQ 655
Cdd:cd05937    78 GS---------RFVIVDPD------------------DPAILIYTSGTTGLPKAAAISWRRTLVtsNLLSHDLNLKNGDR 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  656 VFLMMApaAFDASTFEIWGA--LLHGARLVLFPPESPTpeEIGRVVREHGVTTLW----LTAPLFHAVADRgLDQLRGVR 729
Cdd:cd05937   131 TYTCMP--LYHGTAAFLGACncLMSGGTLALSRKFSAS--QFWKDVRDSGATIIQyvgeLCRYLLSTPPSP-YDRDHKVR 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  730 qlLAGGDVLSPK--HVARVLLGLPALRLIngYGPTENTTFTTCHDVSrGMGTGSV----PIGKPIANTHVYLLdeQMNP- 802
Cdd:cd05937   206 --VAWGNGLRPDiwERFRERFNVPEIGEF--YAATEGVFALTNHNVG-DFGAGAIghhgLIRRWKFENQVVLV--KMDPe 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  803 ---------------VPPNAVGE----LFTGGDGLARGYHERPDQTAERFVPDPFSgvPGARLYRTGDLARYLPNGDMEF 863
Cdd:cd05937   279 tddpirdpktgfcvrAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFR--KGDIYFRTGDLLRQDADGRWYF 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  864 LGRRDGQVKIRGFRIELAEVEAALLQHPALREAVV--IAREDRPGDKRLVAYVVGREAEVP---RFSELRKFLLQRLPDH 938
Cdd:cd05937   357 LDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSAVPtefTKSLLASLARKNLPSY 436


                  ...
gi 260177242  939 MIP 941
Cdd:cd05937   437 AVP 439
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1537-1766 2.79e-09

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: 61.88  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1537 PLTPLQEgiLFHALLEPGGSHYCVQLDLALEGALDFDRLQQAWDETLGAHPALRASFLWEGVpeplQVVRRLVRIPTERI 1616
Cdd:cd19534     3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDG----GWQQRIRGDVEELF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1617 DARSMAVDGDAWI--VERARDERRRGFALDAAPAMRLLLVRTGDRSHRLIWTFHHILLDG--WSVplVLEEVFKRYSGGM 1692
Cdd:cd19534    77 RLEVVDLSSLAQAaaIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsWRI--LLEDLEAAYEQAL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 1693 QHEAAHRTAPRPHRDYVAWLRGAdAQSVER-----FWRRELGGfrEVTPLGIDRPPAGQRAssyRRFERALDEHTTARL 1766
Cdd:cd19534   155 AGEPIPLPSKTSFQTWAELLAEY-AQSPALleelaYWRELPAA--DYWGLPKDPEQTYGDA---RTVSFTLDEEETEAL 227
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 2258-2431 2.93e-09

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: 61.16  E-value: 2.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2258 DRIEDGSQLRLAFLSGDWVPIGMLDelrrAFPNVKLVGLGGATEAT---VWSNYfevdGIDPRWTSipyGRPIQNARYYV 2334
Cdd:cd17636   108 DGLYDLSSLRSSPAAPEWNDMATVD----TSPWGRKPGGYGQTEVMglaTFAAL----GGGAIGGA---GRPSPLVQVRI 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2335 LDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVpdpfsgepgARLYRTGDLARFFRDGNIEFLGRADSQVKIRG 2414
Cdd:cd17636   177 LDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR---------GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGA 247

                         170
                  ....*....|....*..
gi 260177242 2415 YRIECGEVEVALAQHPG 2431
Cdd:cd17636   248 ENIYPAEVERCLRQHPA 264
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 1991-2438 3.62e-09

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 61.94  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALCYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP 2070
Cdd:PRK05605   36 DLYDNAVARFGDRPALDFFGAT-TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 -------RWPLE----RVAAVLGTTRPVcivtderhlgaVEIAARQLGIEHVVSLD--------------------GDGK 2119
Cdd:PRK05605  115 lytahelEHPFEdhgaRVAIVWDKVAPT-----------VERLRRTTPLETIVSVNmiaampllqrlalrlpipalRKAR 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2120 D-----ADGNV---VIHGRRALADLADGNLPRAAgPHNMAYVIFTSGSTGTPKGVVERHSQVI-NLIE---WVNRtylVG 2187
Cdd:PRK05605  184 AaltgpAPGTVpweTLVDAAIGGDGSDVSHPRPT-PDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQgkaWVPG---LG 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2188 PSDRLLFVTSPSFDlsvydVFGM-LAAGGSIHIASEDDL----RSPERLAAeLGRGTITFWDSAPaalqqlvPYFDRIED 2262
Cdd:PRK05605  260 DGPERVLAALPMFH-----AYGLtLCLTLAVSIGGELVLlpapDIDLILDA-MKKHPPTWLPGVP-------PLYEKIAE 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2263 GSQLRLAFLSGdwvpigmldeLRRAFpnvklvglGGAT---EATV--WSNY---FEVDGIDPRWTS-IPYGRPIQNARY- 2332
Cdd:PRK05605  327 AAEERGVDLSG----------VRNAF--------SGAMalpVSTVelWEKLtggLLVEGYGLTETSpIIVGNPMSDDRRp 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2333 -YV-------LDRSGNP------CPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDpfsgepgarLYRTGDLARFFRDG 2398
Cdd:PRK05605  389 gYVgvpfpdtEVRIVDPedpdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG---------WFRTGDVVVMEEDG 459

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 260177242 2399 NIEFLGRADSQVKIRGYRIECGEVEVALAQHP--------GAQRGRGS 2438
Cdd:PRK05605  460 FIRIVDRIKELIITGGFNVYPAEVEEVLREHPgvedaavvGLPREDGS 507
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 983-1043 3.70e-09

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: 55.24  E-value: 3.70e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242  983 EEVLARIWERVLRVDA--VGREDNFF-ELGGDSILAIQVVAGAREV-DLKLTVRQIFTHPTLSSL 1043
Cdd:COG0236     7 EERLAEIIAEVLGVDPeeITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADL 71
PRK05857 PRK05857
fatty acid--CoA ligase;
463-965 4.26e-09

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 61.95  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  463 QTASDYPR---ERCLhhlfeEEARRVPDAVALDA--GSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVV 537
Cdd:PRK05857    7 QAMPQLPStvlDRVF-----EQARQQPEAIALRRcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  538 GILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIVLSAAGAE-------ERLGEGPWTVVRLDEDLGR----PDERDAA 606
Cdd:PRK05857   82 SVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKmassavpEALHSIPVIAVDIAAVTREsehsLDAASLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  607 PNDNVSAENLAYVMYTSGSTGKPKGVAVTHR------NVVRlVRGSSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGA 680
Cdd:PRK05857  162 GNADQGSEDPLAMIFTSGTTGEPKAVLLANRtffavpDILQ-KEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  681 RLVlfppespTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLDQLR-------GVRQLLAGGDVLSPKHVArvLLGLPAL 753
Cdd:PRK05857  241 LCV-------TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKsanatvpSLRLVGYGGSRAIAADVR--FIEATGV 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  754 RLINGYGPTEnttfTTCHDVSRGMGTGSV------PIGKPIANTHVYLLDEQ-MNPVPPNAV-----GELFTGGDGLARG 821
Cdd:PRK05857  312 RTAQVYGLSE----TGCTALCLPTDDGSIvkieagAVGRPYPGVDVYLAATDgIGPTAPGAGpsasfGTLWIKSPANMLG 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  822 YHERPDQTAERFVPDpfsgvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAR 901
Cdd:PRK05857  388 YWNNPERTAEVLIDG---------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEI 458

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242  902 EDrPGDKRLVAYVVGREAEVPRFSELRkfLLQRLPDH--------MIPAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK05857  459 PD-EEFGALVGLAVVASAELDESAARA--LKHTIAARfrresepmARPSTIVIVTDIPRTQSGKVMRASLAA 527
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 2014-2405 4.54e-09

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: 61.85  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGA--GPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVT 2091
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2092 DErhlgaveiaarqlGIEhVVSLDgdgkdadgNVVIHGRRALADLadgNLPRaagPHNMAYVIFTSGSTGTPKGVVERHS 2171
Cdd:cd05927    86 DA-------------GVK-VYSLE--------EFEKLGKKNKVPP---PPPK---PEDLATICYTSGTTGNPKGVMLTHG 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2172 QVINLI----EWVNRTYLVGPSDRLLfvtspSFdLS---VYD---VFGMLAAGGSIHIASED------DL---------- 2225
Cdd:cd05927   138 NIVSNVagvfKILEILNKINPTDVYI-----SY-LPlahIFErvvEALFLYHGAKIGFYSGDirllldDIkalkptvfpg 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2226 --RSPERL-----AAELGRGTITFW------DSAPAALQQLV----PYFDRIED-------GSQLRLAFLSGDWVPIGML 2281
Cdd:cd05927   212 vpRVLNRIydkifNKVQAKGPLKRKlfnfalNYKLAELRSGVvrasPFWDKLVFnkikqalGGNVRLMLTGSAPLSPEVL 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2282 DELRRAF--PNVKLVGL----GGATEATVW-SNYFEVDGIDP----RWTSIPygrpiqNARYYVLDrsgnPCPigvTGDL 2350
Cdd:cd05927   292 EFLRVALgcPVLEGYGQtectAGATLTLPGdTSVGHVGGPLPcaevKLVDVP------EMNYDAKD----PNP---RGEV 358

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260177242 2351 YIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGR 2405
Cdd:cd05927   359 CIRGPNVFSGYYKDPEKTAEALDEDGW--------LHTGDIGEWLPNGTLKIIDR 405
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
606-959 4.68e-09

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 62.29  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  606 APNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVV-RLVRGSSFATFGP-DQVFLMMApaafdasTFEIWG-------AL 676
Cdd:PRK06814  785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLaNRAQVAARIDFSPeDKVFNALP-------VFHSFGltgglvlPL 857

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  677 LHGARLVLFPpeSP-----TPEeigrVVREHGVTTLWLTAPLF--HAVADRGLDqLRGVRQLLAGGDVLSPKhVARVLLG 749
Cdd:PRK06814  858 LSGVKVFLYP--SPlhyriIPE----LIYDTNATILFGTDTFLngYARYAHPYD-FRSLRYVFAGAEKVKEE-TRQTWME 929

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  750 LPALRLINGYGPTEnttfttchdvsrgmgTGSVpigkpIA-NTHVY-----------LLDEQMNPVPP-NAVGELFTGGD 816
Cdd:PRK06814  930 KFGIRILEGYGVTE---------------TAPV-----IAlNTPMHnkagtvgrllpGIEYRLEPVPGiDEGGRLFVRGP 989

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  817 GLARGY--HERPdqtaerfvpdpfsGV---PGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVE--AALLQ 889
Cdd:PRK06814  990 NVMLGYlrAENP-------------GVlepPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEelAAELW 1056

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  890 HPALreAVVIAREDRPGDKRLVAYVVGREAEVPRFseLRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLD 959
Cdd:PRK06814 1057 PDAL--HAAVSIPDARKGERIILLTTASDATRAAF--LAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
prpE PRK10524
propionyl-CoA synthetase; Provisional
 618-965 4.85e-09

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 61.89  E-value: 4.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  618 YVMYTSGSTGKPKGVavtHRNV----VRLvrGSSFAT-FG--PDQVFlmmapaaFDAS--------TFEIWGALLHGARL 682
Cdd:PRK10524  237 YILYTSGTTGKPKGV---QRDTggyaVAL--ATSMDTiFGgkAGETF-------FCASdigwvvghSYIVYAPLLAGMAT 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  683 VLFP--PESPTPEEIGRVVREHGVTTLWlTAPlfhaVADRGLDQ----------LRGVRQLLAGGDVLSpKHVARVL--- 747
Cdd:PRK10524  305 IMYEglPTRPDAGIWWRIVEKYKVNRMF-SAP----TAIRVLKKqdpallrkhdLSSLRALFLAGEPLD-EPTASWIsea 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  748 LGLPalrLINGYGPTEnttfTTCHDVSRGMGTGSVPI-----GKPIANTHVYLLDEQM-NPVPPNAVGELFTGGDgLARG 821
Cdd:PRK10524  379 LGVP---VIDNYWQTE----TGWPILAIARGVEDRPTrlgspGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGP-LPPG 450

