|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
130-731 |
0e+00 |
|
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: 792.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 130 GHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTN 209
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 210 IITSKEllqtklkdivslvprlrhiitvdgkpptwsefpkgvivhtmaavqalgvkanvekkahskplPSDIAVIMYTSG 289
Cdd:cd17639 81 IFTDGK--------------------------------------------------------------PDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 290 STGIPKGVMISHSNIIASITGMARRIPRLgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSAELVCL 369
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPEL-------------------------LGPDDRYLAYLPLAHIFELAAENVCL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 370 SHGCRIGYSSPQTLADqssKIKKGSKGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKG 449
Cdd:cd17639 154 YRGGTIGYGSPRTLTD---KSKRGCKGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 450 CSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVC 529
Cdd:cd17639 231 PGTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPC 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 530 CEIKLKNWEEGGYFnTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedeNGQRWLCTGDIGEFDPDGCLKIIDRKKDL 609
Cdd:cd17639 310 CEIKLVDWEEGGYS-TDKPPPRGEILIRGPNVFKGYYKNPEKTKEAF----DGDGWFHTGDIGEFHPDGTLKIIDRKKDL 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 610 VKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKELTELARTKGFK-GTWEELCNSSEMENEVLKVL 688
Cdd:cd17639 385 VKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVInSEWEELCEDKKLQKAVLKSL 464
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2268062224 689 SEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKEL 731
Cdd:cd17639 465 AETARAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
30-743 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 790.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 30 ISLYTILTYIPFYFLCESKQEKPNQIKAKPVSSKPDSAYRSINS-VDGLASVLYPGCDTLDKVFMYAKNKFKNKRLLGTR 108
Cdd:PLN02387 1 MGAYIVGVLVPLLLTLLLRGSKKGKKRGVPVDVGGEPGYAIRNArFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 109 EILNEEDEIQPNGKIFKKVILGHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVT 188
Cdd:PLN02387 81 KLISREFETSSDGRKFEKLHLGEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 189 LYATLGGPAIVHGLNETEVTNIIT-SKELlqTKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGV---IVHTMAAVQALGV 264
Cdd:PLN02387 161 IYASLGEEALCHSLNETEVTTVICdSKQL--KKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSsnwTVSSFSEVEKLGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 265 KANVEKkahSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGQitghepaaavelwrnrkvhqpasl 344
Cdd:PLN02387 239 ENPVDP---DLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGK------------------------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 345 reEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSVLKPTLMAAVPEIMDRIYKNVMNKV 424
Cdd:PLN02387 292 --NDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 425 NEMSAFQRNLFILAYNYKMEQI------SKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVG 498
Cdd:PLN02387 370 DAKGGLAKKLFDIAYKRRLAAIegswfgAWGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 499 QGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFE 578
Cdd:PLN02387 450 QGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKV 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 579 DENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKEL 658
Cdd:PLN02387 530 DERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQAL 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 659 TELARTKGFK-GTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQA 737
Cdd:PLN02387 610 EKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKD 689
|
....*.
gi 2268062224 738 DIERMY 743
Cdd:PLN02387 690 DLKKLY 695
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
130-743 |
5.39e-179 |
|
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: 522.93 E-value: 5.39e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 130 GHYNWLSYEDVFIRALDFGNGLQMLGQK--PKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEV 207
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 208 TniitskellqtklkdivslvprlrhIITVDgkpptwsefpKGVIVHTMAAVQALGVKAnveKKAHSKPLPSDIAVIMYT 287
Cdd:cd05927 81 S-------------------------IVFCD----------AGVKVYSLEEFEKLGKKN---KVPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 288 SGSTGIPKGVMISHSNIIASITGMarriprlgqitghepaaavelwrNRKVHQPASLREEDVYIGYLPLAHVLELSAELV 367
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGV-----------------------FKILEILNKINPTDVYISYLPLAHIFERVVEAL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 368 CLSHGCRIGYSS--PQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQ 445
Cdd:cd05927 180 FLYHGAKIGFYSgdIRLLLD-----------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 446 ISKG--CSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGRV 523
Cdd:cd05927 249 LRSGvvRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHV 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 524 GAPLVCCEIKLKNWEEGGYFNTDkPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKII 603
Cdd:cd05927 329 GGPLPCAEVKLVDVPEMNYDAKD-PNPRGEVCIRGPNVFSGYYKDPEKTAEAL--DEDG--WLHTGDIGEWLPNGTLKII 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 604 DRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKELTELARTK-GFKGTWEELCNSSEMEN 682
Cdd:cd05927 404 DRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKK 483
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2268062224 683 EVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMY 743
Cdd:cd05927 484 AILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
68-743 |
2.24e-145 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 440.30 E-value: 2.24e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 68 YRSINSVDGLASVL--YPGCDTLDKVFMYAKNKFKNKRLLGTReilneedeIQPNGKIfkkvilGHYNWLSYEDVFIRAL 145
Cdd:PLN02736 24 YRSARSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTART 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 146 DFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIv 225
Cdd:PLN02736 90 AIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 226 SLVPRLRHIITVDGKPPTWSEFPK--GVIVHTMAAVQALGvkaNVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSN 303
Cdd:PLN02736 169 SEIPSVRLIVVVGGADEPLPSLPSgtGVEIVTYSKLLAQG---RSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 304 IIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTL 383
Cdd:PLN02736 246 LIANVAGSSLSTK---------------------------FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 384 adqsskikkGSKGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCS-TPLCDRFVFRN 462
Cdd:PLN02736 299 ---------KLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 463 VRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGY 542
Cdd:PLN02736 370 IKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNY 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 543 FNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGK 622
Cdd:PLN02736 450 TSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVI--DEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEK 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 623 VEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKELTELARTKGFK-GTWEELCNSSEMENEVLKVLSEAAISASLEKFE 701
Cdd:PLN02736 526 IENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFE 605
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2268062224 702 IPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMY 743
Cdd:PLN02736 606 FAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-746 |
1.60e-141 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 428.75 E-value: 1.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 82 YPGCDTLDKVFMYAKNKFKNKRLLGTREilneedeiqpngkifkkviLGHYNWLSYEDVFIRALDFGNGLQMLGQKPKAN 161
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKE-------------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGDR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 162 IAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGKP 241
Cdd:COG1022 68 VAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 242 PtwsefPKGVIVHTMAAVQALGVKANVE---KKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrl 318
Cdd:COG1022 148 L-----RDDPRLLSLDELLALGREVADPaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 319 gqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSAELVCLSHGCRIGYS-SPQTLADqsskikkgskgD 397
Cdd:COG1022 221 -------------------------LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------D 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 398 TSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYN--YKM-EQISKGCSTP--------LCDRFVFRNVRRL 466
Cdd:COG1022 265 LREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAvgRRYaRARLAGKSPSlllrlkhaLADKLVFSKLREA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 467 LGGNIRLLLCGGAPLSATTQRF---MNIcfccPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLknweeggyf 543
Cdd:COG1022 345 LGGRLRFAVSGGAALGPELARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI--------- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 544 ntdkpHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKV 623
Cdd:COG1022 412 -----AEDGEILVRGPNVMKGYYKNPEATAEAFDADG----WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPI 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 624 EAALKNLPLIDNICAYANSyHSYVIGFVVPNQKELTELARTKGFK-GTWEELCNSSEMENEVLKVLseAAISASLEKFEI 702
Cdd:COG1022 483 ENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEV--DRANAGLSRAEQ 559
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2268062224 703 PLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK 746
Cdd:COG1022 560 IKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
46-743 |
3.01e-139 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 425.93 E-value: 3.01e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 46 ESKQEKPNQIKAKPVSSKPDSA--YRSINSVDG----LASVLYPGcDTLDKVFMYAKNKFKNKRLLGTREILNEEDEIQP 119
Cdd:PTZ00216 24 EEYRRYGPQNVPVPGTETENASaiYRIAGVTDEeherLRNEWYYG-PNFLQRLERICKERGDRRALAYRPVERVEKEVVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 120 NGKIFKKVI-LGHYN---WLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGG 195
Cdd:PTZ00216 103 DADGKERTMeVTHFNetrYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 196 PAIVHGLNETEVTNIITSKEllqtKLKDIVSLVP--RLRH--IITVDGKPPtwSEFPKGVIVHTMAAVQALGvkaNVEKK 271
Cdd:PTZ00216 183 DALAYALRETECKAIVCNGK----NVPNLLRLMKsgGMPNttIIYLDSLPA--SVDTEGCRLVAWTDVVAKG---HSAGS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 272 AHSKPLPS---DIAVIMYTSGSTGIPKGVMISHSNIIASITGMArriPRLGQITGHepaaavelwrnrkvhqpasLREED 348
Cdd:PTZ00216 254 HHPLNIPEnndDLALIMYTSGTTGDPKGVMHTHGSLTAGILALE---DRLNDLIGP-------------------PEEDE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 349 VYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKikkgSKGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMS 428
Cdd:PTZ00216 312 TYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 429 AFQRNLFILAYNYKMEQISKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFcCPVGQGYGLTESTG 508
Cdd:PTZ00216 388 SLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVC 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 509 AGTITEVWDYNTGRVGAPLVCCEIKLKNWEEggYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCT 588
Cdd:PTZ00216 467 CGGIQRTGDLEPNAVGQLLKGVEMKLLDTEE--YKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVL--DEDG--WFHT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 589 GDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPNQKELTELARTKG 666
Cdd:PTZ00216 541 GDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEHG 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 667 FKGTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMY 743
Cdd:PTZ00216 621 IEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
130-731 |
6.07e-135 |
|
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: 406.21 E-value: 6.07e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 130 GHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTN 209
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 210 IITSKellqtklkdivslvprlrhiitvdgkpptwsefpkgvivhtmaavqalgvkanvekkahskplPSDIAVIMYTSG 289
Cdd:cd05907 81 LFVED---------------------------------------------------------------PDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 290 STGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLE-LSAELVC 368
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP---------------------------ATEGDRHLSFLPLAHVFErRAGLYVP 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 369 LSHGCRIGY-SSPQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDRIYKNVmnKVNEMSAFQRNLFILAYnykmeqis 447
Cdd:cd05907 151 LLAGARIYFaSSAETLLD-----------DLSEVRPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAV-------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 448 kgcstplcdrfvfrnvrrllGGNIRLLLCGGAPLSATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPL 527
Cdd:cd05907 210 --------------------GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPL 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 528 VCCEIKLknweeggyfntdkpHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGEFDPDGCLKIIDRKK 607
Cdd:cd05907 269 PGVEVRI--------------ADDGEILVRGPNVMLGYYKNPEATAEALDAD----GWLHTGDLGEIDEDGFLHITGRKK 330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 608 DLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSyHSYVIGFVVPNQKELTELARTKGFKG-TWEELCNSSEMENEVLK 686
Cdd:cd05907 331 DLIITSGGKNISPEPIENALKASPLISQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEA 409
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2268062224 687 VLSEAaiSASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKEL 731
Cdd:cd05907 410 AVEAA--NARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
68-743 |
1.06e-123 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 384.76 E-value: 1.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 68 YRSINSVDGLASVLyPGCDTLDKVFMYAKNKFKNKRLLGTREILNeedeiqpnGKIfkkvilGHYNWLSYEDVFIRALDF 147
Cdd:PLN02614 28 YRSIFAKDGFPNPI-EGMDSCWDVFRMSVEKYPNNPMLGRREIVD--------GKP------GKYVWQTYQEVYDIVIKL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 148 GNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSL 227
Cdd:PLN02614 93 GNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 228 VPRLRHIITVDGKPPTWSEFPK--GVIVHTMAAVQALGvkanvEKKAHSKPL--PSDIAVIMYTSGSTGIPKGVMISHSN 303
Cdd:PLN02614 173 TEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLG-----EGKQYDLPIkkKSDICTIMYTSGTTGDPKGVMISNES 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 304 IIASITGMARRiprLGQITghepaaavelwrnrkvhqpASLREEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSpqtl 383
Cdd:PLN02614 248 IVTLIAGVIRL---LKSAN-------------------AALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 384 ADQSSKIKkgskgDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCS----TPLCDRFV 459
Cdd:PLN02614 302 GDVKLLIE-----DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 460 FRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTgAGTITEVWDY--NTGRVGAPLVCCEIKLKNW 537
Cdd:PLN02614 377 FNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVDIRLESV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 538 EEGGYfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEY 617
Cdd:PLN02614 456 PEMEY-DALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDG-----WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEY 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 618 VSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKELTELARTKGFKGTWEELCNSSEMENEVLKVLSEAAISASL 697
Cdd:PLN02614 530 VAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKM 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2268062224 698 EKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMY 743
Cdd:PLN02614 610 KGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
68-743 |
3.32e-122 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 380.70 E-value: 3.32e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 68 YRSINSVDGLASvLYPGCDTLDKVFMYAKNKFKNKRLLGTREILNEEdeiqpngkifkkviLGHYNWLSYEDVFIRALDF 147
Cdd:PLN02430 25 YRNLLSKKGFPP-IDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGK--------------VGPYMWKTYKEVYEEVLQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 148 GNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITS----KELLQ----- 218
Cdd:PLN02430 90 GSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQdkkiKELLEpdcks 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 219 -TKLKDIVSLVPRLRHIIT----VDGKPPTWSEFpkgvivhtmaavqalgVKANVEKKAH-SKPLPSDIAVIMYTSGSTG 292
Cdd:PLN02430 170 aKRLKAIVSFTSVTEEESDkasqIGVKTYSWIDF----------------LHMGKENPSEtNPPKPLDICTIMYTSGTSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 293 IPKGVMISHSNIIASITGMArriprlgqitghepaAAVELWRNRKVHqpaslreEDVYIGYLPLAHVLELSAELVCLSHG 372
Cdd:PLN02430 234 DPKGVVLTHEAVATFVRGVD---------------LFMEQFEDKMTH-------DDVYLSFLPLAHILDRMIEEYFFRKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 373 CRIGYSSPQTLAdqsskikkgSKGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCS- 451
Cdd:PLN02430 292 ASVGYYHGDLNA---------LRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSh 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 452 ---TPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNT-GRVGAPL 527
Cdd:PLN02430 363 kkaSPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 528 VCCEIKLKNWEEGGYFNTDKPhPRGEILIGGQNVTMGYYKNEAKTktdffEDENGQRWLCTGDIGEFDPDGCLKIIDRKK 607
Cdd:PLN02430 443 VYNELRLEEVPEMGYDPLGEP-PRGEICVRGKCLFSGYYKNPELT-----EEVMKDGWFHTGDIGEILPNGVLKIIDRKK 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 608 DLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKELTELARTKGFKGTWEELCNSSEMENEVLKV 687
Cdd:PLN02430 517 NLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2268062224 688 LSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMY 743
Cdd:PLN02430 597 LKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
56-743 |
5.68e-113 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 356.46 E-value: 5.68e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 56 KAKPVSSKPDSA---YRSINSVDGLAsVLYPGCDTLDKVFMYAKNKFKNKRLLGTREILNeedeiqpnGKIfkkvilGHY 132
Cdd:PLN02861 11 ESRPATGGKPSAgpvYRSIYAKDGLL-DLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTD--------SKV------GPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 133 NWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIIT 212
Cdd:PLN02861 76 VWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 213 SkellQTKLKDIVSLVPR----LRHIITVDGKPPTWSEFPK--GVIVHTMAAVQALGvKANVEKKAHSKplpSDIAVIMY 286
Cdd:PLN02861 156 Q----ESKISSILSCLPKcssnLKTIVSFGDVSSEQKEEAEelGVSCFSWEEFSLMG-SLDCELPPKQK---TDICTIMY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 287 TSGSTGIPKGVMISHSNIIASITGmarrIPRLGQITGHepaaavelwrnrkvhqpaSLREEDVYIGYLPLAHVLELSAEL 366
Cdd:PLN02861 228 TSGTTGEPKGVILTNRAIIAEVLS----TDHLLKVTDR------------------VATEEDSYFSYLPLAHVYDQVIET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 367 VCLSHGCRIGY--SSPQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKME 444
Cdd:PLN02861 286 YCISKGASIGFwqGDIRYLME-----------DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 445 QISKGCS----TPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGaGTITEVWDYNT 520
Cdd:PLN02861 355 NLRKGLKqeeaSPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANVFS 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 521 --GRVGAPLVCCEIKLKNWEEGGYfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDG 598
Cdd:PLN02861 434 mvGTVGVPMTTIEARLESVPEMGY-DALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLIDG-----WFHTGDIGEWQPNG 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 599 CLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKELTELARTKGFKGTWEELCNSS 678
Cdd:PLN02861 508 AMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNL 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2268062224 679 EMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMY 743
Cdd:PLN02861 588 KARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
130-613 |
1.35e-109 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 339.67 E-value: 1.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 130 GHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTN 209
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 210 IITSKELLQTKLKDIVSLVPRLRHIITVDGKPPTWSEfpkgvivhtmaAVQALGVKANVEKKAHSKPLPSDIAVIMYTSG 289
Cdd:pfam00501 97 LITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIYTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 290 STGIPKGVMISHSNIIASITGMARRIPRLGqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLAHVLELSAE-LVC 368
Cdd:pfam00501 166 TTGKPKGVMLTHRNLVANVLSIKRVRPRGF-----------------------GLGPDDRVLSTLPLFHDFGLSLGlLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 369 LSHGCRIGYSSPQTLADQsskikKGSKGDTSVLKPTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfilaynykmeqisk 448
Cdd:pfam00501 223 LLAGATVVLPPGFPALDP-----AALLELIERYKVTVLYGVPTLLNMLLEA----------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 449 gcstplcdrfvfRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGT--ITEVWDYNT-GRVGA 525
Cdd:pfam00501 269 ------------GAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTtpLPLDEDLRSlGSVGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 526 PLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGEFDPDGCLKIIDR 605
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPVPPGEP---GELCVRGPGVMKGYLNDPELTAEAFDED----GWYRTGDLGRRDEDGYLEIVGR 409
|
....*...
gi 2268062224 606 KKDLVKLQ 613
Cdd:pfam00501 410 KKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
135-728 |
1.29e-65 |
|
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: 224.93 E-value: 1.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMynfqlvtlyatLGGPAIVHGlnetevtNIITSK 214
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMA-----------LGAVDVVRG-------SDSSVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQTklkdivslvprLRHiitvdgkpptwSEfPKGVIVHTMaavqalgvkanvekkahskplPSDIAVIMYTSGSTGIP 294
Cdd:cd17640 68 ELLYI-----------LNH-----------SE-SVALVVEND---------------------SDDLATIIYTSGTTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 295 KGVMISHSNIIASITgmarripRLGQITGHEPAaavelwrnrkvhqpaslreeDVYIGYLPLAHVLELSAELVCLSHGCR 374
Cdd:cd17640 104 KGVMLTHANLLHQIR-------SLSDIVPPQPG--------------------DRFLSILPIWHSYERSAEYFIFACGCS 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 375 IGYSSPQTLadqsskikkgsKGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAynykmeqiskgcstpl 454
Cdd:cd17640 157 QAYTSIRTL-----------KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF---------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 455 cdrfvfrnvrrLLGGNIRLLLCGGAPLSATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKL 534
Cdd:cd17640 210 -----------LSGGIFKFGISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKI 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 535 KNwEEGGyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQA 614
Cdd:cd17640 278 VD-PEGN--VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL--DSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSN 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 615 GEYVSLGKVEAALKNLPLIDNIcayansyhsYVIG--------FVVPNQKELTELARTKGFKGTWEELCNSSEME----- 681
Cdd:cd17640 351 GENVEPQPIEEALMRSPFIEQI---------MVVGqdqkrlgaLIVPNFEELEKWAKESGVKLANDRSQLLASKKvlkly 421
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2268062224 682 -NEVLKVLSEAAISASLEKFeipLKIRLSPDPWTpETGLVTDAFKLKR 728
Cdd:cd17640 422 kNEIKDEISNRPGFKSFEQI---APFALLEEPFI-ENGEMTQTMKIKR 465
|
|
| carboxyl_red |
NF041592 |
carboxylic acid reductase; |
204-743 |
2.31e-56 |
|
carboxylic acid reductase;
Pssm-ID: 469476 [Multi-domain] Cd Length: 1161 Bit Score: 209.03 E-value: 2.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 204 ETEVTNIITSKELLQtklkDIVSLV---PRLRHIITVDGKPPT-------------WSEFPkGVIVHTMAAVQALGVkan 267
Cdd:NF041592 147 ETEPRVLAASVDLLD----DAVELVltgPAPRRLVVFDYHPEVddhrealeaararLADAG-PVVVETLAEVLERGR--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 268 vEKKAHSKPLPSD---IAVIMYTSGSTGIPKGVMISHSNIiasiTGMARRIPRLGQitGHEPAAAVELwrnrkvhqpasl 344
Cdd:NF041592 219 -ALPAAPPPASDDddpLALLIYTSGSTGAPKGAMYTERLV----ANMWRGSARAGW--GPRAVPSITL------------ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 345 reedvyiGYLPLAHVLELSAELVCLSHGcRIGYSSPQtlADQSSKIKkgskgDTSVLKPTLMAAVPEIMDRIYKNVMnkv 424
Cdd:NF041592 280 -------NFMPMSHVMGRGTLYGTLARG-GTAYFAAR--SDLSTLLE-----DLALVRPTELNFVPRVWDMLFQEYQ--- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 425 nemSAFQRnlfilaynykmeQISKGCSTPLCDRFVFRNVRR-LLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGL 503
Cdd:NF041592 342 ---SELDR------------RAADGADRAAAEAAVKAELREdLLGGRFVSAMTGSAPISAEMKAFVESLLDLHLHDGYGS 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 504 TEstgAGTITevwdyNTGRVGAPLVCcEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGq 583
Cdd:NF041592 407 TE---AGGVF-----IDGRVRRPPVL-DYKLVDVPELGYFGTDRPHPRGELLVKTTTMFPGYYKRPEVTAEVF--DEDG- 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 584 rWLCTGDI-GEFDPDGcLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPnqkelTE-- 660
Cdd:NF041592 475 -FYRTGDIvAELGPDQ-LVYVDRRNNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYVYGNSARAYLLAVVVP-----TEea 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 661 LARTKgfkgtweelcNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIE 740
Cdd:NF041592 548 LARHG----------DAAELKALIAESLQRVAREAGLQSYEIPRDFLIETTPFTLENGLLTGIRKLARPKLKERYGERLE 617
|
...
gi 2268062224 741 RMY 743
Cdd:NF041592 618 QLY 620
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
135-660 |
3.28e-55 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 197.05 E-value: 3.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMynfqlvtlyatLGGPA-----------IVHGLN 203
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLF-----------AGGIFsaanpiytadeLAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 204 ETEVTNIITSKELLQtKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGVIVHTMAAVQALgvkanvekKAHSKPLPSDIAV 283
Cdd:cd05911 80 ISKPKVIFTDPDGLE-KVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDL--------PPPLKDGKDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 284 IMYTSGSTGIPKGVMISHSNIIASITgmarriprlgQITGHEPAaavelwrnrkvhqpaSLREEDVYIGYLPLAHVLELS 363
Cdd:cd05911 151 ILYSSGTTGLPKGVCLSHRNLIANLS----------QVQTFLYG---------------NDGSNDVILGFLPLYHIYGLF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 364 AELVCLSHGCRIgYSSPqtladqsskikkgsKGDTSVL-------KPTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfi 436
Cdd:cd05911 206 TTLASLLNGATV-IIMP--------------KFDSELFldliekyKITFLYLVPPIAAALAKS----------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 laynykmeqiskgcstPLCDRFVFRNVRRLLggnirlllCGGAPLSATTQRFMNICFC-CPVGQGYGLTESTGAGTITEV 515
Cdd:cd05911 254 ----------------PLLDKYDLSSLRVIL--------SGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 516 WDYNTGRVGAPLVCCEIKLKNWEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGEFD 595
Cdd:cd05911 310 GDDKPGSVGRLLPNVEAKIVDDDGK---DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED----GWLHTGDIGYFD 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2268062224 596 PDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICayansyhsyVIG------------FVVPNQ-KELTE 660
Cdd:cd05911 383 EDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHPGVADAA---------VIGipdevsgelpraYVVRKPgEKLTE 450
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
135-738 |
3.81e-55 |
|
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: 196.18 E-value: 3.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEvtniitsk 214
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSG-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ellqtklkdivslvprlrhiitvdgkpptwsefPKGVIVhtmaavqalgvkanvekkahskplpsdiAVIMYTSGSTGIP 294
Cdd:COG0318 97 ---------------------------------ARALVT----------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 295 KGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSAE-LVCLSHGC 373
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALG---------------------------LTPGDVVLVALPLFHVFGLTVGlLAPLLAGA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RI---GYSSPQTLADQsskIKKGskgdtsvlKPTLMAAVPEIMDRIyknvmnkvnemsafqrnlfilaynykmeqiskgC 450
Cdd:COG0318 169 TLvllPRFDPERVLEL---IERE--------RVTVLFGVPTMLARL---------------------------------L 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 451 STPLCDRFVFRNVRrllggnirLLLCGGAPLSATT-QRFMNiCFCCPVGQGYGLTESTGAGTIT--EVWDYNTGRVGAPL 527
Cdd:COG0318 205 RHPEFARYDLSSLR--------LVVSGGAPLPPELlERFEE-RFGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 528 VCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKK 607
Cdd:COG0318 276 PGVEVRIVD-EDG---RELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF---RDG--WLRTGDLGRLDEDGYLYIVGRKK 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 608 DLVKLqAGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVPNQ-KELTElartkgfkgtwEELcnssemene 683
Cdd:COG0318 347 DMIIS-GGENVYPAEVEEVLAAHPGVAEAAVVGvpdEKWGERVVAFVVLRPgAELDA-----------EEL--------- 405
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2268062224 684 vlkvlsEAAISASLEKFEIPLKIRLSPD-PWTPeTGlvtdafKLKRKELKTHYQAD 738
Cdd:COG0318 406 ------RAFLRERLARYKVPRRVEFVDElPRTA-SG------KIDRRALRERYAAG 448
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
130-735 |
2.11e-53 |
|
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: 192.68 E-value: 2.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 130 GHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEvtn 209
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 210 iitSKELLQTKLKDIVSLVPrlrhiiTVDGKPPTWSEFPKGVIvHTMAAVQALGVKANVEKKAhSKPLPSDIAVIMYTSG 289
Cdd:cd05932 79 ---SKALFVGKLDDWKAMAP------GVPEGLISISLPPPSAA-NCQYQWDDLIAQHPPLEER-PTRFPEQLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 290 STGIPKGVMISHSNIIASITGMARRIprlgqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLAHVLELSA-ELVC 368
Cdd:cd05932 148 TTGQPKGVMLTFGSFAWAAQAGIEHI---------------------------GTEENDRMLSYLPLAHVTERVFvEGGS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 369 LSHGCRIGYssPQTLADQSSKIKKGskgdtsvlKPTLMAAVPEIMDRIYKNVMNKVNEmSAFQRNLFIlaynykmeqisk 448
Cdd:cd05932 201 LYGGVLVAF--AESLDTFVEDVQRA--------RPTLFFSVPRLWTKFQQGVQDKIPQ-QKLNLLLKI------------ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 449 gcstPLCDRFVFRNVRRLLGGN-IRLLLCGGAPLS-ATTQRFMNICFccPVGQGYGLTESTGAGTITEVWDYNTGRVGAP 526
Cdd:cd05932 258 ----PVVNSLVKRKVLKGLGLDqCRLAGCGSAPVPpALLEWYRSLGL--NILEAYGMTENFAYSHLNYPGRDKIGTVGNA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 527 LVCCEIKLKnweeggyfntdkphPRGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRK 606
Cdd:cd05932 332 GPGVEVRIS--------------EDGEILVRSPALMMGYYKDPEATAEAFTADG----FLRTGDKGELDADGNLTITGRV 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 607 KDLVKLQAGEYVSLGKVEAALKNLPLIDNICAyANSYHSYVIGFVVPNqkeltELARTKGFKGTWEELcnssemENEVLK 686
Cdd:cd05932 394 KDIFKTSKGKYVAPAPIENKLAEHDRVEMVCV-IGSGLPAPLALVVLS-----EEARLRADAFARAEL------EASLRA 461
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2268062224 687 VLseAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHY 735
Cdd:cd05932 462 HL--ARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
280-711 |
5.10e-53 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 186.72 E-value: 5.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHV 359
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG---------------------------LTEGDVFLSTLPLFHI 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAELVCLSHGCRIGYSSPQTLADQSSKIKKgskgdtsvLKPTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfilay 439
Cdd:cd04433 54 GGLFGLLGALLAGGTVVLLPKFDPEAALELIER--------EKVTILLGVPTLLARLLKA-------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 440 nykmeqiskgcstPLCDRFVFRNVRRLLggnirlllCGGAPLS-ATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDY 518
Cdd:cd04433 106 -------------PESAGYDLSSLRALV--------SGGAPLPpELLERFEEA-PGIKLVNGYGLTETGGTVATGPPDDD 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 519 NTGR--VGAPLVCCEIKLKNwEEGGyfnTDKPHPRGEILIGGQNVTMGYYKNEAKTktdFFEDENGqrWLCTGDIGEFDP 596
Cdd:cd04433 164 ARKPgsVGRPVPGVEVRIVD-PDGG---ELPPGEIGELVVRGPSVMKGYWNNPEAT---AAVDEDG--WYRTGDLGRLDE 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 597 DGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDnicayansyHSYVIGfvVPNQKELTELArtkgfkgTWEELCN 676
Cdd:cd04433 235 DGYLYIVGRLKDMIKSG-GENVYPAEVEAVLLGHPGVA---------EAAVVG--VPDPEWGERVV-------AVVVLRP 295
|
410 420 430
....*....|....*....|....*....|....*
gi 2268062224 677 SSEMENEVLKvlseAAISASLEKFEIPLKIRLSPD 711