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  822 YHERPDQTAERFVPDPFSGVpGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAR 901
Cdd:PRK10524  451 CMQTVWGDDDRFVKTYWSLF-GRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGV 529

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242  902 EDRPGDKRLVAYVVGREAEVPRFSELRKFL---LQRLPDHMI-----PAAVVALDKLPLVPSGKLDRRALPA 965
Cdd:PRK10524  530 KDALKGQVAVAFVVPKDSDSLADREARLALekeIMALVDSQLgavarPARVWFVSALPKTRSGKLLRRAIQA 601
PRK09192 PRK09192
fatty acyl-AMP ligase;
497-980 6.85e-09

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 61.17  E-value: 6.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  497 VVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPL--------DPAYpSERLAFLAHDA 568
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLplpmgfggRESY-IAQLRGMLASA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  569 GVQIVLSAAGAEERLGE---GPWTVVRLD-EDLGRPDERDAAPNDNvSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVR 644
Cdd:PRK09192  128 QPAAIITPDELLPWVNEathGNPLLHVLShAWFKALPEADVALPRP-TPDDIAYLQYSSGSTRFPRGVIITHRALMANLR 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  645 GSSFATfgpdqvfLMMAPAAFDAStfeiWGALLHGARLV--LFPPES--------PTPEeigRVVREHgvttLWLT---- 710
Cdd:PRK09192  207 AISHDG-------LKVRPGDRCVS----WLPFYHDMGLVgfLLTPVAtqlsvdylPTRD---FARRPL----QWLDlisr 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  711 -------APLFhavadrGLD--QLRGVRQLLA------------GGDVLSPkHVARVL------LGLPALRLINGYGPTE 763
Cdd:PRK09192  269 nrgtisySPPF------GYElcARRVNSKDLAeldlscwrvagiGADMIRP-DVLHQFaeafapAGFDDKAFMPSYGLAE 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  764 NTTFTTCHDVSRGMGTGSVPI-------------------------GKPIANTHVYLLDEQMNPVPPNAVGELFTGGDGL 818
Cdd:PRK09192  342 ATLAVSFSPLGSGIVVEEVDRdrleyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSL 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  819 ARGYHERPDqTAERFVPDPFsgvpgarlYRTGDLArYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALR--EA 896
Cdd:PRK09192  422 MSGYFRDEE-SQDVLAADGW--------LDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDA 491

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  897 VVIAREDRPGDKrLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVAL---DKLPLVPSGKLDRRALPAPTLSGRSG 973
Cdd:PRK09192  492 AAFSIAQENGEK-IVLLVQCRISDEERRGQLIHALAALVRSEFGVEAAVELvppHSLPRTSSGKLSRAKAKKRYLSGAFA 570


                  ....*..
gi 260177242  974 PFVAPEG 980
Cdd:PRK09192  571 SLDVAAS 577
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 615-873 7.57e-09

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 61.19  E-value: 7.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRNVVRLVRG------SSFATFGPDQVFLMMAPAA--FDASTFEIWgaLLHGARLVLFP 686
Cdd:PLN02614  224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGvirllkSANAALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGFWR 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  687 PE-----------SPT-----PEEIGRV-------VREHGVTTLWL--------------------TAPLFHAVADRGLD 723
Cdd:PLN02614  302 GDvklliedlgelKPTifcavPRVLDRVysglqkkLSDGGFLKKFVfdsafsykfgnmkkgqshveASPLCDKLVFNKVK 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  724 QLRG--VRQLLAGGDVLSpKHVARVLLGLPALRLINGYGPTENT--TFTTCHDVSRGMGTgsvpIGKPIANTHVYLLD-E 798
Cdd:PLN02614  382 QGLGgnVRIILSGAAPLA-SHVESFLRVVACCHVLQGYGLTESCagTFVSLPDELDMLGT----VGPPVPNVDIRLESvP 456

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242  799 QMN--PVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDpfsgvpgarLYRTGDLARYLPNGDMEFLGRRDGQVKI 873
Cdd:PLN02614  457 EMEydALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDG---------WLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
2014-2423 8.60e-09

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 61.20  E-value: 8.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRwpLER----------VAAVLGT 2083
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE--LHRddhalaarntEPALVVT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2084 TRPVCivtdERHLGAVEIAARQLGIEHVVSLDGDGKDADGNVVihgrraladladgnlpraagphnmAYVIFTSGSTGTP 2163
Cdd:PRK06060  109 SDALR----DRFQPSRVAEAAELMSEAARVAPGGYEPMGGDAL------------------------AYATYTSGTTGPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2164 KGVVERHSQVINLIEWVNRTYL-VGPSDRLLFVTSPSFDLSVYD-VFGMLAAGGSIHIaseddlrSPERLAAELGRGTIT 2241
Cdd:PRK06060  161 KAAIHRHADPLTFVDAMCRKALrLTPEDTGLCSARMYFAYGLGNsVWFPLATGGSAVI-------NSAPVTPEAAAILSA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2242 FWDsaPAALQQLVPYFDRIEDG------SQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEAtvwSNYFEVDGID 2315
Cdd:PRK06060  234 RFG--PSVLYGVPNFFARVIDScspdsfRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEV---GQTFVSNRVD 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2316 pRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADpsqtaerfvPDPFSGEPGarLYRTGDLARFF 2395
Cdd:PRK06060  309 -EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEG--WLDTRDRVCID 376

                         410       420
                  ....*....|....*....|....*...
gi 260177242 2396 RDGNIEFLGRADSQVKIRGYRIECGEVE 2423
Cdd:PRK06060  377 SDGWVTYRCRADDTEVIGGVNVDPREVE 404
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1999-2430 1.22e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 60.40  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1999 RSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVA 2078
Cdd:PRK13383   47 RWPGRTAIIDDD-GALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2079 AVLGTTRPVCIVTDErhlgavEIAARQLGIEHVVsldgdgkdadgnVVIHGRRALADLADGNlPRAAGPHNMayVIFTSG 2158
Cdd:PRK13383  126 AALRAHHISTVVADN------EFAERIAGADDAV------------AVIDPATAGAEESGGR-PAVAAPGRI--VLLTSG 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2159 STGTPKGVvERHSQVINLIE-WV---NRTYLVGPSdRLLFVTSPSFDLSvydvFGML----AAGGSI----HIASEDDLR 2226
Cdd:PRK13383  185 TTGKPKGV-PRAPQLRSAVGvWVtilDRTRLRTGS-RISVAMPMFHGLG----LGMLmltiALGGTVlthrHFDAEAALA 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2227 SperlaAELGRGTItfWDSAPAALQQLVPYFDRIEDGS---QLRLAFLSGDWVPIGMLDELRRAFPNVkLVGLGGATEAT 2303
Cdd:PRK13383  259 Q-----ASLHRADA--FTAVPVVLARILELPPRVRARNplpQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVG 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2304 VWSNYFEVDGIDPRWTsipYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYyadpSQTAERFVPDPFSGepga 2383
Cdd:PRK13383  331 IGALATPADLRDAPET---VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY----TDGGGKAVVDGMTS---- 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 260177242 2384 rlyrTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK13383  400 ----TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHP 442
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 2014-2430 1.32e-08

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: 59.92  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGgayvpldprWPLERVAAVLGTTrpvcivtde 2093
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---------IPIVTVYATLGED--------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlgAVEIAARQLGIEHVVSldgDGKDADgnvvihgrraladladgnlpraagphnMAYVIFTSGSTGTPKGVVERHSQV 2173
Cdd:cd17639    68 ----ALIHSLNETECSAIFT---DGKPDD---------------------------LACIMYTSGSTGNPKGVMLTHGNL 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 INLI----EWVNRtyLVGPSDRLLfvtspS-------FDLSVYDVFgmLAAGGSIHIAS-----EDDLRSPERLAAELgR 2237
Cdd:cd17639   114 VAGIaglgDRVPE--LLGPDDRYL-----AylplahiFELAAENVC--LYRGGTIGYGSprtltDKSKRGCKGDLTEF-K 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2238 GTI-----TFWDS----------APAALQQLV------------------PYFDRI-------EDGSQLRlAFLSGDwvp 2277
Cdd:cd17639   184 PTLmvgvpAIWDTirkgvlaklnPMGGLKRTLfwtayqsklkalkegpgtPLLDELvfkkvraALGGRLR-YMLSGG--- 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2278 iGMLDELRRAFPNVKLVGLG---GATE----ATVwSNYFEvdgidprWTSIPYGRP----------IQNARYYvldrSGN 2340
Cdd:cd17639   260 -APLSADTQEFLNIVLCPVIqgyGLTEtcagGTV-QDPGD-------LETGRVGPPlpcceiklvdWEEGGYS----TDK 326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2341 PCPigvTGDLYIGGTCVSFGYYADPSQTAERFVPDpfsgepgaRLYRTGDLARFFRDGNIEFLGRADSQVKIR-GYRIEC 2419
Cdd:cd17639   327 PPP---RGEILIRGPNVFKGYYKNPEKTKEAFDGD--------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIAL 395

                         490
                  ....*....|.
gi 260177242 2420 GEVEVALAQHP 2430
Cdd:cd17639   396 EKLESIYRSNP 406
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 619-891 1.41e-08

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 60.24  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  619 VMYTSGSTGKPKGVAVTHRNVVRLV----------------------------------------RGSSFATFGPDQVFL 658
Cdd:PLN02861  225 IMYTSGTTGEPKGVILTNRAIIAEVlstdhllkvtdrvateedsyfsylplahvydqvietycisKGASIGFWQGDIRYL 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  659 MMAPAAFDASTF--------EIWGALLH------GARLVLFppESPTPEEIGRVvrEHGVTTLwLTAPLF-HAVADRGLD 723
Cdd:PLN02861  305 MEDVQALKPTIFcgvprvydRIYTGIMQkissggMLRKKLF--DFAYNYKLGNL--RKGLKQE-EASPRLdRLVFDKIKE 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  724 QLRG-VRQLLAGGDVLsPKHVARVLLGLPALRLINGYGPTENT--TFTTCHDVSRGMGTgsvpIGKPIANTHVYLLD--- 797
Cdd:PLN02861  380 GLGGrVRLLLSGAAPL-PRHVEEFLRVTSCSVLSQGYGLTESCggCFTSIANVFSMVGT----VGVPMTTIEARLESvpe 454

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  798 ---EQMNPVPPnavGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLARYLPNGDMEFLGRRDGQVKI- 873
Cdd:PLN02861  455 mgyDALSDVPR---GEICLRGNTLFSGYHKRQDLTEEVLIDGWF---------HTGDIGEWQPNGAMKIIDRKKNIFKLs 522

                         330
                  ....*....|....*...
gi 260177242  874 RGFRIELAEVEAALLQHP 891
Cdd:PLN02861  523 QGEYVAVENLENTYSRCP 540
PRK08315 PRK08315
AMP-binding domain protein; Validated
 1985-2433 1.48e-08

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 60.21  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1985 RERCIHELFESSVERSPGSVALCY-DGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGG 2063
Cdd:PRK08315   14 LEQTIGQLLDRTAARYPDREALVYrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2064 AYVPLDPRWPLERVAAVL---GTTRPVCI--VTDERHLGAV-----EIAARQLG---------IEHVVSLDGD---GKDA 2121
Cdd:PRK08315   94 ILVTINPAYRLSELEYALnqsGCKALIAAdgFKDSDYVAMLyelapELATCEPGqlqsarlpeLRRVIFLGDEkhpGMLN 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2122 DGNVVIHGRRA-LADLADgnlpRAAG-----PHNMAYvifTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLfv 2195
Cdd:PRK08315  174 FDELLALGRAVdDAELAA----RQATldpddPINIQY---TSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLC-- 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2196 tspsfdLSV--YDVFGM----LAA---GGSIHIASE--DDLRSPERLAAElgRGT---------ItfwdsapAALQQlvP 2255
Cdd:PRK08315  245 ------IPVplYHCFGMvlgnLACvthGATMVYPGEgfDPLATLAAVEEE--RCTalygvptmfI-------AELDH--P 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2256 YFDRIeDGSQLRLAFLSGDWVPIgmldEL-RRAfpnVKLVGLG------GATEATVWSNYFEV-DGIDPRWTSIpyGRPI 2327
Cdd:PRK08315  308 DFARF-DLSSLRTGIMAGSPCPI----EVmKRV---IDKMHMSevtiayGMTETSPVSTQTRTdDPLEKRVTTV--GRAL 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2328 QNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAErfVPDPfsgepgARLYRTGDLARFFRDGNIEFLGRA 2406
Cdd:PRK08315  378 PHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDA------DGWMHTGDLAVMDEEGYVNIVGRI 449