Cdd:cd04433 296 GADLDAEELR----AHVRERLAPYKVPRRVVFVDA 326
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
246-721 |
4.09e-51 |
|
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: 188.05 E-value: 4.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 246 EFPKGVIVHTMAAVQALGVKAnvekKAHSKPLPSD--IAVIMYTSGSTGIPKGVMISHSNIiasitgmarriprlgqitg 323
Cdd:cd17632 192 AVGIPVTTLTLIAVRGRDLPP----APLFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLV------------------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 324 hepaaaVELWRNRKVHQPASLREEdVYIGYLPLAHVLELSAELVCLSHGcRIGYSSPQtlADQSSKIKkgskgDTSVLKP 403
Cdd:cd17632 249 ------ATFWLKVSSIQDIRPPAS-ITLNFMPMSHIAGRISLYGTLARG-GTAYFAAA--SDMSTLFD-----DLALVRP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 404 TLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEqiskgcstplcdrfvFRNvrRLLGGNIRLLLCGGAPLSA 483
Cdd:cd17632 314 TELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAE---------------LRE--RVLGGRLLAAVCGSAPLSA 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 484 TTQRFMNICFCCPVGQGYGLTEstgAGTITEvwdynTGRVGAPLVCcEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTM 563
Cdd:cd17632 377 EMKAFMESLLDLDLHDGYGSTE---AGAVIL-----DGVIVRPPVL-DYKLVDVPELGYFRTDRPHPRGELLVKTDTLFP 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 564 GYYKNEAKTKTDFfeDENGqrWLCTGDI-GEFDPDGcLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANS 642
Cdd:cd17632 448 GYYKRPEVTAEVF--DEDG--FYRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNS 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 643 YHSYVIGFVVPNQKELTEL--ARTKGfkgtweelcnssemenEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLV 720
Cdd:cd17632 523 ERAYLLAVVVPTQDALAGEdtARLRA----------------ALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLL 586
|
.
gi 2268062224 721 T 721
Cdd:cd17632 587 S 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
170-635 |
2.32e-48 |
|
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: 180.25 E-value: 2.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 170 AEWMIAAQACFMYNFQLVTLYATlGGPAIVHGLNETEVTNII---TSKELlqTKLKDIVSLVPRLRHIITVDGKPP---- 242
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTT-NSPEACQYVAETSEANILvveNQKQL--QKILQIQDKLPHLKAIIQYKEPLKekep 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 243 ---TWSEFPKgvivhtmaavQALGVKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNiiasITGMARRIPRLG 319
Cdd:cd05933 121 nlySWDEFME----------LGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDN----ITWTAKAASQHM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 320 QItghepaaavelwrnrkvhQPASLREEDVyIGYLPLAHVlelSAEL----VCLSHGCRIGYSSPQTLadqsskikKGSK 395
Cdd:cd05933 187 DL------------------RPATVGQESV-VSYLPLSHI---AAQIldiwLPIKVGGQVYFAQPDAL--------KGTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 396 GDT-SVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISK---GCSTP-----LCDRFVFRNVRRL 466
Cdd:cd05933 237 VKTlREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKlmgGESPSplfyrLAKKLVFKKVRKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 467 LG-GNIRLLLCGGAPLSATTQRF---MNIcfccPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGY 542
Cdd:cd05933 317 LGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 543 fntdkphprGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGK 622
Cdd:cd05933 393 ---------GEICFWGRHVFMGYLNMEDKTEEAI--DEDG--WLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVP 459
|
490
....*....|....
gi 2268062224 623 VEAALKN-LPLIDN 635
Cdd:cd05933 460 IEDAVKKeLPIISN 473
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
129-633 |
1.62e-44 |
|
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: 168.76 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 129 LGHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEW---MIAAQACFMYNfqlVTLYATLGGPAIVHGLNET 205
Cdd:cd17641 6 FGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALS---LGIYQDSMAEEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 206 EVTNIITSKELLQTKLKDIVSLVPRLRHIITVDgkpptwsefPKGVIVHT---MAAVQALGVKANVEKKAHSKPL----- 277
Cdd:cd17641 83 GARVVIAEDEEQVDKLLEIADRIPSVRYVIYCD---------PRGMRKYDdprLISFEDVVALGRALDRRDPGLYereva 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 ---PSDIAVIMYTSGSTGIPKGVMISHSNIIasitgmarriprlgqitGHEpAAAVELwrnrkvhqpASLREEDVYIGYL 354
Cdd:cd17641 154 agkGEDVAVLCTTSGTTGKPKLAMLSHGNFL-----------------GHC-AAYLAA---------DPLGPGDEYVSVL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 355 PLAHVLE----LSAELVClshGCRIGY-SSPQTLadqsskikkgsKGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSA 429
Cdd:cd17641 207 PLPWIGEqmysVGQALVC---GFIVNFpEEPETM-----------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 430 FQRNLF---------ILAYNYKMEQISKGCSTP--LCDRFVFRNVRRLLG-GNIRLLLCGGAPLSATTQRF---MNIcfc 494
Cdd:cd17641 273 FKRFMFelgmklglrALDRGKRGRPVSLWLRLAswLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 495 cPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNweeggyfntdkphpRGEILIGGQNVTMGYYKNEAKTKT 574
Cdd:cd17641 350 -PLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE--------------VGEILVRSPGVFVGYYKNPEATAE 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2268062224 575 DFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLI 633
Cdd:cd17641 415 DFDEDG----WLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYI 469
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
273-633 |
1.95e-44 |
|
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: 166.46 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 273 HSKPL------PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLRE 346
Cdd:cd05914 77 HSEAKaifvsdEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL---------------------------LGK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 347 EDVYIGYLPLAHVLELSAELVC-LSHGCRIGY----SSPQTLADQSSKIKkgskgdtsvlkPTLMAAVPEIMDRIYKNV- 420
Cdd:cd05914 130 GDKILSILPLHHIYPLTFTLLLpLLNGAHVVFldkiPSAKIIALAFAQVT-----------PTLGVPVPLVIEKIFKMDi 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 421 MNKVNemsaFQRNLFILAYNYKMEQISKgcstplcdrFVFRNVRRLLGGNIRLLLCGGAPLSATTQRF---MNICFCcpv 497
Cdd:cd05914 199 IPKLT----LKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEFVIGGAKINPDVEEFlrtIGFPYT--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 498 gQGYGLTEsTGAGTITEVWD-YNTGRVGAPLVCCEIKlknweeggyfnTDKPHPR---GEILIGGQNVTMGYYKNEAKTK 573
Cdd:cd05914 263 -IGYGMTE-TAPIISYSPPNrIRLGSAGKVIDGVEVR-----------IDSPDPAtgeGEIIVRGPNVMKGYYKNPEATA 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 574 TDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLI 633
Cdd:cd05914 330 EAF--DKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
136-627 |
1.54e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 164.97 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 136 SYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKE 215
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 216 LLQTkLKDIVSLVPRLRHIITVDGKP-----PTWSEFpkgvivHTMAAVQAlgvkanvEKKAHSKPLPSDIAVIMYTSGS 290
Cdd:PRK06187 113 FVPL-LAAILPQLPTVRTVIVEGDGPaaplaPEVGEY------EELLAAAS-------DTFDFPDIDENDAAAMLYTSGT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 291 TGIPKGVMISHSNIIASITGMARRIprlgqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLAHVLELSAELVCLS 370
Cdd:PRK06187 179 TGHPKGVVLSHRNLFLHSLAVCAWL---------------------------KLSRDDVYLVIVPMFHVHAWGLPYLALM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 371 HGCRIGYS---SPQTLADQsskIKKgskgdtsvLKPTLMAAVPEIMDriyknvmnkvnemsafqrnlFILAYnykmeqis 447
Cdd:PRK06187 232 AGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPTIWQ--------------------MLLKA-------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 448 kgcstPLCDrfvFRNVRRLlggniRLLLCGGAPLSATT-QRFMNIcFCCPVGQGYGLTESTGAGTI-------TEVWDY- 518
Cdd:PRK06187 273 -----PRAY---FVDFSSL-----RLVIYGGAALPPALlREFKEK-FGIDLVQGYGMTETSPVVSVlppedqlPGQWTKr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 519 -NTGRVgAPLVccEIKLKNwEEGgyfntdKPHPR-----GEILIGGQNVTMGYYKNEAKTKtDFFEDEngqrWLCTGDIG 592
Cdd:PRK06187 339 rSAGRP-LPGV--EARIVD-DDG------DELPPdggevGEIIVRGPWLMQGYWNRPEATA-ETIDGG----WLHTGDVG 403
|
490 500 510
....*....|....*....|....*....|....*
gi 2268062224 593 EFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAAL 627
Cdd:PRK06187 404 YIDEDGYLYITDRIKDVII-SGGENIYPRELEDAL 437
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
278-641 |
2.38e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 152.57 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASItgmarrIPrlgqitghepaaaVELWRNRKVHQPaslreeDVYIGYLPLA 357
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTV------VP-------------LCKHSIFKKYNP------KTHLSYLPIS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVCLSHGCRIgysspqtlaDQSSK-IKKGSKgDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLF- 435
Cdd:PTZ00342 358 HIYERVIAYLSFMLGGTI---------NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVk 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 436 -ILA-----YNYKMEQISKGCSTplcdrfVFRNVRRLLGGNIRLLLCGGAPLSATTQR----FMNICFCcpvgQGYGLTE 505
Cdd:PTZ00342 428 kILSlrksnNNGGFSKFLEGITH------ISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYGLTE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 506 STGAGTITEVWDYNTGRVGAPLV-CCEIKLKNWEEggYFNTDKPhPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqR 584
Cdd:PTZ00342 498 TTGPIFVQHADDNNTESIGGPISpNTKYKVRTWET--YKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTED----G 570
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 585 WLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYAN 641
Cdd:PTZ00342 571 YFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGD 627
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
134-610 |
6.14e-37 |
|
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: 144.63 E-value: 6.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 134 WLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITS 213
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 214 kellqTKLKDIVSLVPRLRHIITVDgkpptwsefpkgvivhtmaavqalgvkanvekkahskplPSDIAVIMYTSGSTGI 293
Cdd:cd05936 104 -----VSFTDLLAAGAPLGERVALT---------------------------------------PEDVAVLQYTSGTTGV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 294 PKGVMISHSNIIASITGMARRIPRLgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSaelVCLSHGC 373
Cdd:cd05936 140 PKGAMLTHRNLVANALQIKAWLEDL-------------------------LEGDDVVLAALPLFHVFGLT---VALLLPL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RIGYsspqtladqsskikkgskgdTSVLKPTLMAavpeimdriyKNVMNkvnEMSAFQRNLFILA---YNYKMEqiskgc 450
Cdd:cd05936 192 ALGA--------------------TIVLIPRFRP----------IGVLK---EIRKHRVTIFPGVptmYIALLN------ 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 451 stplcdrfvFRNVRRLLGGNIRLLLCGGAPLS-ATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDYN-TGRVGAPLV 528
Cdd:cd05936 233 ---------APEFKKRDFSSLRLCISGGAPLPvEVAERFEEL-TGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 529 CCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKD 608
Cdd:cd05936 303 GTEVKIVD-DDG---EELPPGEVGELWVRGPQVMKGYWNRPEETAEAF---VDG--WLRTGDIGYMDEDGYFFIVDRKKD 373
|
..
gi 2268062224 609 LV 610
Cdd:cd05936 374 MI 375
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
278-633 |
1.22e-33 |
|
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: 135.83 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASitgmarriprlgqitghepaaaVELWRNRKVHQPASlreEDVYIGYLPLA 357
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLTHRNLIAM----------------------VAQFVAGEGSNSDS---EDVFLCVLPMF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVCLSH-GCRI----GYSSPQTL-ADQSSKIkkgskgdtsvlkpTLMAAVPEIMDRIYKNvmnkvnemsafq 431
Cdd:cd05904 212 HIYGLSSFALGLLRlGATVvvmpRFDLEELLaAIERYKV-------------THLPVVPPIVLALVKS------------ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 432 rnlfilaynykmeqiskgcstPLCDRFVFRNVRRLLggnirlllCGGAPLSATT-----QRFMNicfcCPVGQGYGLTES 506
Cdd:cd05904 267 ---------------------PIVDKYDLSSLRQIM--------SGAAPLGKELieafrAKFPN----VDLGQGYGMTES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 507 TGAGTITEVWDYNTGRVG-----APLVccEIKLKNWEEGgyfntdKPHP---RGEILIGGQNVTMGYYKNEAKTKTDFfe 578
Cdd:cd05904 314 TGVVAMCFAPEKDRAKYGsvgrlVPNV--EAKIVDPETG------ESLPpnqTGELWIRGPSIMKGYLNNPEATAATI-- 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2268062224 579 DENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI 633
Cdd:cd05904 384 DKEG--WLHTGDLCYIDEDGYLFIVDRLKELIKYK-GFQVAPAELEALLLSHPEI 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
135-610 |
1.55e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 132.34 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQTkLKDIVSLVPRLRHIITVdgkpPTWSEFPKGVIVHTMAAVQALGVKANVEKKAHskplPSDIAVIMYTSGSTGIP 294
Cdd:PRK07656 111 LFLGV-DYSATTRLPALEHVVIC----ETEEDDPHTEKMKTFTDFLAAGDPAERAPEVD----PDDVADILFTSGTTGRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 295 KGVMISHSNIIASITGMARRiprlgqitghepaaavelwrnrkvhqpASLREEDVYIGYLPLAHVLELSAELV-CLSHGC 373
Cdd:PRK07656 182 KGAMLTHRQLLSNAADWAEY---------------------------LGLTEGDRYLAANPFFHVFGYKAGVNaPLMRGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RI----GYSSPQTLAdqssKIKKGskgdtsvlKPTLMAAVPEImdriyknvmnkvnemsafqrnlfilaYNYkMEQISKG 449
Cdd:PRK07656 235 TIlplpVFDPDEVFR----LIETE--------RITVLPGPPTM--------------------------YNS-LLQHPDR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 450 CSTPLcdrfvfrnvrrllgGNIRLLLCGGA--PLsATTQRFMNICFCCPVGQGYGLTESTGAGTIT---EVWDYNTGRVG 524
Cdd:PRK07656 276 SAEDL--------------SSLRLAVTGAAsmPV-ALLERFESELGVDIVLTGYGLSEASGVTTFNrldDDRKTVAGTIG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 525 APLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIID 604
Cdd:PRK07656 341 TAIAGVENKIVN-ELGEEVPVGEV---GELLVRGPNVMKGYYDDPEATAAAI--DADG--WLHTGDLGRLDEEGYLYIVD 412
|
....*.
gi 2268062224 605 RKKDLV 610
Cdd:PRK07656 413 RKKDMF 418
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
274-633 |
4.08e-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: 126.31 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 274 SKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiprLGqitghepaaavelwrnrkvhqpasLREEDVYIGY 353
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALN---LG------------------------LTEDDNWLCA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 354 LPLAHVLELSAELVCLSHGCRIgYSSPQTLADQSSKIKKGSKGdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrn 433
Cdd:cd05912 125 LPLFHISGLSILMRSVIYGMTV-YLVDKFDAEQVLHLINSGKV-------TIISVVPTMLQRL----------------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 434 lfilaynykMEQISKGCSTplcdrfvfrnvrrllggNIRLLLCGGAPLSATT-----QRfmNIcfccPVGQGYGLTEsTG 508
Cdd:cd05912 180 ---------LEILGEGYPN-----------------NLRCILLGGGPAPKPLleqckEK--GI----PVYQSYGMTE-TC 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 509 AGTITEVWDY---NTGRVGAPLVCCEIKLKNweeggyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrW 585
Cdd:cd05912 227 SQIVTLSPEDalnKIGSAGKPLFPVELKIED-------DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF---ENG--W 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2268062224 586 LCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLI 633
Cdd:cd05912 295 FKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAI 341
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
274-660 |
1.45e-30 |
|
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: 125.42 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 274 SKPLPSDIAVIMYTSGSTGIPKGVMISHSNIiasitgmarriprlgqitghepaaaveLWRNRKVHQPASLREEDVYIGY 353
Cdd:cd17631 93 AKVLFDDLALLMYTSGTTGRPKGAMLTHRNL---------------------------LWNAVNALAALDLGPDDVLLVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 354 LPLAHVLELSaelvclshgcriGYSSPQTLADQSSKIKKGSKGDTsVL------KPTLMAAVPEIMdriyknvmnkvnem 427
Cdd:cd17631 146 APLFHIGGLG------------VFTLPTLLRGGTVVILRKFDPET-VLdlierhRVTSFFLVPTMI-------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 428 safqrnlfilaynYKMEQiskgcstplCDRFVFRNVRRLlggniRLLLCGGAPLSATTQRFMnICFCCPVGQGYGLTEST 507
Cdd:cd17631 199 -------------QALLQ---------HPRFATTDLSSL-----RAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTETS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 508 GAGTITEVWDYNT--GRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrW 585
Cdd:cd17631 251 PGVTFLSPEDHRRklGSAGRPVFFVEVRIVD-PDG---REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF---RDG--W 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 586 LCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNiCAyansyhsyVIG------------FVVP 653
Cdd:cd17631 322 FHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAE-VA--------VIGvpdekwgeavvaVVVP 391
|
....*...
gi 2268062224 654 NQK-ELTE 660
Cdd:cd17631 392 RPGaELDE 399
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
134-640 |
2.92e-29 |
|
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: 122.42 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 134 WLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAaqacfmynfqlvtLYATLGGPAIVHGLN----ETEVTN 209
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVA-------------FLAAARAGAVVAPLNpaykKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 210 ---------IITSKELLQTKLKDIVSLVPRLRHIitvdgkpptwsEFPKGVIVHTMAAVQ-ALGVKANVEKKAHSKPLPS 279
Cdd:cd05926 81 yladlgsklVLTPKGELGPASRAASKLGLAILEL-----------ALDVGVLIRAPSAESlSNLLADKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMArriprlgqitghepaaavelwrnrKVHQpasLREEDVYIGYLPLAHV 359
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAASATNIT------------------------NTYK---LTPDDRTLVVMPLFHV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAelVCLShgcrigysspqTLADQSSKIK----KGSK--GDTSVLKPTLMAAVPEIMDRIYKNVM-NKVNEMSAFqr 432
Cdd:cd05926 203 HGLVA--SLLS-----------TLAAGGSVVLpprfSASTfwPDVRDYNATWYTAVPTIHQILLNRPEpNPESPPPKL-- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 433 nlfilaynykmeqiskgcstplcdRFvfrnvrrllggnIRlllCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTI 512
Cdd:cd05926 268 ------------------------RF------------IR---SCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTS 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 T--EVWDYNTGRVGAPlVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGD 590
Cdd:cd05926 309 NplPPGPRKPGSVGKP-VGVEVRILD-EDG---EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD----GWFRTGD 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2268062224 591 IGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAYA 640
Cdd:cd05926 380 LGYLDADGYLFLTGRIKELIN-RGGEKISPLEVDGVLLSHPAVLEAVAFG 428
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
278-668 |
3.13e-28 |
|
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: 118.50 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLA 357
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP---------------------------LGPGDVFLNQAPFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVCLSHGcrigysspQTLAdqsskikkgskgdtsvlkptlmaAVPEimdriyknvmnkvnEMSAFQRNLFil 437
Cdd:cd05945 149 FDLSVMDLYPALASG--------ATLV-----------------------PVPR--------------DATADPKQLF-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 438 AYNYKMeQISKGCSTP----LCDRFVFRNVRRLlgGNIRL-LLCGGAPLSATTQRFMNiCF-CCPVGQGYGLTESTGAGT 511
Cdd:cd05945 182 RFLAEH-GITVWVSTPsfaaMCLLSPTFTPESL--PSLRHfLFCGEVLPHKTARALQQ-RFpDARIYNTYGPTEATVAVT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 512 ITEV-----WDYNTGRVGAPLVCCEIKLknWEEGGyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDEnGQRWL 586
Cdd:cd05945 258 YIEVtpevlDGYDRLPIGYAKPGAKLVI--LDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-GQRAY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 587 CTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICA---YANSYHSYVIGFVVPnqKELTELAR 663
Cdd:cd05945 333 RTGDLVRLEADGLLFYRGRLDFQVKLN-GYRIELEEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVP--KPGAEAGL 409
|
....*
gi 2268062224 664 TKGFK 668
Cdd:cd05945 410 TKAIK 414
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
280-633 |
1.79e-27 |
|
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: 116.24 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITgmarriprlgqitghepaAAVELWRnrkvhqpasLREEDVYIGYLPLAHV 359
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVR------------------ALVDAWR---------WTEDDVLLHVLPLHHV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAELVC-LSHGcrigySSPQTLADQSSKIKKGSKGDTSVlkpTLMAAVPEIMDRIyknvmnkvneMSAFQRNLfila 438
Cdd:cd05941 143 HGLVNALLCpLFAG-----ASVEFLPKFDPKEVAISRLMPSI---TVFMGVPTIYTRL----------LQYYEAHF---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 439 ynYKMEQISKGCStplcdrfvfrnvrrllgGNIRLLLCGGAPLSATT-QRFMNIcfccpVGQG----YGLTESTGAGTIT 513
Cdd:cd05941 201 --TDPQFARAAAA-----------------ERLRLMVSGSAALPVPTlEEWEAI-----TGHTllerYGMTEIGMALSNP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 514 EVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGE 593
Cdd:cd05941 257 LDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEV---GEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGV 329
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2268062224 594 FDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLI 633
Cdd:cd05941 330 VDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGV 369
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
135-636 |
3.17e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.22 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQTKLKDIVSLVPRLrhiITVDGKPPTW-SEFPKgvivhtmaavqalgvkanvekkahskplpSDIAVIMYTSGSTGI 293
Cdd:PRK03640 108 DFEAKLIPGISVKFAEL---MNGPKEEAEIqEEFDL-----------------------------DEVATIMYTSGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 294 PKGVMISHSNIIASITGMARRiprLGqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSAELVCLSHGC 373
Cdd:PRK03640 156 PKGVIQTYGNHWWSAVGSALN---LG------------------------LTEDDCWLAAVPIFHISGLSILMRSVIYGM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RIgYSSPQTLADQSSKIKKGSKGdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrnlfilaynykMEQISKGcSTP 453
Cdd:PRK03640 209 RV-VLVEKFDAEKINKLLQTGGV-------TIISVVSTMLQRL--------------------------LERLGEG-TYP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 454 lcdrfvfrnvrrllgGNIRLLLCGGAPLSATT-----QRfmNIcfccPVGQGYGLTEsTGAGTITEVWDY---NTGRVGA 525
Cdd:PRK03640 254 ---------------SSFRCMLLGGGPAPKPLleqckEK--GI----PVYQSYGMTE-TASQIVTLSPEDaltKLGSAGK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 526 PLVCCEIKL-KNWEEGgyfntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIID 604
Cdd:PRK03640 312 PLFPCELKIeKDGVVV------PPFEEGEIVVKGPNVTKGYLNREDATRETF---QDG--WFKTGDIGYLDEEGFLYVLD 380
|
490 500 510
....*....|....*....|....*....|..
gi 2268062224 605 RKKDLVkLQAGEYVSLGKVEAALKNLPLIDNI 636
Cdd:PRK03640 381 RRSDLI-ISGGENIYPAEIEEVLLSHPGVAEA 411
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
232-638 |
3.68e-27 |
|
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: 114.67 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 232 RHIITVDGKPPTWSEFPKGVIVHTMAAVQALGvKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGM 311
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALD-DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 312 ARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAH---VLELsaeLVCLSHGCRIgysspqtladqss 388
Cdd:TIGR01733 153 ARRYG---------------------------LDPDDRVLQFASLSFdasVEEI---FGALLAGATL------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 389 kikkgskgdtsvlkptlmAAVPEIMDRiyknvmnkvnemsAFQRNLFILAYNYKmeqISKGCSTP-LCDRFVFRNVRRLL 467
Cdd:TIGR01733 190 ------------------VVPPEDEER-------------DDAALLAALIAEHP---VTVLNLTPsLLALLAAALPPALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 468 GgnIRLLLCGGAPLSATT-----QRFMNICFCcpvgQGYGLTESTGAGTITEVWDYNTGR-----VGAPLVCCEIKLKNw 537
Cdd:TIGR01733 236 S--LRLVILGGEALTPALvdrwrARGPGARLI----NLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRLYVLD- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 538 eeggyfNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED----ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLV 610
Cdd:TIGR01733 309 ------DDLRPVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQV 382
|
410 420
....*....|....*....|....*...