                         490       500       510
                  ....*....|....*....|....*....|..
gi 260177242 2407 DSQVkIRG----Y-RiecgEVEVALAQHPGAQ 2433
Cdd:PRK08315  450 KDMI-IRGgeniYpR----EIEEFLYTHPKIQ 476
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 2014-2430 2.07e-08

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: 59.40  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTR-PVCIVTD 2092
Cdd:cd05932     7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSEsKALFVGK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ERHLGAVEIAARQLGIEHVVSLDGDGKDADGNVVIhgrRALADLADGNLPRaaGPHNMAYVIFTSGSTGTPKGVVERHSQ 2172
Cdd:cd05932    87 LDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDL---IAQHPPLEERPTR--FPEQLATLIYTSGTTGQPKGVMLTFGS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2173 VINLIEWVNRTYLVGPSDRLLfvtspSFdLSVYDVFG-MLAAGGSIHIASEddLRSPERL---AAELGRGTITFWDSAP- 2247
Cdd:cd05932   162 FAWAAQAGIEHIGTEENDRML-----SY-LPLAHVTErVFVEGGSLYGGVL--VAFAESLdtfVEDVQRARPTLFFSVPr 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2248 ---------------AALQQL--VPYFDR-----IEDG---SQLRLAFLSGDWVPIGMLDELRRafpnvklVGLG----- 2297
Cdd:cd05932   234 lwtkfqqgvqdkipqQKLNLLlkIPVVNSlvkrkVLKGlglDQCRLAGCGSAPVPPALLEWYRS-------LGLNileay 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2298 GATEATVWSNYfevdgidprwtsipyGRPIQNARYYVldrsGNPCP-----IGVTGDLYIGGTCVSFGYYADPSQTAERF 2372
Cdd:cd05932   307 GMTENFAYSHL---------------NYPGRDKIGTV----GNAGPgvevrISEDGEILVRSPALMMGYYKDPEATAEAF 367

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2373 VPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKI-RGYRIECGEVEVALAQHP 2430
Cdd:cd05932   368 TADGF--------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHD 418
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 2014-2431 2.29e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 59.25  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDe 2093
Cdd:PRK13390   25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVAS- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 rhlGAVEIAARQLGIEHVVSLDGDGKdadgnvvIHGRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVverhsqv 2173
Cdd:PRK13390  104 ---AALDGLAAKVGADLPLRLSFGGE-------IDGFGSFEAALAGAGPRLTEQPCGAVMLYSSGTTGFPKGI------- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2174 inliewvnRTYLVG-----PSDRLLFVTSPSFDLSVYDVF---------------GML-AAGGSIHIA----SEDDLRSP 2228
Cdd:PRK13390  167 --------QPDLPGrdvdaPGDPIVAIARAFYDISESDIYyssapiyhaaplrwcSMVhALGGTVVLAkrfdAQATLGHV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2229 ERLaaelgrgTITFWDSAPAALQQLVPYFDRIE---DGSQLRLAFLSGDWVPI----GMLDELrrafpnvklvglggatE 2301
Cdd:PRK13390  239 ERY-------RITVTQMVPTMFVRLLKLDADVRtryDVSSLRAVIHAAAPCPVdvkhAMIDWL----------------G 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2302 ATVWSNY--FEVDG---ID-PRWTSIP--YGRPIQNArYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAErfv 2373
Cdd:PRK13390  296 PIVYEYYssTEAHGmtfIDsPDWLAHPgsVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--- 371

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2374 pdpfSGEPGARLYRT-GDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK13390  372 ----AQHPAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPA 426
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1065-1495 2.34e-08

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: 58.92  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1065 PLTPIQR--WFLSGEPAAPHHFNQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMWRARGMPSgGPVPYEVV 1142
Cdd:cd19533     3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPY-TPVPIRHI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1143 DLSELPgEERRAALEARAAEAQASLDLTDGPILRVVQFRLGpgePDRLLVV--VHHLAVDVVSWGILLADLATAHRQLVE 1220
Cdd:cd19533    82 DLSGDP-DPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLG---DNRHFWYqrVHHIVMDGFSFALFGQRVAEIYTALLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1221 GEIVRlPSKTTSLRRWGERLLATVD-EVVAAELPFW-EALDGqgvRPLPRGCEPAEDREGDAQTVEVWLGGPETEALLGR 1298
Cdd:cd19533   158 GRPAP-PAPFGSFLDLVEEEQAYRQsERFERDRAFWtEQFED---LPEPVSLARRAPGRSLAFLRRTAELPPELTRTLLE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1299 VGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGReelfpdIEVA--RTVGWFTTIHPVVLPGRPQSAGARL-KAV 1375
Cdd:cd19533   234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR------LGAAarQTPGMVANTLPLRLTVDPQQTFAELvAQV 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1376 KEAIRRVPKHG-IGYG-ILRYLGSDEVVTRLARlpapeVAFNYLgRLDRALPKDGP-FVMAPEAAGPS------VSPRGK 1446
Cdd:cd19533   308 SRELRSLLRHQrYRYEdLRRDLGLTGELHPLFG-----PTVNYM-PFDYGLDFGGVvGLTHNLSSGPTndlsifVYDRDD 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 260177242 1447 RShalqtmvvaepqGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIAH 1495
Cdd:cd19533   382 ES------------GLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 2146-2439 2.48e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 59.44  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2146 GPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSP--SFDLSVYDVFGMLAAggsIHIASED 2223
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPfhAYGFNSCTLFPLLSG---VPVVFAY 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2224 DLRSPERLAAELGRGTITFWDSAPAALQQLVPYFDRIEDG-SQLRLAFLSGDWVPIGMLDELRRAFPNVKLVGLGGATEA 2302
Cdd:PRK06334  258 NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESClPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTEC 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2303 tvwSNYFEVDGIDPRWTSIPYGRPIQNARYYVLDRSGN-PCPIGVTGDLYIGGTCVSFGYY-ADPSQTaerfvpdpFSGE 2380
Cdd:PRK06334  338 ---SPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLgEDFGQG--------FVEL 406

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2381 PGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQRGRGSG 2439
Cdd:PRK06334  407 GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADHAG 465
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 615-931 2.58e-08

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 59.44  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  615 NLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSSF------ATFGPDQVFLMMAPAA--FDASTFEIW---GALL---HGA 680
Cdd:PLN02430  221 DICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLfmeqfeDKMTHDDVYLSFLPLAhiLDRMIEEYFfrkGASVgyyHGD 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  681 RLVL---FPPESPT-----P-------EEIGRVVRE------------HGVTTLWLTA--------PLFHAVADRGL-DQ 724
Cdd:PLN02430  301 LNALrddLMELKPTllagvPrvferihEGIQKALQElnprrrlifnalYKYKLAWMNRgyshkkasPMADFLAFRKVkAK 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  725 LRG-VRQLLAGGDVLSPKhVARVLLGLPALRLINGYGPTEnttftTCHDVSRG-------MGTgsvpIGKPIANTHVYLL 796
Cdd:PLN02430  381 LGGrLRLLISGGAPLSTE-IEEFLRVTSCAFVVQGYGLTE-----TLGPTTLGfpdemcmLGT----VGAPAVYNELRLE 450

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  797 D-EQM--NPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLARYLPNGDMEFLGRRDGQVKI 873
Cdd:PLN02430  451 EvPEMgyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWF---------HTGDIGEILPNGVLKIIDRKKNLIKL 521

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242  874 -RGFRIELAEVEAALLQHPALREAVVIAREDRPgdkRLVAYVVGREAEVPRFSELRKFL 931
Cdd:PLN02430  522 sQGEYVALEYLENVYGQNPIVEDIWVYGDSFKS---MLVAVVVPNEENTNKWAKDNGFT 577
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2001-2430 3.22e-08

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 58.85  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVALcYDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGgaYVPLDPRWPLER--VA 2078
Cdd:PRK10946   37 SDAIAV-ICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRseLN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2079 AVLGTTRPVCIVTDERH-LGAVEIAARQLGIEH----VVSLDGDGkdadgnvvihGRRALAD-LADGNLPRAAGPHNMAY 2152
Cdd:PRK10946  114 AYASQIEPALLIADRQHaLFSDDDFLNTLVAEHsslrVVLLLNDD----------GEHSLDDaINHPAEDFTATPSPADE 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2153 VIF---TSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLL--FVTSPSFDLSVYDVFGMLAAGGSIHIASEDdlrS 2227
Cdd:PRK10946  184 VAFfqlSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLcaLPAAHNYPMSSPGALGVFLAGGTVVLAPDP---S 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 PERLAAELGRGTITFWDSAPAA----LQQLVpyfdriEDGSQLRLAFLSGDWVPIGMLDE-LRRAFPNV---KLVGLGGA 2299
Cdd:PRK10946  261 ATLCFPLIEKHQVNVTALVPPAvslwLQAIA------EGGSRAQLASLKLLQVGGARLSEtLARRIPAElgcQLQQVFGM 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2300 TEATVwsNYFEVDgiDPRWTSI-PYGRPIQNA-RYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPF 2377
Cdd:PRK10946  335 AEGLV--NYTRLD--DSDERIFtTQGRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF 410

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2378 sgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK10946  411 --------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHP 455
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 2015-2406 4.21e-08

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: 58.59  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRP-VCIVTDE 2093
Cdd:cd17641    13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGArVVIAEDE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHLGAV-EIAARQLGIEHVVSLD-------GDGKDADGNVVIHGRRALADLADG---NLPRAAGPHNMAYVIFTSGSTGT 2162
Cdd:cd17641    93 EQVDKLlEIADRIPSVRYVIYCDprgmrkyDDPRLISFEDVVALGRALDRRDPGlyeREVAAGKGEDVAVLCTTSGTTGK 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2163 PKGVVERHSQVINLIEWVNRTYLVGPSDRLL-FVTSPSFDLSVYDVFGMLAAGGSIHIASE-----DDLR--------SP 2228
Cdd:cd17641   173 PKLAMLSHGNFLGHCAAYLAADPLGPGDEYVsVLPLPWIGEQMYSVGQALVCGFIVNFPEEpetmmEDLReigptfvlLP 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2229 ERL----AAELgrgTITFWDSAP-------AALQQLVPYFDRIEDGSQ----LRLAFLSGDWVPIGMLDElRRAFPNVKL 2293
Cdd:cd17641   253 PRVwegiAADV---RARMMDATPfkrfmfeLGMKLGLRALDRGKRGRPvslwLRLASWLADALLFRPLRD-RLGFSRLRS 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2294 VGLGGATEATVWSNYFEVDGIDPRWTsipYGRpIQNARYYVLDRSGN--------PCP-----IGVTGDLYIGGTCVSFG 2360
Cdd:cd17641   329 AATGGAALGPDTFRFFHAIGVPLKQL---YGQ-TELAGAYTVHRDGDvdpdtvgvPFPgtevrIDEVGEILVRSPGVFVG 404

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 260177242 2361 YYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRA 2406
Cdd:cd17641   405 YYKNPEATAEDFDEDGW--------LHTGDAGYFKENGHLVVIDRA 442
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 2014-2391 4.92e-08