gi 2268062224 611 KLQaGEYVSLGKVEAALKNLPLIDNICA 638
Cdd:TIGR01733 383 KIR-GYRIELGEIEAALLRHPGVREAVV 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
276-640 |
9.55e-27 |
|
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: 114.01 E-value: 9.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 276 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLP 355
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG---------------------------LGPGDVFLVASP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 356 LAHVlelsaelvclshgcrIGYSSPQTLAdqsskikkgskgdtsvlkptLMAAVPEIMDRIYKnvMNKVNEMSAFQRNLF 435
Cdd:cd05903 143 MAHQ---------------TGFVYGFTLP--------------------LLLGAPVVLQDIWD--PDKALALMREHGVTF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 436 ILAYNYKMEQI---SKGCSTPLCDrfvfrnvrrllggnIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTI 512
Cdd:cd05903 186 MMGATPFLTDLlnaVEEAGEPLSR--------------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TEVWD-----YNTGRVGAPLvccEIKLKNweegGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLC 587
Cdd:cd05903 252 ITPAPedrrlYTDGRPLPGV---EIKVVD----DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-----WFR 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2268062224 588 TGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICAYA 640
Cdd:cd05903 320 TGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
135-639 |
4.95e-26 |
|
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: 112.95 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQtKLKDIVSLVPRLRHIITVDGKPPTwSEFPKGVIVHTMAAVQALGVKAnvekkAHSKPLPSDIAVIMYTSGSTGIP 294
Cdd:TIGR03098 106 ERLD-LLHPALPGCHDLRTLIIVGDPAHA-SEGHPGEEPASWPKLLALGDAD-----PPHPVIDSDMAAILYTSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 295 KGVMISHSNIIASITGMARRIprlgqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLAHVLELSAELVCLSHGCR 374
Cdd:TIGR03098 179 KGVVLSHRNLVAGAQSVATYL---------------------------ENRPDDRLLAVLPLSFDYGFNQLTTAFYVGAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 375 I---GYSSPQTLADqsSKIKKGSKGdtsvlkptlMAAVPEIMDRiyknvmnkvnemsafqrnLFILAYnykmeqiskgcs 451
Cdd:TIGR03098 232 VvlhDYLLPRDVLK--ALEKHGITG---------LAAVPPLWAQ------------------LAQLDW------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 452 tPLCDrfvFRNVRRLLGGnirlllcGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTI-TEVWDYNTGRVGAPLVCC 530
Cdd:TIGR03098 271 -PESA---APSLRYLTNS-------GGAMPRATLSRLRSFLPNARLFLMYGLTEAFRSTYLpPEEVDRRPDSIGKAIPNA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 531 EIKLKNwEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDF-----FEDEN--GQRWLCTGDIGEFDPDGCLKII 603
Cdd:TIGR03098 340 EVLVLR-EDGSEC---APGEEGELVHRGALVAMGYWNDPEKTAERFrplppFPGELhlPELAVWSGDTVRRDEEGFLYFV 415
|
490 500 510
....*....|....*....|....*....|....*.
gi 2268062224 604 DRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAY 639
Cdd:TIGR03098 416 GRRDEMIK-TSGYRVSPTEVEEVAYATGLVAEAVAF 450
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
181-638 |
7.19e-26 |
|
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: 112.04 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 181 MYNFqlvtlyaTLGGPAIVHGLNETEVTNIITSKELLQtKLK-----------DIVSLvPRLRHIITVDGK--------- 240
Cdd:cd05909 60 MLNY-------TAGLRELRACIKLAGIKTVLTSKQFIE-KLKlhhlfdveydaRIVYL-EDLRAKISKADKckaflagkf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 241 PPTWSEFPKGVivhtmaavqalgvkanvekkahSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgq 320
Cdd:cd05909 131 PPKWLLRIFGV----------------------APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD---- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 321 itghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSAELVclshgcrigysSPQTladqsskikkgsKGDTSV 400
Cdd:cd05909 185 -----------------------PNPEDVVFGALPFFHSFGLTGCLW-----------LPLL------------SGIKVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 401 LKPTLMAA--VPEImdrIYKNvmnKVNemsafqrnlfILaynykmeqiskgCSTPLCDRFVFRNVRRLLGGNIRLLLCGG 478
Cdd:cd05909 219 FHPNPLDYkkIPEL---IYDK---KAT----------IL------------LGTPTFLRGYARAAHPEDFSSLRLVVAGA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 479 APLSATT-QRFMNIcFCCPVGQGYGLTESTGAGTITEVW-DYNTGRVGAPLVCCEIKLKNWEeggyfnTDKPHPRGE--- 553
Cdd:cd05909 271 EKLKDTLrQEFQEK-FGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVE------THEEVPIGEggl 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 554 ILIGGQNVTMGYYKNEAKTKTDFfedenGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLI 633
Cdd:cd05909 344 LLVRGPNVMLGYLNEPELTSFAF-----GDGWYDTGDIGKIDGEGFLTITGRLSRFAKI-AGEMVSLEAIEDILSEILPE 417
|
....*
gi 2268062224 634 DNICA 638
Cdd:cd05909 418 DNEVA 422
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
136-633 |
8.03e-26 |
|
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: 112.24 E-value: 8.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 136 SYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKE 215
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 216 LLQtKLKDIVSLVPRLRHIITVDGKPP--TWSEFPKGVIVHTMAAVQALGVKANVEKKahskplPSDIAVIMYTSGSTGI 293
Cdd:cd17642 126 GLQ-KVLNVQKKLKIIKTIIILDSKEDykGYQCLYTFITQNLPPGFNEYDFKPPSFDR------DEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 294 PKGVMISHSNIIASITgmARRIPRLGqitghepaaavelwrnrkvHQPAslrEEDVYIGYLPLAHVLELSAELVCLSHGC 373
Cdd:cd17642 199 PKGVQLTHKNIVARFS--HARDPIFG-------------------NQII---PDTAILTVIPFHHGFGMFTTLGYLICGF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RIGYSSP-------QTLADQsskikkgsKGDTSVLKPTLMAAVPEimdriyknvmnkvnemsafqrnlfilaynykmeqi 446
Cdd:cd17642 255 RVVLMYKfeeelflRSLQDY--------KVQSALLVPTLFAFFAK----------------------------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 447 skgcsTPLCDRFVFrnvrrllgGNIRLLLCGGAPLSATTQRFMNICFCCP-VGQGYGLTESTGAGTITEVWDYNTGRVGA 525
Cdd:cd17642 292 -----STLVDKYDL--------SNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 526 PLVCCEIKLKNWEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTdfFEDENGqrWLCTGDIGEFDPDGCLKIIDR 605
Cdd:cd17642 359 VVPFFYAKVVDLDTG---KTLGPNERGELCVKGPMIMKGYVNNPEATKA--LIDKDG--WLHSGDIAYYDEDGHFFIVDR 431
|
490 500
....*....|....*....|....*...
gi 2268062224 606 KKDLVKLQaGEYVSLGKVEAALKNLPLI 633
Cdd:cd17642 432 LKSLIKYK-GYQVPPAELESILLQHPKI 458
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
135-627 |
4.73e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 111.55 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKaNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:PRK08633 642 LSYGKALTGALALARLLKRELKDEE-NVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQT-KLKDIVSLVPRLRHIITVDGKPPTWSEFPKgviVHTMAAVQALGvKANVEKKAHSKPLPSDIAVIMYTSGSTGI 293
Cdd:PRK08633 721 KFLEKlKNKGFDLELPENVKVIYLEDLKAKISKVDK---LTALLAARLLP-ARLLKRLYGPTFKPDDTATIIFSSGSEGE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 294 PKGVMISHSNIIASItgmarriprlgqitghepAAAVELWRnrkvhqpasLREEDVYIGYLPLAHVLELSAEL-VCLSHG 372
Cdd:PRK08633 797 PKGVMLSHHNILSNI------------------EQISDVFN---------LRNDDVILSSLPFFHSFGLTVTLwLPLLEG 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 373 CRIGYSSPQTLADQSSK-IKKgskgdtsvLKPTLMAAVPEIMdRIY-KNvmNKVN-EMsaFQRNLFILAYNYKMEQiskg 449
Cdd:PRK08633 850 IKVVYHPDPTDALGIAKlVAK--------HRATILLGTPTFL-RLYlRN--KKLHpLM--FASLRLVVAGAEKLKP---- 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 450 cstPLCDRFVFRNvrrllggNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESTGAGT-------ITEVW---DYN 519
Cdd:PRK08633 913 ---EVADAFEEKF-------GIRIL------------------------EGYGATETSPVASvnlpdvlAADFKrqtGSK 958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 520 TGRVGAPLVCCEIKLKNWEeggyfnTDKPHPRGE---ILIGGQNVTMGYYKNEAKTKtDFFEDENGQRWLCTGDIGEFDP 596
Cdd:PRK08633 959 EGSVGMPLPGVAVRIVDPE------TFEELPPGEdglILIGGPQVMKGYLGDPEKTA-EVIKDIDGIGWYVTGDKGHLDE 1031
|
490 500 510
....*....|....*....|....*....|.
gi 2268062224 597 DGCLKIIDRKKDLVKLqAGEYVSLGKVEAAL 627
Cdd:PRK08633 1032 DGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
278-657 |
5.27e-25 |
|
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: 108.77 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqITGHEpaaavelwrnrKVHQPASLREeDVYIG--YLP 355
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP----LTPGD-----------RVLQFTSFSF-DVSVWeiFGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 356 LAHvlelSAELVCLSHGCRigySSPQTLAD--QSSKIkkgskgdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrn 433
Cdd:cd05930 156 LLA----GATLVVLPEEVR---KDPEALADllAEEGI-------------TVLHLTPSLLRLL----------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 434 lfiLAYNYkmeqiskgcstplcdrfvFRNVRRLlggniRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESTGAGTI 512
Cdd:cd05930 199 ---LQELE------------------LAALPSL-----RLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TEV----WDYNTGRVGAPLVCCEIKLKNweEGGyfntdKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED-ENGQR 584
Cdd:cd05930 253 YRVppddEEDGRVPIGRPIPNTRVYVLD--ENL-----RPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPNpFGPGE 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 585 WLC-TGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDN---ICAYANSYHSYVIGFVVPNQKE 657
Cdd:cd05930 326 RMYrTGDLVRWLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLAHPGVREaavVAREDGDGEKRLVAYVVPDEGG 401
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
280-640 |
1.25e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 107.38 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHV 359
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG---------------------------LGEDDVYLTVLPLFHI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 --LELSAeLVCLSHGCRIgysspqTLADQSS------KIKKgsKGDT-----SVLKPTLMAAVPEIMDRiyknvMNKVne 426
Cdd:cd05934 135 naQAVSV-LAALSVGATL------VLLPRFSasrfwsDVRR--YGATvtnylGAMLSYLLAQPPSPDDR-----AHRL-- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 427 msafqrnlfilaynykmeqiskgcstplcdRFVFrnvrrllggnirlllcGGAPLSATTQRFMNIcFCCPVGQGYGLTEs 506
Cdd:cd05934 199 ------------------------------RAAY----------------GAPNPPELHEEFEER-FGVRLLEGYGMTE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 507 TGAGTITEVWDYN-TGRVGAPLVCCEIKLKNWEeggyfntDKPHPR---GEILI---GGQNVTMGYYKNEAKTKTDFfed 579
Cdd:cd05934 231 TIVGVIGPRDEPRrPGSIGRPAPGYEVRIVDDD-------GQELPAgepGELVIrglRGWGFFKGYYNMPEATAEAM--- 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2268062224 580 ENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAYA 640
Cdd:cd05934 301 RNG--WFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREAAVVA 358
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
188-610 |
6.61e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 103.88 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 188 TLYATLGG---------------PAIVHGLNETEVTNIITSKELLQT----KLKDIVSLVPRLRHIITVDGKPPTWSefP 248
Cdd:PRK07529 96 THFALWGGeaagianpinpllepEQIAELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVDLARYLPG--P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 249 KGVIVHTM---AAVQALGVKANVEKK------AHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIAsitgMArriprlg 319
Cdd:PRK07529 174 KRLAVPLIrrkAHARILDFDAELARQpgdrlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA----NA------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 320 qitghepaaavelWrnrKVHQPASLREEDVYIGYLPLAHVLELSAE-LVCLSHGCRIGYSSPQtladqsskikkGSKGdt 398
Cdd:PRK07529 243 -------------W---LGALLLGLGPGDTVFCGLPLFHVNALLVTgLAPLARGAHVVLATPQ-----------GYRG-- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 399 svlkptlmaavPEIMDRIYKNVMN-KVNEMSAFQRnlfilAYNYKMEQISKGcstplcdrfvfRNVRRLlggniRLLLCG 477
Cdd:PRK07529 294 -----------PGVIANFWKIVERyRINFLSGVPT-----VYAALLQVPVDG-----------HDISSL-----RYALCG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 478 GAPLS-ATTQRFMN---IcfccPVGQGYGLTESTGAGTITEV-WDYNTGRVGAPLVCCEIK-LKNWEEGGYFNTDKPHPR 551
Cdd:PRK07529 342 AAPLPvEVFRRFEAatgV----RIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRvVILDDAGRYLRDCAVDEV 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2268062224 552 GEILIGGQNVTMGYYkNEAKTKTDFFEDengqRWLCTGDIGEFDPDGCLKIIDRKKDLV 610
Cdd:PRK07529 418 GVLCIAGPNVFSGYL-EAAHNKGLWLED----GWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
273-635 |
5.78e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 100.46 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 273 HSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITgMARR-IPRLGQitghepaaavelwrnrkvhqpaslREEDVYi 351
Cdd:PRK05605 213 HPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA-QGKAwVPGLGD------------------------GPERVL- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 352 GYLPLAHVLELSaelVCLSHGCRIG-----YSSPQtlADQSSKIKKGSKgdtsvlkPTLMAAVPEIMDRIYKnvmnkvne 426
Cdd:PRK05605 267 AALPMFHAYGLT---LCLTLAVSIGgelvlLPAPD--IDLILDAMKKHP-------PTWLPGVPPLYEKIAE-------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 427 mSAFQRNLFIlaynykmeqisKGcstplcdrfvfrnvrrllggnIRLLLCGGAPLSATTqrfmnicfccpVGQ------- 499
Cdd:PRK05605 327 -AAEERGVDL-----------SG---------------------VRNAFSGAMALPVST-----------VELwekltgg 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 500 ----GYGLTEST---GAGTITEvwDYNTGRVGAPLVCCEIKLKNWEeggyfNTDKPHP---RGEILIGGQNVTMGYYKNE 569
Cdd:PRK05605 363 llveGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPE-----DPDETMPdgeEGELLVRGPQVFKGYWNRP 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2268062224 570 AKTKtDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDN 635
Cdd:PRK05605 436 EETA-KSFLDG----WFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
280-656 |
1.16e-21 |
|
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: 96.96 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASitgmarriprlgqitghepaaavelwrNRKVHQPASLREEDVYIGYLPLAHV 359
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAA---------------------------NLQLIHAMGLTEADVYLNMLPLFHI 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAELVCLSHGCR---IGYSSPQTLAD--QSSKIkkgskgdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrnl 434
Cdd:cd17637 54 AGLNLALATFHAGGAnvvMEKFDPAEALEliEEEKV-------------TLMGSFPPILSNL------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 435 filaynykMEQISKGCSTPLCDRFVFrnvrrllggnirlllcgGAPLSATTQRFMNIC---FCCpvgqGYGLTESTGAGT 511
Cdd:cd17637 103 --------LDAAEKSGVDLSSLRHVL-----------------GLDAPETIQRFEETTgatFWS----LYGQTETSGLVT 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 512 ITEVWDyNTGRVGAPLVCCEIKLKNweeggyfNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCT 588
Cdd:cd17637 154 LSPYRE-RPGSAGRPGPLVRVRIVD-------DNDRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTF---RNG--WHHT 220
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 589 GDIGEFDPDGCLKIIDRK--KDLVKlQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIGfvVPNQK 656
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPAIAEVC---------VIG--VPDPK 278
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
134-635 |
3.06e-21 |
|
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: 97.75 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 134 WLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITS 213
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 214 KELLQtklkdivslvpRLRHIITVdgkpptwsefpkgvivhTMAAVQALGVKANVekkAHSKPLPSDIAVIMYTSGSTGI 293
Cdd:cd12116 92 DALPD-----------RLPAGLPV-----------------LLLALAAAAAAPAA---PRTPVSPDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 294 PKGVMISHSNIIASITGMARRiPRLGQ------ITghEPA---AAVELwrnrkvhqpaslreedvyigYLPL---AHVLE 361
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRER-LGLGPgdrllaVT--TYAfdiSLLEL--------------------LLPLlagARVVI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 362 LSAELVclshgcrigySSPQTLADQSSKIkkgskgdtsvlKPTLMAAVPeimdriyknvmnkvnemsAFQRNLFilayny 441
Cdd:cd12116 198 APRETQ----------RDPEALARLIEAH-----------SITVMQATP------------------ATWRMLL------ 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 442 kmeqiSKGcstplcdrfvFRNVRRLlggnirLLLCGGAPLSATTQRFmnicFCCPVGQG---YGLTESTGAGTITEVWDY 518
Cdd:cd12116 233 -----DAG----------WQGRAGL------TALCGGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAA 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 519 NTG-RVGAPLVcceiklknweeggyfNTD--------KPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQ 583
Cdd:cd12116 288 AGPiPIGRPLA---------------NTQvyvldaalRPVPPgvpGELYIGGDGVAQGYLGRPALTAERFVPDpfaGPGS 352
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2268062224 584 RWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN 635
Cdd:cd12116 353 RLYRTGDLVRRRADGRLEYLGRADGQVKIR-GHRIELGEIEAALAAHPGVAQ 403
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
136-619 |
4.45e-21 |
|
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: 97.32 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 136 SYEDVFIRALDFGNGLQMLGQKPKANIAIFcetraewmiaaqacfMYNFQ--LVTLYATLGGPAIVHGLN---------- 203
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATL---------------AWNTHrhLELYYAVPGMGAVLHTINprlfpeqiay 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 204 -----ETEVtnIITSKELLQtKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGVIVHTMAAVQALGVKANVEKKAHskplp 278
Cdd:cd12119 92 iinhaEDRV--VFVDRDFLP-LLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDEN----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 279 sDIAVIMYTSGSTGIPKGVMISH-SNIIASITGMARriprlgqitghepaaavelwrnrkvhQPASLREEDVYIGYLPLA 357
Cdd:cd12119 164 -TAAAICYTSGTTGNPKGVVYSHrSLVLHAMAALLT--------------------------DGLGLSESDVVLPVVPMF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKgdtsvlkPTLMAAVPEIMdriyknvmnkvnemsafqrnLFIL 437
Cdd:cd12119 217 HVNAWGLPYAAAMVGAKLVLPGPYLDPASLAELIEREG-------VTFAAGVPTVW--------------------QGLL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 438 AYnykmeqiskgcstplcdrfVFRNVRRLLGGniRLLLCGGA--PLS---ATTQRFMNICfccpvgQGYGLTESTGAGTI 512
Cdd:cd12119 270 DH-------------------LEANGRDLSSL--RRVVIGGSavPRSlieAFEERGVRVI------HAWGMTETSPLGTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 ------------TEVWDY--NTGRVgAPLVccEIKLKNwEEGGyfntDKPH---PRGEILIGGQNVTMGYYKNEAKTKtd 575
Cdd:cd12119 323 arppsehsnlseDEQLALraKQGRP-VPGV--ELRIVD-DDGR----ELPWdgkAVGELQVRGPWVTKSYYKNDEESE-- 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2268062224 576 fFEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVS 619
Cdd:cd12119 393 -ALTEDG--WLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWIS 432
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
274-653 |
1.00e-20 |
|
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: 96.19 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 274 SKPLPSDIAVIMYTSGSTGIPKGVMISH---SNIIASItgmarriprlgqitghepaaavelwrNRKVHqpasLREEDVY 350
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHraaLNTILDI--------------------------NRRFA----VGPDDRV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 351 IGYLPLAH---------VLELSAELVCLSHGCRigySSPQTLAD--QSSKIkkgskgdtsvlkpTLMAAVPEIMdriykn 419
Cdd:cd12114 171 LALSSLSFdlsvydifgALSAGATLVLPDEARR---RDPAHWAEliERHGV-------------TLWNSVPALL------ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 420 vmnkvnEMsafqrnlfilaynykmeqiskgcstpLCDrfVFRNVRRLLGGnIRLLLCGG--APLS---ATTQRFMNicfC 494
Cdd:cd12114 229 ------EM--------------------------LLD--VLEAAQALLPS-LRLVLLSGdwIPLDlpaRLRALAPD---A 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 495 CPVGQGyGLTESTGAGTITEVWDYNTGRV----GAPLvcceiklknweEGGYFNTDKPHPR-------GEILIGGQNVTM 563
Cdd:cd12114 271 RLISLG-GATEASIWSIYHPIDEVPPDWRsipyGRPL-----------ANQRYRVLDPRGRdcpdwvpGELWIGGRGVAL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 564 GYYKNEAKTKTDFFEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICA--YAN 641
Cdd:cd12114 339 GYLGDPELTAARFVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR-GYRIELGEIEAALQAHPGVARAVVvvLGD 417
|
410
....*....|..
gi 2268062224 642 SYHSYVIGFVVP 653
Cdd:cd12114 418 PGGKRLAAFVVP 429
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
280-633 |
2.16e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 95.68 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASitgmarriprlgqitghepaaaVELWRNRKVHQPASLREEDVYIGYLPLAHV 359
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAM----------------------VELFVRFEASQYEYPGSDNVYLAALPMFHI 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAELV-CLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSVLKPTLMAAVpeimdriyknvmnkvnemsafqrnlfila 438
Cdd:PLN02574 257 YGLSLFVVgLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALT----------------------------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 439 ynykmeQISKG-CSTPLcdrfvfrnvrrllgGNIRLLLCGGAPLSA-TTQRFMNICFCCPVGQGYGLTESTGAGT----I 512
Cdd:PLN02574 308 ------KKAKGvCGEVL--------------KSLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTrgfnT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TEVWDYNTGRVGAPLVccEIKLKNWEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIG 592
Cdd:PLN02574 368 EKLSKYSSVGLLAPNM--QAKVVDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG----WLRTGDIA 438
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2268062224 593 EFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI 633
Cdd:PLN02574 439 YFDEDGYLYIVDRLKEIIKYK-GFQIAPADLEAVLISHPEI 478
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
278-663 |
1.43e-19 |
|
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: 94.15 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIP-----RLGQITgheP----AAAVELWrnrkvhqpaslreed 348
Cdd:COG1020 616 PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGlgpgdRVLQFA---SlsfdASVWEIF--------------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 349 vyigyLPLAHvlelSAELVCLSHGCRigySSPQTLAD--QSSKIkkgskgdtsvlkpTLMAAVPeimdriyknvmnkvne 426
Cdd:COG1020 678 -----GALLS----GATLVLAPPEAR---RDPAALAEllARHRV-------------TVLNLTP---------------- 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 427 mSAFQrnLFIlaynykmEQISKGCSTPlcdrfvfrnvrrllggniRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTE 505
Cdd:COG1020 717 -SLLR--ALL-------DAAPEALPSL------------------RLVLVGGEALPPELvRRWRARLPGARLVNLYGPTE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 506 STGAGTITEVWDYNTGR----VGAPLVcceiklknweeggyfNT-----DK---PHP---RGEILIGGQNVTMGYYKNEA 570
Cdd:COG1020 769 TTVDSTYYEVTPPDADGgsvpIGRPIA---------------NTrvyvlDAhlqPVPvgvPGELYIGGAGLARGYLNRPE 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 571 KTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYH 644
Cdd:COG1020 834 LTAERFVADpfgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAredAPGD 912
|
410
....*....|....*....
gi 2268062224 645 SYVIGFVVPNQKELTELAR 663
Cdd:COG1020 913 KRLVAYVVPEAGAAAAAAL 931
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-703 |
1.67e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 90.80 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNII--ASITGMarripRLGqitghepaaavelwrnrkvhqpasLREEDVYIGYLP 355
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGE-----RLG------------------------LTEQDRLCIPVP 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 356 LAHVLELS-AELVCLSHGCRIGYssPQTLADQSSKIKKGSKGdtsvlKPTLMAAVPEImdriyknvmnkvnemsafqrnl 434
Cdd:cd05917 52 LFHCFGSVlGVLACLTHGATMVF--PSPSFDPLAVLEAIEKE-----KCTALHGVPTM---------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 435 FILAYNykmeqiskgcsTPLCDRFVFRNVRrllGGNIrlllcGGAPL-SATTQRFMNICFCCPVGQGYGLTESTGAGTIT 513
Cdd:cd05917 103 FIAELE-----------HPDFDKFDLSSLR---TGIM-----AGAPCpPELMKRVIEVMNMKDVTIAYGMTETSPVSTQT 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 514 EVWD-----YNTgrVGAPLVCCEIKLKNwEEGGyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKtdffEDENGQRWLCT 588
Cdd:cd05917 164 RTDDsiekrVNT--VGRIMPHTEAKIVD-PEGG--IVPPVGVPGELCIRGYSVMKGYWNDPEKTA----EAIDGDGWLHT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 589 GDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIGfvVPNQKELTELArtkgfk 668
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTHPKVSDVQ---------VVG--VPDERYGEEVC------ 296
|
410 420 430
....*....|....*....|....*....|....*
gi 2268062224 669 gTWEELCNSSEMENEVLKvlseAAISASLEKFEIP 703
Cdd:cd05917 297 -AWIRLKEGAELTEEDIK----AYCKGKIAHYKVP 326
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
150-616 |
1.69e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 92.91 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 150 GLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK--------ELLQTKL 221
Cdd:PRK12583 61 GLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsdyhAMLQELL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 222 KDIVSL---------VPRLRHIITVDGKPP----TWSEF---PKGVIVHTMAAVQAlgvkanvekkahsKPLPSDIAVIM 285
Cdd:PRK12583 141 PGLAEGqpgalacerLPELRGVVSLAPAPPpgflAWHELqarGETVSREALAERQA-------------SLDRDDPINIQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 286 YTSGSTGIPKGVMISHSNIIASITGMARRIprlgqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLAH----VLe 361
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNILNNGYFVAESL---------------------------GLTEHDRLCVPVPLYHcfgmVL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 362 lsAELVCLSHGCRIGYssPQTLADQSSKIKKGSKGdtsvlKPTLMAAVPEIMdriyknvmnkVNEMSAFQRNLFILAyny 441
Cdd:PRK12583 260 --ANLGCMTVGACLVY--PNEAFDPLATLQAVEEE-----RCTALYGVPTMF----------IAELDHPQRGNFDLS--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 442 kmeqiskgcstplcdrfvfrnvrrllggNIRLLLCGGAP-LSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNT 520
Cdd:PRK12583 318 ----------------------------SLRTGIMAGAPcPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 521 GR---VGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPD 597
Cdd:PRK12583 370 RRvetVGRTQPHLEVKVVD-PDG---ATVPRGEIGELCTRGYSVMKGYWNNPEATAESI--DEDG--WMHTGDLATMDEQ 441
|
490
....*....|....*....