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: 58.24  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLR-GLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTD 2092
Cdd:cd17632    68 ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ERHLG-AVEIAARQLGIEHVVSLDGDGK-DADGNVVIHGRRALADLA------------DGNLPRAA------GPHNMAY 2152
Cdd:cd17632   148 AEHLDlAVEAVLEGGTPPRLVVFDHRPEvDAHRAALESARERLAAVGipvttltliavrGRDLPPAPlfrpepDDDPLAL 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2153 VIFTSGSTGTPKGVVERHSQVINLieWVNRTYLVGPSDR---LLFVTSPSFDLSVYDVFGMLAAGGSIHIASEDDLRS-- 2227
Cdd:cd17632   228 LIYTSGSTGTPKGAMYTERLVATF--WLKVSSIQDIRPPasiTLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTlf 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2228 -------P--------------ERLAAELGRGTITFWDSAPAALQQLVPYFDRIEdGSQLRLAFLSGdwVPIGmlDELrR 2286
Cdd:cd17632   306 ddlalvrPtelflvprvcdmlfQRYQAELDRRSVAGADAETLAERVKAELRERVL-GGRLLAAVCGS--APLS--AEM-K 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2287 AFP----NVKLVGLGGATEATVWSnyfeVDG-------IDPRWTSIPygrpiqNARYYVLDRsgnPCPigvTGDLYIGGT 2355
Cdd:cd17632   380 AFMesllDLDLHDGYGSTEAGAVI----LDGvivrppvLDYKLVDVP------ELGYFRTDR---PHP---RGELLVKTD 443

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 260177242 2356 CVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDL 2391
Cdd:cd17632   444 TLFPGYYKRPEVTAEVFDEDGF--------YRTGDV 471
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 2151-2428 6.99e-08

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 58.40  E-value: 6.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2151 AYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSP--SFDLSVYDVFGMLAAGGSIHIASEDDLRSP 2228
Cdd:PRK08633  785 ATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWLPLLEGIKVVYHPDPTDALGI 864

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2229 ERLAAELGR----GTITFWdSAPAALQQLVPyfdriEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATEAT- 2303
Cdd:PRK08633  865 AKLVAKHRAtillGTPTFL-RLYLRNKKLHP-----LMFASLRLVVAGAEKLKPEVADAFEEKF-GIRILEGYGATETSp 937

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2304 VWS----NYFEVDG---IDPRWTSIpyGRPIQNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAErFVPD 2375
Cdd:PRK08633  938 VASvnlpDVLAADFkrqTGSKEGSV--GMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD 1014

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2376 PfsgePGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQ 2428
Cdd:PRK08633 1015 I----DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK 1063
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1065-1494 1.17e-07

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: 56.69  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1065 PLTPIQRWFLSgepaapHHFNQAVLLALRDAWVpKHVDA---------AVGAVIRHHDALRLRFVAEDGMWRARGMPSGG 1135
Cdd:cd19536     3 PLSSLQEGMLF------HSLLNPGGSVYLHNYT-YTVGRrlnldllleALQVLIDRHDILRTSFIEDGLGQPVQVVHRQA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1136 PVPYEVVDLSELPgEERRAALEARAAEAQASLDLTDGPILRVVQFRLGPGEPDRLLVVVHHLAVDVVSWGILLADLATAH 1215
Cdd:cd19536    76 QVPVTELDLTPLE-EQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1216 RQLVEGEIVRLPsKTTSLRRWGERLLATVDEvvAAELPFW-EALDGQGVRPLPrgcEPAEDREGDAQTVEVWLGGPETEA 1294
Cdd:cd19536   155 NQLLEYKPLSLP-PAQPYRDFVAHERASIQQ--AASERYWrEYLAGATLATLP---ALSEAVGGGPEQDSELLVSVPLPV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1295 LLGRVGEAYRTRADEVILAALAGALTEWAGGEAAYVAVEGHGREELFPDIEvaRTVGWFTTihpvVLPGRPQSAGAR--- 1371
Cdd:cd19536   229 RSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLN----TLPLRVTLSEETved 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1372 -LKAVKEAIRRVPKHgiGYGILRYLGSDEvvtrlARLPAPEVAFNYlgrldralpKDGPFVMAPEAAGPSVSPRG----- 1445
Cdd:cd19536   303 lLKRAQEQELESLSH--EQVPLADIQRCS-----EGEPLFDSIVNF---------RHFDLDFGLPEWGSDEGMRRgllfs 366

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 260177242 1446 --KRSHALQTMVVAEPQGLRTRFAFQPKRHSHEEIARLAARYGQLLEELIA 1494
Cdd:cd19536   367 efKSNYDVNLSVLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELAT 417
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 587-866 1.33e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 57.29  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  587 PWTVVrldEDLGRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSS------FATFGPDQVFLMM 660
Cdd:PTZ00216  240 AWTDV---VAKGHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEdrlndlIGPPEEDETYCSY 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  661 APAA--FDASTFEIW---GALL---------------HGaRLVLFPP-----------------ES--PTPEEIGRVVRE 701
Cdd:PTZ00216  317 LPLAhiMEFGVTNIFlarGALIgfgsprtltdtfarpHG-DLTEFRPvfligvprifdtikkavEAklPPVGSLKRRVFD 395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  702 H-----------GVTTLWLTAPLFHAVadRGLdqLRG-VRQLLAGGDVLSPK--HVARVLLGlpalRLINGYGPTEnttf 767
Cdd:PTZ00216  396 HayqsrlralkeGKDTPYWNEKVFSAP--RAV--LGGrVRAMLSGGGPLSAAtqEFVNVVFG----MVIQGWGLTE---- 463

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  768 TTCH-DVSRGMGTGSVPIGKPIANTHVYLLD--EQMNPVPPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpga 844
Cdd:PTZ00216  464 TVCCgGIQRTGDLEPNAVGQLLKGVEMKLLDteEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGW------ 537

                         330       340
                  ....*....|....*....|..
gi 260177242  845 rlYRTGDLARYLPNGDMEFLGR 866
Cdd:PTZ00216  538 --FHTGDVGSIAANGTLRIIGR 557
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 1987-2170 1.58e-07

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 56.81  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1987 RCIHELFESSVERSPGSVALCYDGVPP----LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTG 2062
Cdd:PRK08180   39 RRLTDRLVHWAQEAPDRVFLAERGADGgwrrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2063 GAYVPLDPRWPL-----ERVAAVLGTTRPVCIVTDERHLGAVEIAA-RQLGIEHVVSldgDGKDADGNVVihgrrALADL 2136
Cdd:PRK08180  119 VPYAPVSPAYSLvsqdfGKLRHVLELLTPGLVFADDGAAFARALAAvVPADVEVVAV---RGAVPGRAAT-----PFAAL 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 260177242 2137 ADGNLPRAA-------GPHNMAYVIFTSGSTGTPKGVVERH 2170
Cdd:PRK08180  191 LATPPTAAVdaahaavGPDTIAKFLFTSGSTGLPKAVINTH 231
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 2147-2436 1.61e-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: 56.73  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2147 PHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLFVTSPSFDLsvydvfGMLAAGGSIHIASEDDLR 2226
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDM------GLIAFHLAPLIAGMNQYL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2227 SPERL----------AAELGRGTITfwdSAPA-----ALQQLVPYFDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFPNV 2291
Cdd:cd05908   179 MPTRLfirrpilwlkKASEHKATIV---SSPNfgykyFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKY 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2292 KL-----VGLGGATEATVW-------SNYF----------------EVDGIDPR-WTSIPYGRPIQNARYYVLDRSGNPC 2342
Cdd:cd05908   256 GLkrnaiLPVYGLAEASVGaslpkaqSPFKtitlgrrhvthgepepEVDKKDSEcLTFVEVGKPIDETDIRICDEDNKIL 335

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2343 PIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLArFFRDGNIEFLGRADSQVKIRGYRIECGEV 2422
Cdd:cd05908   336 PDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW--------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDI 406

                         330
                  ....*....|....
gi 260177242 2423 EVALAQHPGAQRGR 2436
Cdd:cd05908   407 ERIAEELEGVELGR 420
PRK03584 PRK03584
acetoacetate--CoA ligase;
618-958 1.79e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 56.73  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  618 YVMYTSGSTGKPK-------GVAVTHRNVVRLvrgssFATFGPDQVFL-------MMapaafdastfeiW----GALLHG 679
Cdd:PRK03584  267 WILYSSGTTGLPKcivhghgGILLEHLKELGL-----HCDLGPGDRFFwyttcgwMM------------WnwlvSGLLVG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  680 ARLVLF--PPESPTPEEIGRVVREHGVTTLWLTAPLFHAVADRGLD-----QLRGVRQLLAGGDVLSPK-------HVAr 745
Cdd:PRK03584  330 ATLVLYdgSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVpgethDLSALRTIGSTGSPLPPEgfdwvyeHVK- 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  746 vllglPALRLINGYGPTEnttFTTCHdvsrgmgTGSVPIgKPI-----------ANTHVYllDEQMNPVpPNAVGEL--- 811
Cdd:PRK03584  409 -----ADVWLASISGGTD---ICSCF-------VGGNPL-LPVyrgeiqcrglgMAVEAW--DEDGRPV-VGEVGELvct 469

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  812 ---------FTGGDGLARgYHERpdqtaerfvpdPFSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAE 882
Cdd:PRK03584  470 kpfpsmplgFWNDPDGSR-YRDA-----------YFDTFPG--VWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAE 535

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  883 VEAALLQHPALREAVVIAREDRPGDKRLVAYVVGREaEVPRFSELRKFLLQRL-----PDHmIPAAVVALDKLPLVPSGK 957
Cdd:PRK03584  536 IYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAE-GVTLDDALRARIRTTIrtnlsPRH-VPDKIIAVPDIPRTLSGK 613


                  .
gi 260177242  958 L 958
Cdd:PRK03584  614 K 614
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
613-959 2.02e-07

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 56.64  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  613 AENLAYVMYTSGSTGKPKGVAVTHRNV---VRLVRgsSFATFGPDQVFlMMAPAAFDAS--TFEIWGALLHGARLVLFPp 687
Cdd:PRK08043  364 PEDAALILFTSGSEGHPKGVVHSHKSLlanVEQIK--TIADFTPNDRF-MSALPLFHSFglTVGLFTPLLTGAEVFLYP- 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  688 eSP-----TPEeigrVVREHGVTTLWLTAPLF--HAVADRGLDQLRgVRQLLAGGDVLSPkHVARVLLGLPALRLINGYG 760
Cdd:PRK08043  440 -SPlhyriVPE----LVYDRNCTVLFGTSTFLgnYARFANPYDFAR-LRYVVAGAEKLQE-STKQLWQDKFGLRILEGYG 512

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  761 PTEnttfttCHDVsrgmgtgsVPIGKPIA---NTHVYLL---DEQMNPVPP-NAVGELFTGGDGLARGYH--ERPDQTaE 831
Cdd:PRK08043  513 VTE------CAPV--------VSINVPMAakpGTVGRILpgmDARLLSVPGiEQGGRLQLKGPNIMNGYLrvEKPGVL-E 577

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  832 RFVPDPFSGVPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGDKRLV 911
Cdd:PRK08043  578 VPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALV 657

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 260177242  912 AYVVgrEAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLD 959
Cdd:PRK08043  658 LFTT--DSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 618-915 2.14e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 56.29  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  618 YVMYTSGSTGKPKGVAVTHRNVVRLVRGSSFATFGPDQVFLMMAPAAFDASTFE--IWGALLHGARLVLFppesptpeEI 695
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHgfLYGSLSLGNTFVMF--------EG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  696 GRVVREHGVTTLW-------LTAPLFHAVADRGLDQ-------------LRGVRQLLAGGDVLS---PKHVARVLlglpA 752
Cdd:PTZ00237  330 GIIKNKHIEDDLWntiekhkVTHTLTLPKTIRYLIKtdpeatiirskydLSNLKEIWCGGEVIEesiPEYIENKL----K 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  753 LRLINGYGPTEN--TTFTTCHDVSRGMGTgsvpIGKPIANTHVYLLDEQMNPVPPNAVGEL---FTGGDGLARGYHERPD 827
Cdd:PTZ00237  406 IKSSRGYGQTEIgiTYLYCYGHINIPYNA----TGVPSIFIKPSILSEDGKELNVNEIGEVafkLPMPPSFATTFYKNDE 481

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  828 QTAERFvpdpfSGVPGarLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIAREDRPGD 907
Cdd:PTZ00237  482 KFKQLF-----SKFPG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCY 554


                  ....*...
gi 260177242  908 KRLVAYVV 915
Cdd:PTZ00237  555 NVPIGLLV 562
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 2153-2431 2.22e-07

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: 55.35  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2153 VIFTSGSTGTPKGVVERHSQVINLIEWVNRTYLVGPSDRLLfVTSPSFDLS-VYDVFGMLAAGGSIHIASEDDlrsPERL 2231
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYL-NMLPLFHIAgLNLALATFHAGGANVVMEKFD---PAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2232 AAELGRGTITFWDSAPAALQQLVpyfDRIED-GSQLR-LAFLSGDWVP--IGMLDELRRAfpnvKLVGLGGATEA---TV 2304
Cdd:cd17637    81 LELIEEEKVTLMGSFPPILSNLL---DAAEKsGVDLSsLRHVLGLDAPetIQRFEETTGA----TFWSLYGQTETsglVT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2305 WSNYFEVDGidprwtsiPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFvpdpfsgepgaR 2384
Cdd:cd17637   154 LSPYRERPG--------SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-----------R 214

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 260177242 2385 --LYRTGDLARFFRDGNIEFLGRADSQ--VKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd17637   215 ngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPA 265
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 2001-2430 2.31e-07

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: 56.00  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2001 PGSVAL--CYDGVPpLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVA 2078
Cdd:cd17642    31 PGTIAFtdAHTGVN-YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2079 AVLGTTRPVCIVTDERHLGAVEIAARQLG-IEHVVSLDGD----GKDADGNVVIHGRRALADLADGNLPRAAGPHNMAYV 2153
Cdd:cd17642   110 HSLNISKPTIVFCSKKGLQKVLNVQKKLKiIKTIIILDSKedykGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALI 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2154 IFTSGSTGTPKGVVERHSQ-VINLIEWVNRTYLVGPSDRLLFVTSPSFdlsvYDVFGMLAAGGSIHIASEDDLRSpeRLA 2232
Cdd:cd17642   190 MNSSGSTGLPKGVQLTHKNiVARFSHARDPIFGNQIIPDTAILTVIPF----HHGFGMFTTLGYLICGFRVVLMY--KFE 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2233 AELGRGTITFWDSAPAAL-QQLVPYFDRIE-----DGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLG-GATEATVw 2305
Cdd:cd17642   264 EELFLRSLQDYKVQSALLvPTLFAFFAKSTlvdkyDLSNLHEIASGGAPLSKEVGEAVAKRF-KLPGIRQGyGLTETTS- 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2306 SNYFEVDGiDPRWTSIPYGRPIQNARYYVLDrSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarl 2385
Cdd:cd17642   342 AILITPEG-DDKPGAVGKVVPFFYAKVVDLD-TGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW-------- 411

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 260177242 2386 YRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd17642   412 LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHP 456
PRK05857 PRK05857
fatty acid--CoA ligase;
1998-2167 3.31e-07

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 55.78  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1998 ERSPGSVAL--CyDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLE 2075
Cdd:PRK05857   25 RQQPEAIALrrC-DGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2076 RVAAVLGTTRPVCIVTDERhlGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHGRRalaDLADGNLprAAGPHNMAYVIF 2155
Cdd:PRK05857  104 AIERFCQITDPAAALVAPG--SKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDA---ASLAGNA--DQGSEDPLAMIF 176

                         170
                  ....*....|..
gi 260177242 2156 TSGSTGTPKGVV 2167
Cdd:PRK05857  177 TSGTTGEPKAVL 188
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 478-963 3.83e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 55.34  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  478 FEEEARRV-PDAVALDAGSNVVSYGELNRRADKLAHMLRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAY 556
Cdd:PRK08162   23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  557 PSERLAF-LAH-DAGVQIV----LSAAGAEERLGEGPWTVVRLDED-------------------LGRPDERDAAPNDNV 611
Cdd:PRK08162  103 DAASIAFmLRHgEAKVLIVdtefAEVAREALALLPGPKPLVIDVDDpeypggrfigaldyeaflaSGDPDFAWTLPADEW 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  612 SAENLAYvmyTSGSTGKPKGVAVTHRNVVRLVRGSSFAT-FGPDQVFLMMAPaafdasTFEIWG-------ALLHGARLV 683
Cdd:PRK08162  183 DAIALNY---TSGTTGNPKGVVYHHRGAYLNALSNILAWgMPKHPVYLWTLP------MFHCNGwcfpwtvAARAGTNVC 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  684 LfppESPTPEEIGRVVREHGVTTLwLTAPLFHAV-------ADRGLDQLrgVRQLLAGgdvlSPKHVArVLLGLPA--LR 754
Cdd:PRK08162  254 L---RKVDPKLIFDLIREHGVTHY-CGAPIVLSAlinapaeWRAGIDHP--VHAMVAG----AAPPAA-VIAKMEEigFD 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  755 LINGYGPTEntTF---TTC-----------HDVSRGMGTGSVPIgkpIANTHVYLLD-EQMNPVPPNA--VGELFTGGDG 817
Cdd:PRK08162  323 LTHVYGLTE--TYgpaTVCawqpewdalplDERAQLKARQGVRY---PLQEGVTVLDpDTMQPVPADGetIGEIMFRGNI 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  818 LARGYHERPDQTAERFVPDPFsgvpgarlyRTGDLARYLPngdmeflgrrDGQVKIR----------GFRIELAEVEAAL 887
Cdd:PRK08162  398 VMKGYLKNPKATEEAFAGGWF---------HTGDLAVLHP----------DGYIKIKdrskdiiisgGENISSIEVEDVL 458

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242  888 LQHPALREAVVIAREDRPGDKRLVAYVVGREAEVPRFSELRKFLLQRLPDHMIPAAVVaLDKLPLVPSGKLDRRAL 963
Cdd:PRK08162  459 YRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 495-637 6.39e-07

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: 54.66  E-value: 6.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  495 SNVVSYGELNRRADKLAHMLRLK-GVGTETRVGLCLERSVELVVGILGVLKAGGAYVPLDPAYPSERLAFLAHDAGVQIV 573
Cdd:cd05905    12 ATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  574 LSA----------------AGAEERLGEGPWTVVRLDEDL-GRPDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTH 636
Cdd:cd05905    92 LTVeaclkglpkkllksktAAEIAKKKGWPKILDFVKIPKsKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSH 171


                  .
gi 260177242  637 R 637
Cdd:cd05905   172 S 172
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 731-879 7.66e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 54.72  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  731 LLAGGDVLSPKhVARVLLGLPALRLINGYGPTENTTFTTCHDVsRGMGTGSvpIGKPIANTHVYLLDE----QMNPVPPN 806
Cdd:PTZ00342  466 ILNGGGKLSPK-IAEELSVLLNVNYYQGYGLTETTGPIFVQHA-DDNNTES--IGGPISPNTKYKVRTwetyKATDTLPK 541

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260177242  807 avGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYRTGDLARYLPNGDMEFLGRRDGQVKI-RGFRIE 879
Cdd:PTZ00342  542 --GELLIKSDSIFSGYFLEKEQTKNAFTEDGY--------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 2014-2166 8.44e-07

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 54.14  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTDE 2093
Cdd:PRK08276   12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2094 RHLGAVE--IAARQLGIEHVVSLDGDgkdadgnvvIHGRRALADLADGNLP-----RAAGPHnMAYvifTSGSTGTPKGV 2166
Cdd:PRK08276   92 ALADTAAelAAELPAGVPLLLVVAGP---------VPGFRSYEEALAAQPDtpiadETAGAD-MLY---SSGTTGRPKGI 158
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 2014-2185 1.12e-06

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 54.18  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAgPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPrwPL-----ERVAAVLGTTRPVC 2088
Cdd:PRK05850   36 LTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSV--PQggahdERVSAVLRDTSPSV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2089 IVTDERHLGAVE--IAARQLGIE-HVVSLDGDGKDADGNVvihgrralaDLADGNLPraagphNMAYVIFTSGSTGTPKG 2165
Cdd:PRK05850  113 VLTTSAVVDDVTeyVAPQPGQSApPVIEVDLLDLDSPRGS---------DARPRDLP------STAYLQYTSGSTRTPAG 177

                         170       180
                  ....*....|....*....|
gi 260177242 2166 VVERHSQVINLIEWVNRTYL 2185
Cdd:PRK05850  178 VMVSHRNVIANFEQLMSDYF 197
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 2324-2431 1.25e-06

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 54.00  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2324 GRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFL 2403
Cdd:PRK05677  381 GIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW--------LKTGDIALIQEDGYMRIV 452

                          90       100
                  ....*....|....*....|....*...
gi 260177242 2404 GRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK05677  453 DRKKDMILVSGFNVYPNELEDVLAALPG 480
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 2015-2394 1.78e-06

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: 53.20  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPL-----ERVAAVLGTTRPVCI 2089
Cdd:cd05921    27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFELLKPGLV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2090 VTD-----ERHLGAVEIaarqLGIEHVVSldgdGKDADGNVVIHGRRALADLADGNLPRA---AGPHNMAYVIFTSGSTG 2161
Cdd:cd05921   107 FAQdaapfARALAAIFP----LGTPLVVS----RNAVAGRGAISFAELAATPPTAAVDAAfaaVGPDTVAKFLFTSGSTG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2162 TPKGVVERHSQVINLIEWVNRTYLV-GPSDRLLFVTSP-SFDLSVYDVFGM-LAAGGSIHIaseDDLR-SPERLA---AE 2234
Cdd:cd05921   179 LPKAVINTQRMLCANQAMLEQTYPFfGEEPPVLVDWLPwNHTFGGNHNFNLvLYNGGTLYI---DDGKpMPGGFEetlRN 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2235 LGRGTITFWDSAPAALQQLVPYfdrIEDGSQLRlaflsgdwvpigmldelRRAFPNVKLVGLGGATEA-TVWSNYFEVdG 2313
Cdd:cd05921   256 LREISPTVYFNVPAGWEMLVAA---LEKDEALR-----------------RRFFKRLKLMFYAGAGLSqDVWDRLQAL-A 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2314 IDPRWTSIPYG--------RPIQNARYYVLDRSGN---PCPiGVT------GDLYIG---GTCVSFGYYADPSQTAERFV 2373
Cdd:cd05921   315 VATVGERIPMMaglgatetAPTATFTHWPTERSGLiglPAP-GTElklvpsGGKYEVrvkGPNVTPGYWRQPELTAQAFD 393

                         410       420
                  ....*....|....*....|.
gi 260177242 2374 PDPFsgepgarlYRTGDLARF 2394
Cdd:cd05921   394 EEGF--------YCLGDAAKL 406
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1062-1325 4.31e-06

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: 51.71  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1062 GEMPLTPIQR--WFLS--GEPAAPHHfnQAVLLALRDAWVPKHVDAAVGAVIRHHDALRLRFVAEDGMWRARGM-PSGGP 1136
Cdd:cd19546     3 DEVPATAGQLrtWLLArlDEETRGRH--LSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILdADAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1137 VPYEVVDLSE--LPGEERRAALEaraaeaqaSLDLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATA 1214
Cdd:cd19546    81 PELPVVPATEeeLPALLADRAAH--------LFDLTRETPWRCTLFALSDTE-HVLLLVVHRIAADDESLDVLVRDLAAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1215 HRQLVEG---EIVRLPSKTTSLRRWGERLLATVDE---VVAAELPFW-EALDGqgvrpLPRGCEPAEDREGD------AQ 1281
Cdd:cd19546   152 YGARREGrapERAPLPLQFADYALWERELLAGEDDrdsLIGDQIAYWrDALAG-----APDELELPTDRPRPvlpsrrAG 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 260177242 1282 TVEVWLGGpETEALLGRVGEAYRTRADEVILAALAGALTEWAGG 1325
Cdd:cd19546   227 AVPLRLDA-EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAG 269
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
1566-1789 6.41e-06