gi 2268062224 598 GCLKIIDRKKDLVkLQAGE 616
Cdd:PRK12583 442 GYVRIVGRSKDMI-IRGGE 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
278-633 |
4.43e-19 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 91.20 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGmarriprlgQITGHEPaaavELWrnrkvhqpasLREEDVYIGYLPLA 357
Cdd:PLN02246 178 PDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQ---------QVDGENP----NLY----------FHSDDVILCVLPMF 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVClshGCRIGysspqtladqsSKIKKGSKGDTSVL-------KPTLMAAVPEIMDRIYKNvmnkvnemsaf 430
Cdd:PLN02246 235 HIYSLNSVLLC---GLRVG-----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKS----------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 431 qrnlfilaynykmeqiskgcstPLCDRFVFrnvrrllgGNIRLLLCGGAPL-----SATTQRFMNICFccpvGQGYGLTE 505
Cdd:PLN02246 290 ----------------------PVVEKYDL--------SSIRMVLSGAAPLgkeleDAFRAKLPNAVL----GQGYGMTE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 506 stgAGTI--------TEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYKN-EAKTKTDf 576
Cdd:PLN02246 336 ---AGPVlamclafaKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDpEATANTI- 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 577 feDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI 633
Cdd:PLN02246 409 --DKDG--WLHTGDIGYIDDDDELFIVDRLKELIKYK-GFQVAPAELEALLISHPSI 460
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
280-735 |
8.79e-19 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 88.16 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASitgmarriprlgqitghepAAAVelwrnrkvHQPASLREEDVYIGYLPLAHV 359
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLAS-------------------AAGL--------HSRLGFGGGDSWLLSLPLYHV 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 ---------LELSAELVCLSHgcrigysspqtlaDQSSKIKKGSKGDTSV-LKPTlmaavpeimdriyknvmnkvnemsA 429
Cdd:cd17630 54 gglailvrsLLAGAELVLLER-------------NQALAEDLAPPGVTHVsLVPT------------------------Q 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 430 FQRnlfILAynykmeqiSKGCSTPLcdrfvfrnvrrllgGNIRLLLCGGAPLS------ATTQRFmnicfccPVGQGYGL 503
Cdd:cd17630 97 LQR---LLD--------SGQGPAAL--------------KSLRAVLLGGAPIPpellerAADRGI-------PLYTTYGM 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 504 TESTGAGTITEVWDYNTGRVGAPLVCCEIKLknweeggyfntdkpHPRGEILIGGQNVTMGYYKNEakTKTDFFEDEngq 583
Cdd:cd17630 145 TETASQVATKRPDGFGRGGVGVLLPGRELRI--------------VEDGEIWVGGASLAMGYLRGQ--LVPEFNEDG--- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 584 rWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVPNQKELTe 660
Cdd:cd17630 206 -WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVVGvpdEELGQRPVAVIVGRGPADP- 282
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2268062224 661 lartkgfkgtwEELcnssemenevlkvlsEAAISASLEKFEIPlkIRLSPDPWTPETGLVtdafKLKRKELKTHY 735
Cdd:cd17630 283 -----------AEL---------------RAWLKDKLARFKLP--KRIYPVPELPRTGGG----KVDRRALRAWL 325
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
278-653 |
1.18e-18 |
|
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: 89.29 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITgmarriprlgqitghEPAAAVELWRNRKVHQPASLrEEDVYIGYLpla 357
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS---------------QPPARLDVGPGSRVAQVLSI-AFDACIGEI--- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 hvlelsaeLVCLSHGCRIGYSSP-QTLADQSSKIkkgskgDTSVLKPTLMAAVPeimDRIYKNVmnkvnemsafqrnlfi 436
Cdd:cd17653 165 --------FSTLCNGGTLVLADPsDPFAHVARTV------DALMSTPSILSTLS---PQDFPNL---------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 laynykmEQISKG---CSTPLCDRFVFRnvRRLLggnirlllcggaplsattqrfmnicfccpvgQGYGLTESTGAGTIT 513
Cdd:cd17653 212 -------KTIFLGgeaVPPSLLDRWSPG--RRLY-------------------------------NAYGPTECTISSTMT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 514 EVWDYNTGRVGAPL--VCCEIKLKNWEEggyfntdKPHPR-GEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCT 588
Cdd:cd17653 252 ELLPGQPVTIGKPIpnSTCYILDADLQP-------VPEGVvGEICISGVQVARGYLGNPALTASKFVPDpfWPGSRMYRT 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2268062224 589 GDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEA-ALKNLPLIDNicAYANSYHSYVIGFVVP 653
Cdd:cd17653 325 GDYGRWTEDGGLEFLGREDNQVKVR-GFRINLEEIEEvVLQSQPEVTQ--AAAIVVNGRLVAFVTP 387
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
280-637 |
2.68e-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: 88.30 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARriprlgqitghepaaavelWRNrkvhqpasLREEDVYIGYLPLAHV 359
Cdd:cd05935 85 DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAV-------------------WTG--------LTPSDVILACLPLFHV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAelvclshgcrigysspqtladqsskikkgskgdtsvlkpTLMAAVpeimdriykNVMNKVNEMSAFQRNLFILAY 439
Cdd:cd05935 138 TGFVG---------------------------------------SLNTAV---------YVGGTYVLMARWDRETALELI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 440 NYKMEQISKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPL-SATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDY 518
Cdd:cd05935 170 EKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMpPAVAEKLLKL-TGLRFVEGYGLTETMSQTHTNPPLRP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 519 NTGRVGAPLVCCEIKLKNWEEGGYFNtdkPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDeNGQRWLCTGDIGEFDPDG 598
Cdd:cd05935 249 KLQCLGIP*FGVDARVIDIETGRELP---PNEVGEIVVRGPQIFKGYWNRPEETEESFIEI-KGRRFFRTGDLGYMDEEG 324
|
330 340 350
....*....|....*....|....*....|....*....
gi 2268062224 599 CLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNIC 637
Cdd:cd05935 325 YFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVC 362
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
260-656 |
3.37e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 88.73 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 260 QALGVKANVEKKAHS--KPLP---SDIAVIMYTSGSTGIPKGVMISHSNIIASitgMARRIPRLGQitgHEPAAavelwr 334
Cdd:PRK12492 183 QAVPFKQALRQGRGLslKPVPvglDDIAVLQYTGGTTGLAKGAMLTHGNLVAN---MLQVRACLSQ---LGPDG------ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 335 nrkvhQPASLREEDVYIGYLPLAHVLELSAELVCL----SHGCRIgySSPQtlaDQSSKIKKGSKGDTSVL--KPTLMAA 408
Cdd:PRK12492 251 -----QPLMKEGQEVMIAPLPLYHIYAFTANCMCMmvsgNHNVLI--TNPR---DIPGFIKELGKWRFSALlgLNTLFVA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 409 vpeimdriyknvmnkvnemsafqrnlfilaynykmeqiskgcstpLCDRFVFRNVRRllgGNIRLLLCGGAPL-SATTQR 487
Cdd:PRK12492 321 ---------------------------------------------LMDHPGFKDLDF---SALKLTNSGGTALvKATAER 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 488 FMNICfCCPVGQGYGLTESTGAGTITEvwdYNT----GRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTM 563
Cdd:PRK12492 353 WEQLT-GCTIVEGYGLTETSPVASTNP---YGElarlGTVGIPVPGTALKVID-DDG---NELPLGERGELCIKGPQVMK 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 564 GYYKNEAKTKtdffEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNiCAyansy 643
Cdd:PRK12492 425 GYWQQPEATA----EALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVAN-CA----- 493
|
410
....*....|...
gi 2268062224 644 hsyVIGfvVPNQK 656
Cdd:PRK12492 494 ---AIG--VPDER 501
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
227-631 |
3.39e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 88.67 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 227 LVPR--LRHIITV---DGKPPTWSEFPKGVIVHTMAAVQAL----GVKAN-VEKKAHSKPL------PSDIAVIMYTSGS 290
Cdd:PRK05677 139 VLPKtgVKHVIVTevaDMLPPLKRLLINAVVKHVKKMVPAYhlpqAVKFNdALAKGAGQPVteanpqADDVAVLQYTGGT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 291 TGIPKGVMISHSNIIASitgMARRIPRLGqitghepaaavelwrnrkvhqpASLRE-EDVYIGYLPLAHVLELS----AE 365
Cdd:PRK05677 219 TGVAKGAMLTHRNLVAN---MLQCRALMG----------------------SNLNEgCEILIAPLPLYHIYAFTfhcmAM 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 366 LVCLSHGCRIgySSPQtlaDQSSKIKKGSKgdtsvlkptlmaavpeimdriyknvmnkvNEMSAF--QRNLFIlaynykm 443
Cdd:PRK05677 274 MLIGNHNILI--SNPR---DLPAMVKELGK-----------------------------WKFSGFvgLNTLFV------- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 444 eqiskgcstPLCDRFVFRNvrrLLGGNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLTESTGAGTITEVWDYNTGR 522
Cdd:PRK05677 313 ---------ALCNNEAFRK---LDFSALKLTLSGGMALqLATAERWKEVT-GCAICEGYGMTETSPVVSVNPSQAIQVGT 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 523 VGAPLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKI 602
Cdd:PRK05677 380 IGIPVPSTLCKVID-DDGNELPLGEV---GELCVKGPQVMKGYWQRPEATDEIL--DSDG--WLKTGDIALIQEDGYMRI 451
|
410 420
....*....|....*....|....*....
gi 2268062224 603 IDRKKDLVkLQAGEYVSLGKVEAALKNLP 631
Cdd:PRK05677 452 VDRKKDMI-LVSGFNVYPNELEDVLAALP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
278-737 |
6.60e-18 |
|
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: 87.21 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaaveLWRNRKVHQPASlreedvyigYLPLA 357
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG---------------LTSESRVLQFAS---------YTFDV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVclSHGCrigysspqtladqsskikkgskgdtsvlkptlmAAVPEIMDRiyknvMNKVNE-MSAFQRNLFI 436
Cdd:cd05918 161 SILEIFTTLA--AGGC---------------------------------LCIPSEEDR-----LNDLAGfINRLRVTWAF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 LaynykmeqiskgcsTPlcdrfvfrNVRRLLG----GNIRLLLCGGAPLSATTQ-------RFMNicfccpvgqGYGLTE 505
Cdd:cd05918 201 L--------------TP--------SVARLLDpedvPSLRTLVLGGEALTQSDVdtwadrvRLIN---------AYGPAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 506 STGAGTITEVWDYNTGR-VGAPL-VCCEIKLKNweeggyfNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDe 580
Cdd:cd05918 250 CTIAATVSPVVPSTDPRnIGRPLgATCWVVDPD-------NHDRLVPIgavGELLIEGPILARGYLNDPEKTAAAFIED- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 581 ngQRWLC------------TGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKN-LPLIDNICAYA-----NS 642
Cdd:cd05918 322 --PAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIR-GQRVELGEIEHHLRQsLPGAKEVVVEVvkpkdGS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 643 YHSYVIGFVVPNQKELTELARTKGFkgtweeLCNSSEMENEVLKVlsEAAISASLEKFEIP-LKIRLSPDPWTPeTGlvt 721
Cdd:cd05918 399 SSPQLVAFVVLDGSSSGSGDGDSLF------LEPSDEFRALVAEL--RSKLRQRLPSYMVPsVFLPLSHLPLTA-SG--- 466
|
490
....*....|....*.
gi 2268062224 722 dafKLKRKELKTHYQA 737
Cdd:cd05918 467 ---KIDRRALRELAES 479
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
286-631 |
1.14e-17 |
|
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: 86.58 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 286 YTSGSTGIPKGVMISH-SNIIASItgmarriprlgqitghepaAAVELWRnrkvhqpasLREEDVYIGYLPLAHvlelsa 364
Cdd:cd12118 140 YTSGTTGRPKGVVYHHrGAYLNAL-------------------ANILEWE---------MKQHPVYLWTLPMFH------ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 365 elvclshgCRiGYSSPQTLAdqsskikkgSKGDTSVLKPTLMAavPEIMDRIYKNvmnKVNEMSAFQRNLFILAyNYKme 444
Cdd:cd12118 186 --------CN-GWCFPWTVA---------AVGGTNVCLRKVDA--KAIYDLIEKH---KVTHFCGAPTVLNMLA-NAP-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 445 qiskgcstplcdrfvfRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCcpVGQGYGLTESTGAGTITEvW--DYNT-- 520
Cdd:cd12118 240 ----------------PSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFD--VTHVYGLTETYGPATVCA-WkpEWDElp 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 521 --------GRVGAPLVcceikLKNWEEGGYFNTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLC 587
Cdd:cd12118 301 teerarlkARQGVRYV-----GLEEVDVLDPETMKPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAF---RGG--WFH 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2268062224 588 TGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 631
Cdd:cd12118 371 SGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHP 413
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
278-638 |
1.43e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 86.85 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGQIT-GHEpaaavelwrnrkvhqpaslreedVYIGYLPL 356
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEeGCE-----------------------VVITALPL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 357 AHVLELSAE-LVCLS-HGCRIGYSSPQTLadqsskikkgsKGDTSVLKPTLMAAVPEImDRIYKNVMNkvnemsafqrnl 434
Cdd:PRK08751 264 YHIFALTANgLVFMKiGGCNHLISNPRDM-----------PGFVKELKKTRFTAFTGV-NTLFNGLLN------------ 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 435 filaynykmeqiskgcsTPLCDRFVFRNVRRLLGGnirlllcGGAPLSATTQRFMNICfCCPVGQGYGLTESTGAGTIT- 513
Cdd:PRK08751 320 -----------------TPGFDQIDFSSLKMTLGG-------GMAVQRSVAERWKQVT-GLTLVEAYGLTETSPAACINp 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 514 -EVWDYNtGRVGAPLVCCEIKLKNweeggyfNTDKPHPRGEI---LIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTG 589
Cdd:PRK08751 375 lTLKEYN-GSIGLPIPSTDACIKD-------DAGTVLAIGEIgelCIKGPQVMKGYWKRPEETAKVM--DADG--WLHTG 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2268062224 590 DIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICA 638
Cdd:PRK08751 443 DIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAMMPGVLEVAA 490
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
278-610 |
2.78e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 85.84 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMarriprlgqitghepaaavELWrnrkvHQPASLR----EEDVYIGY 353
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQM-------------------EAW-----LQPAFEKkprpDQLNFVCA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 354 LPLAHVLELSaelVCLSHGCRigysspqtladqsskikkgsKGDTSVLKPTlmaavPeimdriyKNVMNKVNEMSAFQRN 433
Cdd:PRK07059 259 LPLYHIFALT---VCGLLGMR--------------------TGGRNILIPN-----P-------RDIPGFIKELKKYQVH 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 434 LFI---LAYNYKMeqiskgcSTPLCDRFVFRNVRRLLGGnirlllcGGAPLSATTQRFMNICfCCPVGQGYGLTESTGAG 510
Cdd:PRK07059 304 IFPavnTLYNALL-------NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 511 TI--TEVWDYnTGRVGAPLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCT 588
Cdd:PRK07059 369 TCnpVDATEF-SGTIGLPLPSTEVSIRD-DDGNDLPLGEP---GEICIRGPQVMAGYWNRPDETAKVMTADG----FFRT 439
|
330 340
....*....|....*....|..