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 51.25  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1566 LEGALDFDRLQQAWDETLGAHPALRA--SFLWEGVPEplqvvrrlvRIPTERIDARSMAVDGDawiveraRDERRRGFAL 1643
Cdd:PRK09294   30 LRGVLDIDALSDAFDALLRAHPVLAAhlEQDSDGGWE---------LVADDLLHPGIVVVDGD-------AARPLPELQL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1644 DAAPAMRLLLVRTGDRSHRLIWTFHHILLDGWSVPLVLEEVFKRYSGGMQHEAAHRT----APRPHRDYVAwLRGADAQS 1719
Cdd:PRK09294   94 DQGVSLLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDVVTTGDPGPIrpqpAPQSLEAVLA-QRGIRRQA 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242 1720 VERFWRR-------ELGGFREVTPLGIDRPPAGQRASSYRrferaLDEHTTARLEQVLRERQLTIGTLIAGawAILL 1789
Cdd:PRK09294  173 LSGAERFmpamyayELPPTPTAAVLAKPGLPQAVPVTRCR-----LSKAQTSSLAAFGRRHRLTVNALVSA--AILL 242
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1104-1326 9.63e-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: 50.73  E-value: 9.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1104 AVGAVIRHHDALRLRFVAEDGMWRARGMPSGGP-VPYEVVDLSElpgeerRAALEARAAEAQASLDLTDGPILRVVQFRL 1182
Cdd:cd19538    44 ALYDVVERHESLRTVFPEEDGVPYQLILEEDEAtPKLEIKEVDE------EELESEINEAVRYPFDLSEEPPFRATLFEL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1183 GPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGE---IVRLPSKTTSLRRWGERLLAT---VDEVVAAELPFW- 1255
Cdd:cd19538   118 GENE-HVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEapeLAPLPVQYADYALWQQELLGDesdPDSLIARQLAYWk 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260177242 1256 EALDGQGVR-PLPRGCEPAEDR--EGDAQTVEVwlggpeTEALLGRVGE-AYRTRAD--EVILAALAGALTEWAGGE 1326
Cdd:cd19538   197 KQLAGLPDEiELPTDYPRPAESsyEGGTLTFEI------DSELHQQLLQlAKDNNVTlfMVLQAGFAALLTRLGAGT 267
PLN02246 PLN02246
4-coumarate--CoA ligase
 2014-2430 1.06e-05

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 50.75  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGA-------YVPLDprwpLERVAAVLGTTrp 2086
Cdd:PLN02246   51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTPAE----IAKQAKASGAK-- 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2087 vCIVTDERHLGAVEIAARQLGIEhVVSLDGDgkdADGNVVIhgrRALADLADGNLPRAA-GPHNMAYVIFTSGSTGTPKG 2165
Cdd:PLN02246  125 -LIITQSCYVDKLKGLAEDDGVT-VVTIDDP---PEGCLHF---SELTQADENELPEVEiSPDDVVALPYSSGTTGLPKG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2166 VVERH-SQVINLIEWV---NRTYLVGPSDRLLFVTsPSFDL----SVydVFGMLAAGGSIHIASEDDLrspERLAAELGR 2237
Cdd:PLN02246  197 VMLTHkGLVTSVAQQVdgeNPNLYFHSDDVILCVL-PMFHIyslnSV--LLCGLRVGAAILIMPKFEI---GALLELIQR 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2238 GTITFWDSAPAALQQLV--PYFDRiEDGSQLRLAfLSGDwVPIG--MLDELRRAFPNVKLvGLG-GATEA-TVWS----- 2306
Cdd:PLN02246  271 HKVTIAPFVPPIVLAIAksPVVEK-YDLSSIRMV-LSGA-APLGkeLEDAFRAKLPNAVL-GQGyGMTEAgPVLAmclaf 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2307 --NYFEVdgidprwTSIPYGRPIQNARYYVLD-RSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepga 2383
Cdd:PLN02246  347 akEPFPV-------KSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW------ 413

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 260177242 2384 rlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PLN02246  414 --LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHP 458
PRK09192 PRK09192
fatty acyl-AMP ligase;
2008-2191 1.23e-05

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 50.77  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2008 YDG----VPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLdprwPL--------- 2074
Cdd:PRK09192   40 YDRrgqlEEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL----PLpmgfggres 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2075 --ERVAAVLGTTRPVCIVTDERHLGAVEIAARQLGIEHVvsldGDGKDADgnvvihgrraLADLADGNLPRAAgPHNMAY 2152
Cdd:PRK09192  116 yiAQLRGMLASAQPAAIITPDELLPWVNEATHGNPLLHV----LSHAWFK----------ALPEADVALPRPT-PDDIAY 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 260177242 2153 VIFTSGSTGTPKGVVERHSQVI-NLIEWVNRTYLVGPSDR 2191
Cdd:PRK09192  181 LQYSSGSTRFPRGVIITHRALMaNLRAISHDGLKVRPGDR 220
PRK13382 PRK13382
bile acid CoA ligase;
1992-2431 1.28e-05

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 50.53  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1992 LFESSVERSPGSVALCyDGVPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPR 2071
Cdd:PRK13382   48 GFAIAAQRCPDRPGLI-DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2072 WPLERVAAVLGTTRPVCIVTDERHLGAVEIAARqlGIEHVVSLDgDGKDADGNVVIhgrRALADLADGNLPRAAGPHNMA 2151
Cdd:PRK13382  127 FAGPALAEVVTREGVDTVIYDEEFSATVDRALA--DCPQATRIV-AWTDEDHDLTV---EVLIAAHAGQRPEPTGRKGRV 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2152 yVIFTSGSTGTPKGVveRHSQ---------VINLIEWVNR--TYLVGPsdrllfvtspsfdlsvydvfgMLAAGGSIHIA 2220
Cdd:PRK13382  201 -ILLTSGTTGTPKGA--RRSGpggigtlkaILDRTPWRAEepTVIVAP---------------------MFHAWGFSQLV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2221 seddlrsperLAAELGRGTITFWDSAPAALQQLV----PY--------FDRIED----------GSQLRLAFLSGDWVPI 2278
Cdd:PRK13382  257 ----------LAASLACTIVTRRRFDPEATLDLIdrhrATglavvpvmFDRIMDlpaevrnrysGRSLRFAAASGSRMRP 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2279 GMLDELRRAFPNVkLVGLGGATEATVWSNyfeVDGIDPRWTSIPYGRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVS 2358
Cdd:PRK13382  327 DVVIAFMDQFGDV-IYNNYNATEAGMIAT---ATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQF 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2359 FGYyadPSQTAERFVPDPFSgepgarlyrTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK13382  403 DGY---TSGSTKDFHDGFMA---------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPD 463
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 118-267 1.54e-05

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: 50.13  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  118 LRRAP------------DQWQILFAFHHIVCDGWSAMIVAAEFAELCAadveGRAATLTPiSRGFRDYLVWHRDLLASDD 185
Cdd:cd19544   107 LRQAPllrahvaedpanGRWLLLLLFHHLISDHTSLELLLEEIQAILA----GRAAALPP-PVPYRNFVAQARLGASQAE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  186 ASALVREwaaMVGDLDVST-PLDLpTDLPRRAQQryhVRQHFRDLGADLMDRVRESARAEGVTTYTVLLAAYQVLLTRLS 264
Cdd:cd19544   182 HEAFFRE---MLGDVDEPTaPFGL-LDVQGDGSD---ITEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCS 254


                  ...
gi 260177242  265 SQR 267
Cdd:cd19544   255 GRD 257
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1991-2431 1.55e-05

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 50.44  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1991 ELFESSVERSPGSVALCYDGvPPLTYSDLNGRANRLG-WLLRGLGAGPEERVVVWMdraPELV---VALLGILKTGGAYV 2066
Cdd:PRK08974   27 DMFEQAVARYADQPAFINMG-EVMTFRKLEERSRAFAaYLQNGLGLKKGDRVALMM---PNLLqypIALFGILRAGMIVV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2067 ---PL-DPRwPLERVAAVLGTTRPVcIVTDERHlgAVEIAARQLGIEHVV--SLdGD----GKDADGNVVIHGRRALA-- 2134
Cdd:PRK08974  103 nvnPLyTPR-ELEHQLNDSGAKAIV-IVSNFAH--TLEKVVFKTPVKHVIltRM-GDqlstAKGTLVNFVVKYIKRLVpk 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2135 -DLADGNLPRAA--------------GPHNMAYVIFTSGSTGTPKGVVERHSQVINLIEWVNRTY--LVGPSDRLLFVTS 2197
Cdd:PRK08974  178 yHLPDAISFRSAlhkgrrmqyvkpelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYgpLLHPGKELVVTAL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2198 P---SFDLSVYDVFGMLAAGGSIHIASEDDLrspERLAAELGRGTITFWDSAPAALQQLV--PYFDRIeDGSQLRLAFLS 2272
Cdd:PRK08974  258 PlyhIFALTVNCLLFIELGGQNLLITNPRDI---PGFVKELKKYPFTAITGVNTLFNALLnnEEFQEL-DFSSLKLSVGG 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2273 GDWVPIGMLDELRRAFPNVKLVGLGgATEAT--VWSNYFEVDGIDprwTSIpyGRPIQNARYYVLDRSGNPCPIGVTGDL 2350
Cdd:PRK08974  334 GMAVQQAVAERWVKLTGQYLLEGYG-LTECSplVSVNPYDLDYYS---GSI--GLPVPSTEIKLVDDDGNEVPPGEPGEL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2351 YIGGTCVSFGYYADPSQTAErFVPDPFsgepgarlYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK08974  408 WVKGPQVMLGYWQRPEATDE-VIKDGW--------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478


                  .
gi 260177242 2431 G 2431
Cdd:PRK08974  479 K 479
PRK05691 PRK05691
peptide synthase; Validated
 1998-2415 1.75e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 50.55  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1998 ERSPGSVALCY-----DGVPPLTYSDLNGRANRLGWLLRGLgAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDP-- 2070
Cdd:PRK05691   20 AQTPDRLALRFladdpGEGVVLSYRDLDLRARTIAAALQAR-ASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 ---RWPLERVAAVLGTTRPVCIVTDERHLGAVeiaarqLGIEHvvsldgdGKDADGNVVIHGRRALADLADGNLPRAAGP 2147
Cdd:PRK05691   99 sarRHHQERLLSIIADAEPRLLLTVADLRDSL------LQMEE-------LAAANAPELLCVDTLDPALAEAWQEPALQP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2148 HNMAYVIFTSGSTGTPKGV-VERHSQVINliEWVNRTYL---VGPSDRLLfvtspSFdLSVYDVFGMLaaGG-------- 2215
Cdd:PRK05691  166 DDIAFLQYTSGSTALPKGVqVSHGNLVAN--EQLIRHGFgidLNPDDVIV-----SW-LPLYHDMGLI--GGllqpifsg 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2216 --SIHIASEDDLRSPERLAAELGR--GTITFWDS----------APAALQQLvpyfdrieDGSQLRLAFlSGDwVPIgML 2281
Cdd:PRK05691  236 vpCVLMSPAYFLERPLRWLEAISEygGTISGGPDfayrlcservSESALERL--------DLSRWRVAY-SGS-EPI-RQ 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2282 DELRR--------AFPNVKLVGLGGATEATVWSN---------YFEVD-----------GIDPRWTSIPYGRPIQNARyY 2333
Cdd:PRK05691  305 DSLERfaekfaacGFDPDSFFASYGLAEATLFVSggrrgqgipALELDaealarnraepGTGSVLMSCGRSQPGHAVL-I 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2334 VLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPdpfsgEPGARLYRTGDLArFFRDGNIEFLGRADSQVKIR 2413
Cdd:PRK05691  384 VDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE-----HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVR 457


                  ..
gi 260177242 2414 GY 2415
Cdd:PRK05691  458 GH 459
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 2015-2179 2.86e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 49.56  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVL--GTTRpVCIVTD 2092
Cdd:PRK08162   45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLrhGEAK-VLIVDT 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ERHlGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHGRRALADLADGNLPRAA-GPHNMAYVI---FTSGSTGTPKGVVE 2168
Cdd:PRK08162  124 EFA-EVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWtLPADEWDAIalnYTSGTTGNPKGVVY 202

                         170
                  ....*....|....*.
gi 260177242 2169 RH-----SQVINLIEW 2179
Cdd:PRK08162  203 HHrgaylNALSNILAW 218
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
487-960 3.67e-05

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 48.99  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  487 DAVALDAGSNVVS---YGELNRRADKLAHmlRLKGVGTETRVGLCLERSVELVVGILGVLKAGGAYV----PLDPAYPSE 559
Cdd:PRK05851   18 DLVVLDRESGLWRrhpWPEVHGRAENVAA--RLLDRDRPGAVGLVGEPTVELVAAIQGAWLAGAAVSilpgPVRGADDGR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  560 -------RLAflahDAGVQIVLSAAGAEERLGEGPWTVVRldEDLGR-PDERDAAPNDNVSAENLAYVMYTSGSTGKPKG 631
Cdd:PRK05851   96 wadatltRFA----GIGVRTVLSHGSHLERLRAVDSSVTV--HDLATaAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  632 VAVTHRNVVRLVRG--SSFATFGPDQVFLMMAPAAFDASTFEIWGALLHGARLVLFPPE--SPTPEEIGRVVREHGVTtl 707
Cdd:PRK05851  170 AILSPGAVLSNLRGlnARVGLDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTafSASPFRWLSWLSDSRAT-- 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  708 WLTAPLF-HAVADRGLDQLRGV-----RQLLAGGDVLSPKHVARVL-----LGLPALRLINGYGPTENTTFTTC------ 770
Cdd:PRK05851  248 LTAAPNFaYNLIGKYARRVSDVdlgalRVALNGGEPVDCDGFERFAtamapFGFDAGAAAPSYGLAESTCAVTVpvpgig 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  771 ---HDVSRGMGTGS---VPIGKPIANTHVYLL-DEQMNPVPPNAVGELFTGGDGLARGY-HERPDQTAERFvpdpfsgvp 842
Cdd:PRK05851  328 lrvDEVTTDDGSGArrhAVLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGYlGQAPIDPDDWF--------- 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  843 garlyRTGDLArYLPNGDMEFLGRRDGQVKIRGFRIELAEVEAALLQHPALREAVVIA-----REDRPGdkrlvaYVVGR 917
Cdd:PRK05851  399 -----PTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvgtgeGSARPG------LVIAA 466

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 260177242  918 EAEVPRFSELRKFLLQRLPDH--MIPAAVVALD--KLPLVPSGKLDR 960
Cdd:PRK05851  467 EFRGPDEAGARSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKLRR 513
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 1998-2433 3.77e-05

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 48.71  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1998 ERSPGSVALCYDGvPPLTYSDLNGRANRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERV 2077
Cdd:PRK09029   14 QVRPQAIALRLND-EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2078 AAVLgttrpvcivtderhlgaveiaaRQLGIEHVVSLDGDGKdadgnvvIHGRRALADLADGNLPRAA-GPHNMAYVIFT 2156
Cdd:PRK09029   93 EELL----------------------PSLTLDFALVLEGENT-------FSALTSLHLQLVEGAHAVAwQPQRLATMTLT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2157 SGSTGTPKGVVERHSQ-------VINLIEWvnrtylvGPSDRLLfvtspsFDLSVYDVFGM------LAAGGSIHIASED 2223
Cdd:PRK09029  144 SGSTGLPKAAVHTAQAhlasaegVLSLMPF-------TAQDSWL------LSLPLFHVSGQgivwrwLYAGATLVVRDKQ 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2224 DLrsperlaaelgrgtitfwdsaPAALQQ-----LVPyfdriedgSQL-RLaflsgdwvpigmLDELRRAFpNVKLVGLG 2297
Cdd:PRK09029  211 PL---------------------EQALAGcthasLVP--------TQLwRL------------LDNRSEPL-SLKAVLLG 248

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2298 GA---TEATV---------WSNY-----------FEVDGIDprwtsiPYGRPIQNaRYYVLdrsgnpcpigVTGDLYIGG 2354
Cdd:PRK09029  249 GAaipVELTEqaeqqgircWCGYgltemastvcaKRADGLA------GVGSPLPG-REVKL----------VDGEIWLRG 311

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260177242 2355 TCVSFGYYADPSQTaerfvpdPFSGEPGarLYRTGDLARfFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGAQ 2433
Cdd:PRK09029  312 ASLALGYWRQGQLV-------PLVNDEG--WFATRDRGE-WQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQ 380
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1063-1267 4.21e-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, 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: 48.61  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1063 EMPLTPIQR--WFLS---GEPAAphhFNQAVLLALRDawvpkHVD-----AAVGAVIRHHDALRLRFVAEDGMwrarGMP 1132
Cdd:cd19532     1 TEPMSFGQSrfWFLQqylEDPTT---FNVTFSYRLTG-----PLDvarleRAVRAVGQRHEALRTCFFTDPED----GEP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1133 SGGPVPYEVVDLSELPGEERRAALEARAAEAQASLDLTDGPILRVVQFRLGPGEPDrLLVVVHHLAVDVVSWGILLADLA 1212
Cdd:cd19532    69 MQGVLASSPLRLEHVQISDEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHY-LIFGYHHIAMDGVSFQIFLRDLE 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260177242 1213 TAHRQLvegeivRLPSKTTSLRRWGERLLATVDE-VVAAELPFWEALDGQGVRPLP 1267
Cdd:cd19532   148 RAYNGQ------PLLPPPLQYLDFAARQRQDYESgALDEDLAYWKSEFSTLPEPLP 197
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 2324-2430 5.29e-05

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 48.66  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2324 GRPIQNARYYVLDRSGNPCPIGVTGDLYIGGTCVSFGYYADPSQTAERFVPDPFsgepgarlYRTGDLARFFRDGNIEFL 2403
Cdd:PRK12492  389 GIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGW--------FKTGDIAVIDPDGFVRIV 460

                          90       100
                  ....*....|....*....|....*..
gi 260177242 2404 GRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:PRK12492  461 DRKKDLIIVSGFNVYPNEIEDVVMAHP 487
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1065-1406 7.50e-05

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: 47.87  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1065 PLTPIQRWFLSG-EPA------APHHFnqavlLALRDAWV-PKHVDAAVGAVIRHHDALRLRFvAEDGmwRARGMPSGGP 1136
Cdd:cd19535     3 PLTDVQYAYWIGrQDDqelggvGCHAY-----LEFDGEDLdPDRLERAWNKLIARHPMLRAVF-LDDG--TQQILPEVPW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1137 VPYEVVDLSELPgeERRAALEARAAEAQAS---LDLTDGPILRVVQFRLgPGEPDRLLVVVHHLAVDVVSWGILLADLAT 1213
Cdd:cd19535    75 YGITVHDLRGLS--EEEAEAALEELRERLShrvLDVERGPLFDIRLSLL-PEGRTRLHLSIDLLVADALSLQILLRELAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1214 AHRQlvEGEivRLPSKTTSLRRWGERLLATVDEVVAAELPFWEA-LDGQGVRP-LPRGCEPAEDREGDAQTVEVWLGGPE 1291
Cdd:cd19535   152 LYED--PGE--PLPPLELSFRDYLLAEQALRETAYERARAYWQErLPTLPPAPqLPLAKDPEEIKEPRFTRREHRLSAEQ 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1292 TEALlgrvgeayRTRADE-------VILAALAGALTEWAGGEAAYVAVEGHGREELFPDIEvaRTVGWFTTIHPV-VLPG 1363
Cdd:cd19535   228 WQRL--------KERARQhgvtpsmVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVN--DVVGDFTSLLLLeVDGS 297

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 260177242 1364 RPQSAGARLKAVKEAIRRVPKHGIGYGIlrylgsdEVVTRLAR 1406
Cdd:cd19535   298 EGQSFLERARRLQQQLWEDLDHSSYSGV-------VVVRRLLR 333
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 805-964 1.05e-04

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 47.30  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  805 PNAVGELFTGGDGLARGYherpdqtaerfVPDPFsgvPGARLYRTGDLARYLPNGDMEFLGRRDGQVKIRGFRIELAEVE 884
Cdd:PRK07445  298 ANQTGNITIQAQSLALGY-----------YPQIL---DSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVE 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  885 AALLQHPALREAVVIAREDRPGDKRLVAYVVGReAEVPRFSELRKFLLQRLPDHMIPAAVVALDKLPLVPSGKLDRRALP 964
Cdd:PRK07445  364 AAILATGLVQDVCVLGLPDPHWGEVVTAIYVPK-DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 2014-2174 1.15e-04

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: 47.29  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGW-LLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTD 2092
Cdd:cd05938     6 YTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ERHLGAVE---IAARQLGIEhvVSLDGDGKDADGnvVIHGRRALADLADGNLPRA--AGPHNM--AYVIFTSGSTGTPKG 2165
Cdd:cd05938    86 PELQEAVEevlPALRADGVS--VWYLSHTSNTEG--VISLLDKVDAASDEPVPASlrAHVTIKspALYIYTSGTTGLPKA 161


                  ....*....
gi 260177242 2166 VVERHSQVI 2174
Cdd:cd05938   162 ARISHLRVL 170
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1606-2139 2.89e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 46.40  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1606 RRLVRIPT---ERIDARSMAVDGDAWIVERARDERRRGFALDAAPAMRLLLVRTGDRSHRLI-WTFHHILLDGWSVPLVL 1681
Cdd:COG3321   858 RRRVPLPTypfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALaLAAAALAALLALVALAA 937

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1682 EEVFKRYSGGMQHEAAHRTAPRPHRDYVAWLRGADAQSVERFWRRELGGFREVTPLGIDRPPAGQRASSYRRFERALDEH 1761
Cdd:COG3321   938 AAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1762 TTARLEQVLRERQLTIGTLIAGAWAILLERYGGRRDVVFGETVSGRSAPLEGIERMVGLfINTVPMRAVVDPERPIGEWL 1841
Cdd:COG3321  1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAE-LALAAAALALAAALAAAALA 1096

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1842 TELQGRRAERTAYEHASLAQVQAWSEVPHGSALFESLIVVENYPVAPAFSGDELSVRLVGGDEQTNYPVTLVALPGRRLT 1921
Cdd:COG3321  1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1922 LRLLYEAERIPDGAAEGVLSHLESLLCAIADDPDLPTGDLPLLSAHERRQVVADWNDTARAYARERCIHELFESSVERSP 2001
Cdd:COG3321  1177 LALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2002 GSVALCYDGVPPLTYsdlngranRLGWLLRGLGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVL 2081
Cdd:COG3321  1257 AALAALALLAAAAGL--------AALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAA 1328

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 2082 GTTRPVCIVTDERHLGAVEIAARQLGIEHVVSLDGDGKDADGNVVIHGRRALADLADG 2139
Cdd:COG3321  1329 ALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 2014-2432 3.30e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 45.83  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2014 LTYSDLNGRANRLGWLLRG-LGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVTD 2092
Cdd:PRK07867   29 TSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2093 ERHLGAVeiaarqlgiehvvsldgDGKDADGNVVIHGRRALADLADGNL-----PRAAGPHNMAYVIFTSGSTGTPKGVV 2167
Cdd:PRK07867  109 SAHAELL-----------------DGLDPGVRVINVDSPAWADELAAHRdaeppFRVADPDDLFMLIFTSGTSGDPKAVR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2168 ERHSQVINLIEWVNRTYLVGPSDrLLFVTSPSF-------DLSVydvfgMLAAGGSIHI-----ASE--DDLRsperlaa 2233
Cdd:PRK07867  172 CTHRKVASAGVMLAQRFGLGPDD-VCYVSMPLFhsnavmaGWAV-----ALAAGASIALrrkfsASGflPDVR------- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2234 elgRGTITFWDSAPAALQQLVPYFDRIEDGSQ-LRLAFlsGDWVPIGMLDELRRAFpNVKLVGLGGATEAtvwsnyfevd 2312
Cdd:PRK07867  239 ---RYGATYANYVGKPLSYVLATPERPDDADNpLRIVY--GNEGAPGDIARFARRF-GCVVVDGFGSTEG---------- 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2313 GIDPRWT------SIpyGRPIQNARyyVLD-RSGNPCPIGV-------TGDLYIG------GTCVSFGYYADPSQTAERF 2372
Cdd:PRK07867  303 GVAITRTpdtppgAL--GPLPPGVA--IVDpDTGTECPPAEdadgrllNADEAIGelvntaGPGGFEGYYNDPEADAERM 378

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2373 VpdpfsgepgARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPGA 2432
Cdd:PRK07867  379 R---------GGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDA 429
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 976-1043 4.56e-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: 41.08  E-value: 4.56e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260177242    976 VAPEGHPEEVLARIWERVLRV------DAVGREDNFFELGGDSILAIQVVAG-AREVDLKLTVRQIFTHPTLSSL 1043
Cdd:smart00823    4 LPPAERRRLLLDLVREQVAAVlghaaaEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAAL 78
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 3-494 4.86e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 45.63  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    3 TPLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFG 82
Cdd:COG3321   861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   83 VTDGSSWDEPTAAAWLQAEAARPFDLRAGALRVRALRRAPDQWQILFAfhhivcdgwsAMIVAAEFAELCAADVEGRAAT 162
Cdd:COG3321   941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAA----------AAAAAAALAAAAALALLAAAAL 1010

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  163 LTPISRGFRDYLVWHRDLLASDDASALVREWAAMVGDLDVSTPLDLPTDLPRRAQQRYHVRQHFRDLGADLMDRVRESAR 242
Cdd:COG3321  1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  243 AEGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGHMAGIVPVPARIDAAATPRAIIRELRNALRVTAK 322
Cdd:COG3321  1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  323 LQSVPLSRLAEQCRVPKSPGRMPLVQAVFQEIRSFNEAIRPEGFGHMLRWSRGPLGFEVEVPSELGSQLDLEVRCYDFFS 402
Cdd:COG3321  1171 AALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  403 SSVRTCWRYDPDLFLPETVERWADYYAALLRELVGDLGRLALQIDFIPEPERRRVLVEWNQTASDYPRERCLHHLFEEEA 482
Cdd:COG3321  1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAAL 1330

                         490
                  ....*....|..
gi 260177242  483 RRVPDAVALDAG 494
Cdd:COG3321  1331 AALAAAVAAALA 1342
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1168-1242 5.44e-04

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: 45.00  E-value: 5.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260177242 1168 DLTDGPILRVVQFRLGPGEpDRLLVVVHHLAVDVVSWGILLADLATAHRQLVEGEIVRLPSKTTSLR---RWGERLLA 1242
Cdd:cd20484   104 VLENGPLMRVHLFSRSEQE-HFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYdfvAWEQDMLA 180
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 595-866 1.36e-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: 43.89  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  595 EDLGR--PDERDAAPNDNVSAENLAYVMYTSGSTGKPKGVAVTHRNVVRLVRGSS------FATFGPDQV--FLMMAPAA 664
Cdd:cd05933   129 MELGRsiPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASqhmdlrPATVGQESVvsYLPLSHIA 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  665 fdASTFEIWGALLHGArLVLFP-PES-------------PT-----P---EEIGRVVREHGV--TTL------W------ 708
Cdd:cd05933   209 --AQILDIWLPIKVGG-QVYFAqPDAlkgtlvktlrevrPTafmgvPrvwEKIQEKMKAVGAksGTLkrkiasWakgvgl 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  709 ----------LTAPLFHAVADR----------GLDQlrgVRQLLAGGDVLSPKhVARVLLGLpALRLINGYGPTENttfT 768
Cdd:cd05933   286 etnlklmggeSPSPLFYRLAKKlvfkkvrkalGLDR---CQKFFTGAAPISRE-TLEFFLSL-NIPIMELYGMSET---S 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  769 TCHDVSRGMGTGSVPIGKPIANTHVYLLDEQmnpvpPNAVGELFTGGDGLARGYHERPDQTAERFVPDPFsgvpgarlYR 848
Cdd:cd05933   358 GPHTISNPQAYRLLSCGKALPGCKTKIHNPD-----ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGW--------LH 424

                         330
                  ....*....|....*...
gi 260177242  849 TGDLARYLPNGDMEFLGR 866
Cdd:cd05933   425 SGDLGKLDEDGFLYITGR 442
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 2142-2191 1.40e-03

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 43.93  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260177242 2142 PRAAGPHNMAYVIFTSGSTGTPKGVVERHSqviNLIEWVNRTYLV---GPSDR 2191
Cdd:PLN02736  215 FRPPKPEDVATICYTSGTTGTPKGVVLTHG---NLIANVAGSSLStkfYPSDV 264
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
2008-2398 2.72e-03

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 42.85  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2008 YDGVPP--LTYSDLNGRANRLGWLLRG-LGAGPEERVVVWMDRAPELVVALLGILKTGGAYVPLDPRWPLERVAAVLGTT 2084
Cdd:PRK05620   31 WGGAEQeqTTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2085 RPVCIVTDERHLGA-VEIAARQLGIEHVVSLDGDGKDAD-----GNVVIHGRRALAD--LADGNLPRAAgPHNMAYVIFT 2156
Cdd:PRK05620  111 EDEVIVADPRLAEQlGEILKECPCVRAVVFIGPSDADSAaahmpEGIKVYSYEALLDgrSTVYDWPELD-ETTAAAICYS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2157 SGSTGTPKGVVERHSQVinlieWVNRTYLVGpSDRLLFVTSPSFDLSV--YDVFGM---LAA--GGSIHIASEDDLrSPE 2229
Cdd:PRK05620  190 TGTTGAPKGVVYSHRSL-----YLQSLSLRT-TDSLAVTHGESFLCCVpiYHVLSWgvpLAAfmSGTPLVFPGPDL-SAP 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2230 RLA-------AELGRGTITFWdsapaaLQQLVPYFDRIEDGSQLRLAFLSGDWVPIGMLDELRRAFpNVKLVGLGGATE- 2301
Cdd:PRK05620  263 TLAkiiatamPRVAHGVPTLW------IQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTEt 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2302 ---ATVWSNYFEVDGiDPRWT-SIPYGRPIQNARYYVL---------DRSgnpcpigvTGDLYIGGTCVSFGYYADPSQT 2368
Cdd:PRK05620  336 spvGTVARPPSGVSG-EARWAyRVSQGRFPASLEYRIVndgqvmestDRN--------EGEIQVRGNWVTASYYHSPTEE 406

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 260177242 2369 ----AERFVPDPFSGEPGA----RLYRTGDLARFFRDG 2398
Cdd:PRK05620  407 gggaASTFRGEDVEDANDRftadGWLRTGDVGSVTRDG 444
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 4-423 3.09e-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: 42.56  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242    4 PLPLSEGQRSLWLAQELAGDVPVYTLPLVFRVTGPLSEAAIRRSMEAVLERRDALRLVVRPDNEGLVQSLADVSAVDFGV 83
Cdd:cd19537     1 DTALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242   84 TDGSSWDEptaaawlqaeAARPFDLRAGALrVRALrraPDQWQILFAFHHIVCDGWSAMIVAAEFAELCAADvegraaTL 163
Cdd:cd19537    81 DTLDVWKE----------INRPFDLEREDP-IRVF---ISPDTLLVVMSHIICDLTTLQLLLREVSAAYNGK------LL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  164 TPISRGFRDYLVWHRDllASDDASALVREWaamvgdLDVSTPLDLPtdlPRRAQQRYHVRQHFRDLGADLMDRVRESARA 243
Cdd:cd19537   141 PPVRREYLDSTAWSRP--ASPEDLDFWSEY------LSGLPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTS 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  244 EGVTTYTVLLAAYQVLLTRLSSQRPFLVGCGVSGRTRTWQLGVVGhmagiV---PVPARI----DAAATPRAIIRELRNA 316
Cdd:cd19537   210 SGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVG-----LflePLPIRIrfpsSSDASAADFLRAVRRS 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242  317 LRvTAKLQSVPLSRLAEQCRVPKSPGRMPLVQAV--FQEIRSFNEAIRPEGFGHMLRWSRG---PLGFE-VEVPSElGSQ 390
Cdd:cd19537   285 SQ-AALAHAIPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEPLYTWAEGakfPLMFEfTALSDD-SLL 362

                         410       420       430
                  ....*....|....*....|....*....|...
gi 260177242  391 LDLEvrcydffsssvrtcwrYDPDLFLPETVER 423
Cdd:cd19537   363 LRLE----------------YDTDCFSEEEIDR 379
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 2015-2170 3.53e-03

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 42.43  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2015 TYSDLNGRANRLGWLLRGLGAGPEERV--VVW-MDRAPElvvALLGILKTGGAYVPLDPRWPLERVAAVLGTTRPVCIVT 2091
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVatIAWnTWRHLE---AWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2092 DERHLGAVE-IAARQLGIEHVVSLdgdgKDADGNVVIHGRRALA-----DLADGNLPRAAGPHNMAYVI-FTSGSTGTPK 2164
Cdd:PRK06018  118 DLTFVPILEkIADKLPSVERYVVL----TDAAHMPQTTLKNAVAyeewiAEADGDFAWKTFDENTAAGMcYTSGTTGDPK 193


                  ....*.
gi 260177242 2165 GVVERH 2170
Cdd:PRK06018  194 GVLYSH 199
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 2360-2431 3.87e-03

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: 42.42  E-value: 3.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260177242 2360 GYYADPSQTAERFVPDPFsgEPGARLYRTGDLARFFRDGNIEFLGRADSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:cd05937   316 GYLHNEDATESKLVRDVF--RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPD 385
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1992-2170 4.25e-03

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 42.65  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 1992 LFESSVERSPGSVALcYDGV-PPLTYSDLNGRANRLGWLLRGlGAGPEERVVVWMDRAPELVVALLGILKTGgaYVPLDP 2070
Cdd:PRK06814  637 LIEAAKIHGFKKLAV-EDPVnGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAG--RVPAMI 712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2071 RWPLErVAAVLGTTRPVCIVT--------DERHLGAVeIAARQLGIeHVVSLDgdgkdaDGNVVIHGRRALADLADGNLP 2142
Cdd:PRK06814  713 NFSAG-IANILSACKAAQVKTvltsrafiEKARLGPL-IEALEFGI-RIIYLE------DVRAQIGLADKIKGLLAGRFP 783

                         170       180       190
                  ....*....|....*....|....*....|..
gi 260177242 2143 RAAG----PHNMAYVIFTSGSTGTPKGVVERH 2170
Cdd:PRK06814  784 LVYFcnrdPDDPAVILFTSGSEGTPKGVVLSH 815
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 2324-2430 4.55e-03

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: 41.98  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2324 GRPIQnARYYVLDRSGNPCPIGVTGDLYIGGTcVSFGYYADPSQTAERFVPDPFSGepgarlyrTGDLARFFRDGNIEFL 2403
Cdd:cd05929   300 GRAVL-GKVHILDEDGNEVPPGEIGEVYFANG-PGFEYTNDPEKTAAARNEGGWST--------LGDVGYLDEDGYLYLT 369

                          90       100
                  ....*....|....*....|....*..
gi 260177242 2404 GRADSQVKIRGYRIECGEVEVALAQHP 2430
Cdd:cd05929   370 DRRSDMIISGGVNIYPQEIENALIAHP 396
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 2041-2431 5.35e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 41.94  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2041 VVVWMDRAPELVVALLGILKTGGAYVPLDPRwplERVAAVLGTTRPV-C--IVTDERHLGAVeiaaRQLGIEHVVSLDGD 2117
Cdd:PRK13388   55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALAADIRRAdCqlLVTDAEHRPLL----DGLDLPGVRVLDVD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2118 GKDAdgnvvihgRRALADLADGNLPRAAGPHNMAYVIFTSGSTGTPKGVVERHSQVInliewvnrtylvgpsdRLLFVTS 2197
Cdd:PRK13388  128 TPAY--------AELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA----------------FAGRALT 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2198 PSFDLSVYDVF---------GMLAAGGSIHIASEDDLRSPERLAA-----ELGRGTITFWDSAPAALQQLVPYFDRIEDG 2263
Cdd:PRK13388  184 ERFGLTRDDVCyvsmplfhsNAVMAGWAPAVASGAAVALPAKFSAsgfldDVRRYGATYFNYVGKPLAYILATPERPDDA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2264 -SQLRLAFlsGDWVPIGMLDELRRAFpNVKLVGLGGATEATVwsNYFEVDGIDPrwTSIpyGRPIQNARYYVLDrSGNPC 2342
Cdd:PRK13388  264 dNPLRVAF--GNEASPRDIAEFSRRF-GCQVEDGYGSSEGAV--IVVREPGTPP--GSI--GRGAPGVAIYNPE-TLTEC 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260177242 2343 PIGV--------TGDLYIG------GTCVSFGYYADPSQTAERFvpdpfsgepgaR--LYRTGDLARFFRDGNIEFLGRA 2406
Cdd:PRK13388  334 AVARfdahgallNADEAIGelvntaGAGFFEGYYNNPEATAERM-----------RhgMYWSGDLAYRDADGWIYFAGRT 402

                         410       420
                  ....*....|....*....|....*
gi 260177242 2407 DSQVKIRGYRIECGEVEVALAQHPG 2431
Cdd:PRK13388  403 ADWMRVDGENLSAAPIERILLRHPA 427
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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