gi 2268062224 589 GDIGEFDPDGCLKIIDRKKDLV 610
Cdd:PRK07059 440 GDVGVMDERGYTKIVDRKKDMI 461
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
155-673 |
7.39e-17 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 84.41 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 155 GQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKD-IVSL---VPR 230
Cdd:PRK06087 70 GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDlILPLqnqLPQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 231 LRHIITVDGKPPTWSEFpkgvivhTMAAVQALGVKANVEKKAHSkplpSDIAVIMYTSGSTGIPKGVMISHSNIIASitg 310
Cdd:PRK06087 150 LQQIVGVDKLAPATSSL-------SLSQIIADYEPLTTAITTHG----DELAAVLFTSGTEGLPKGVMLTHNNILAS--- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 311 marriprlgqitghEPAAAVELwrnrkvhqpaSLREEDVYIGYLPLAHvlelsaelvclSHGCRIGYSSPQTLadqsski 390
Cdd:PRK06087 216 --------------ERAYCARL----------NLTWQDVFMMPAPLGH-----------ATGFLHGVTAPFLI------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 391 kkgskGDTSVL----KPT-------------LMAAVPEIMDrIYKNVMNKVNEMSAfqrnlfilaynykmeqiskgcstp 453
Cdd:PRK06087 254 -----GARSVLldifTPDaclalleqqrctcMLGATPFIYD-LLNLLEKQPADLSA------------------------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 454 lcdrfvfrnvrrllggnIRLLLCGGAPLSATT-----QRFMNICFCcpvgqgYGLTESTGAGTITEvwDYNTGRVGA--- 525
Cdd:PRK06087 304 -----------------LRFFLCGGTTIPKKVarecqQRGIKLLSV------YGSTESSPHAVVNL--DDPLSRFMHtdg 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 526 -PLVCCEIKLKNweegGYFNTDKPHPRGEILIGGQNVTMGYYKNeaKTKTDFFEDENGqrWLCTGDIGEFDPDGCLKIID 604
Cdd:PRK06087 359 yAAAGVEIKVVD----EARKTLPPGCEGEEASRGPNVFMGYLDE--PELTARALDEEG--WYYSGDLCRMDEAGYIKITG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 605 RKKDLVkLQAGEYVSLGKVEAALKNLPLI--------------DNICAYA---NSYHSyvigfvvPNQKELTE-LARTKG 666
Cdd:PRK06087 431 RKKDII-VRGGENISSREVEDILLQHPKIhdacvvampderlgERSCAYVvlkAPHHS-------LTLEEVVAfFSRKRV 502
|
....*..
gi 2268062224 667 FKGTWEE 673
Cdd:PRK06087 503 AKYKYPE 509
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
134-610 |
1.54e-16 |
|
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: 83.44 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 134 WLSYEDVFIRALDFGNGLQMLGqKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLN---ETEVTNI 210
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAilaDAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 211 ITSKELLqTKLKDIVSLVPRLRH--IITVDGKPPTwsefpkgvivhTMAAVQALGVKanvekkahskplPSDIAVIMYTS 288
Cdd:cd05931 103 LTTAAAL-AAVRAFAASRPAAGTprLLVVDLLPDT-----------SAADWPPPSPD------------PDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 289 GSTGIPKGVMISHSNIIASITGMARRiprlgqitghepaaavelwrnrkvhqpASLREEDVYIGYLPLAH----VLELsa 364
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRA---------------------------YGLDPGDVVVSWLPLYHdmglIGGL-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 365 eLVCLSHGCRIGYSSPQT-LADQSSKIKKGSKGdtsvlKPTLMAAvPeimdriykNvmnkvnemsaFqrnlfilAYNYkm 443
Cdd:cd05931 210 -LTPLYSGGPSVLMSPAAfLRRPLRWLRLISRY-----RATISAA-P--------N----------F-------AYDL-- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 444 eqiskgCstplCDRFVFRNVRRLLGGNIRLLLCGGAPLSATT-QRFMNiCFcCPVG-------QGYGLTEST-------- 507
Cdd:cd05931 256 ------C----VRRVRDEDLEGLDLSSWRVALNGAEPVRPATlRRFAE-AF-APFGfrpeafrPSYGLAEATlfvsggpp 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 508 GAGTITEVWDY----NTGRVGAP-------LVCC-------EIKLKNWEeggyfnTDKPHPR---GEILIGGQNVTMGYY 566
Cdd:cd05931 324 GTGPVVLRVDRdalaGRAVAVAAddpaareLVSCgrplpdqEVRIVDPE------TGRELPDgevGEIWVRGPSVASGYW 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2268062224 567 KNEAKTKTDFF----EDENGqrWLCTGDIGeFDPDGCLKIIDRKKDLV 610
Cdd:cd05931 398 GRPEATAETFGalaaTDEGG--WLRTGDLG-FLHDGELYITGRLKDLI 442
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
286-631 |
2.03e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.14 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 286 YTSGSTGIPKGVMISHSNIIASItgmarriprLGQITGHEPAAAvelwrnrkvhqpaslreeDVYIGYLPLAHvlelsae 365
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAYLST---------LSAIIGWEMGTC------------------PVYLWTLPMFH------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 366 lvclshgCRiGYSSPQTLAdqsskikkgSKGDTSVLKPTLMAavPEImdriYKNV-MNKVNEMSAFQRNLFILAynykme 444
Cdd:PLN03102 239 -------CN-GWTFTWGTA---------ARGGTSVCMRHVTA--PEI----YKNIeMHNVTHMCCVPTVFNILL------ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 445 qisKGCSTPLCDRfvfrnvrrllGGNIRLLLCGGAPLSATTQRFMNICFccPVGQGYGLTESTGAGTITEVWD-YN---- 519
Cdd:PLN03102 290 ---KGNSLDLSPR----------SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEWQDeWNrlpe 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 520 ------TGRVGAP-LVCCEIKLKNWEeggyfnTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLC 587
Cdd:PLN03102 355 nqqmelKARQGVSiLGLADVDVKNKE------TQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF---KHG--WLN 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2268062224 588 TGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 631
Cdd:PLN03102 424 TGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYP 466
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
278-633 |
2.83e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 82.24 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIiasitgmarriprlgqitghepaaaveLWRNRKVHQPASLREEDVYIGYLPLA 357
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNL---------------------------HWKSIDHVIALGLTASERLLVVGPLY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HV--LELSAeLVCLSHGCRIgysspqtladqssKIKKGSKGDTsvlkptLMAAVPEimDRIYKNVMNKVnemsafqrnlf 435
Cdd:PRK06145 201 HVgaFDLPG-IAVLWVGGTL-------------RIHREFDPEA------VLAAIER--HRLTCAWMAPV----------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 436 ilaynykmeQISKGCSTPLCDRFVFRNVRRLLGGNIRlllcggAP---LSATTQRFMNICFCcpvgQGYGLTESTGAGTI 512
Cdd:PRK06145 248 ---------MLSRVLTVPDRDRFDLDSLAWCIGGGEK------TPesrIRDFTRVFTRARYI----DAYGLTETCSGDTL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TEVWDY--NTGRVGAPLVCCEIKLKNwEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGD 590
Cdd:PRK06145 309 MEAGREieKIGSTGRALAHVEIRIAD-GAGRWL---PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----WFRSGD 379
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2268062224 591 IGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLI 633
Cdd:PRK06145 380 VGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEV 421
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
278-610 |
6.66e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 81.08 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASitgmarriprlgqitghePAAAVELWRnrkvhqpasLREEDVYIGYLPLA 357
Cdd:PRK07514 155 ADDLAAILYTSGTTGRSKGAMLSHGNLLSN------------------ALTLVDYWR---------FTPDDVLIHALPIF 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVlelsaelvclsHGCRIgySSPQTLADQSSKIKKgSKGDTSVL-----KPTLMAAVPEIMDRIYKNvmnkvnemsafqr 432
Cdd:PRK07514 208 HT-----------HGLFV--ATNVALLAGASMIFL-PKFDPDAVlalmpRATVMMGVPTFYTRLLQE------------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 433 nlfilaynykmeqiskgcstplcDRFVfrnvrRLLGGNIRLLLCGGAPLSATTQRfmniCFCCPVGQG----YGLTEsTG 508
Cdd:PRK07514 261 -----------------------PRLT-----REAAAHMRLFISGSAPLLAETHR----EFQERTGHAilerYGMTE-TN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 509 ------------AGTitevwdyntgrVGAPLVCCEIKLKNWEEGgyfntdKPHPRGE---ILIGGQNVTMGYYKNEAKTK 573
Cdd:PRK07514 308 mntsnpydgerrAGT-----------VGFPLPGVSLRVTDPETG------AELPPGEigmIEVKGPNVFKGYWRMPEKTA 370
|
330 340 350
....*....|....*....|....*....|....*..
gi 2268062224 574 TDFFEDenGqrWLCTGDIGEFDPDGCLKIIDRKKDLV 610
Cdd:PRK07514 371 EEFRAD--G--FFITGDLGKIDERGYVHIVGRGKDLI 403
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
135-627 |
9.39e-16 |
|
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: 80.88 E-value: 9.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQTKLKDIVSLVPRLRHIITVDGKPPtwsEFPKGVIVHTMAAVQALGVKANVEkkahskplPSDIAVIMYTSGSTGIP 294
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIVSGGAGP---EAGALLLAELVAAEAEQLKPAATH--------ADDPAFWLYSSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 295 KGVMISHSNIIASITGMARRIprLGqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHVLELSAELVC-LSHGC 373
Cdd:cd05959 179 KGVVHLHADIYWTAELYARNV--LG------------------------IREDDVCFSAAKLFFAYGLGNSLTFpLSVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RI----GYSSPQTLADqssKIKKGskgdtsvlKPTLMAAVPEimdrIYkNVMNKVNEMSafQRNLfilaynykmeqiskg 449
Cdd:cd05959 233 TTvlmpERPTPAAVFK---RIRRY--------RPTVFFGVPT----LY-AAMLAAPNLP--SRDL--------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 450 cstplcdrfvfrnvrrllgGNIRLLLCGGAPLSATT-QRFMNIcFCCPVGQGYGLTE------STGAGTItevwDYNTgr 522
Cdd:cd05959 280 -------------------SSLRLCVSAGEALPAEVgERWKAR-FGLDILDGIGSTEmlhiflSNRPGRV----RYGT-- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 523 VGAPLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDfFEDEngqrWLCTGDIGEFDPDGCLKI 602
Cdd:cd05959 334 TGKPVPGYEVELRD-EDGGDVADGEP---GELYVRGPSSATMYWNNRDKTRDT-FQGE----WTRTGDKYVRDDDGFYTY 404
|
490 500
....*....|....*....|....*
gi 2268062224 603 IDRKKDLVKLqAGEYVSLGKVEAAL 627
Cdd:cd05959 405 AGRADDMLKV-SGIWVSPFEVESAL 428
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-636 |
1.08e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 80.79 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 269 EKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASI--TGMARRIPRLGQITGhepaaavelwrnrkvhqpaslre 346
Cdd:PLN02330 174 DTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsSLFSVGPEMIGQVVT----------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 347 edvyIGYLPLAHVLELSAelVCLShgcrigysspqTLADQSsKIKKGSKGDTSVLKPTLMAA-------VPEIMDRIYKN 419
Cdd:PLN02330 231 ----LGLIPFFHIYGITG--ICCA-----------TLRNKG-KVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 420 vmnkvnemsafqrnlfilaynykmeqiskgcstPLCDRFVFRNVRrllggnIRLLLCGGAPL-----SATTQRFMNIcfc 494
Cdd:PLN02330 293 ---------------------------------PIVEEFDLSKLK------LQAIMTAAAPLapellTAFEAKFPGV--- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 495 cPVGQGYGLTESTGAgTITEvWDYNTGR-------VGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYK 567
Cdd:PLN02330 331 -QVQEAYGLTEHSCI-TLTH-GDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYN 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2268062224 568 NeaKTKTDFFEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNI 636
Cdd:PLN02330 405 N--KEETDRTIDEDG--WLHTGDIGYIDDDGDIFIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDA 468
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
277-656 |
1.10e-15 |
|
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: 80.20 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 277 LPSDIAVIMYTSGSTGIPKGVMISHSNIIAS------ITGMARRIPRLGQItghepaaavelwrnrkvhqpASLrEEDVY 350
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAahawrrEYELDSFPVRLLQM--------------------ASF-SFDVF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 351 IGylPLAHVLELSAELVCLSHGCRIgysSPQTLADqsskIKKGSKGDTSVLKPTLMAAVpeiMDRIYKNvmnkvnEMSAF 430
Cdd:cd17650 150 AG--DFARSLLNGGTLVICPDEVKL---DPAALYD----LILKSRITLMESTPALIRPV---MAYVYRN------GLDLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 431 QRNLFILAynykmeqiSKGCstPLCDrfvFRNVRRLLGGNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESTGAG 510
Cdd:cd17650 212 AMRLLIVG--------SDGC--KAQD---FKTLAARFGQGMRII------------------------NSYGVTEATIDS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 511 TITEVWDYNTGR-----VGAPLVCCEIKLKNweeggyfNTDKPHP---RGEILIGGQNVTMGYYKNEAKTKTDFFED--E 580
Cdd:cd17650 255 TYYEEGRDPLGDsanvpIGRPLPNTAMYVLD-------ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVENpfA 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2268062224 581 NGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVPNQK 656
Cdd:cd17650 328 PGERMYRTGDLARWRADGNVELLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVVAVredKGGEARLCAYVVAAAT 405
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
229-633 |
1.41e-15 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 80.48 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 229 PRLRHIITVDGK----------PPTWSEFPkgvivhtmAAVQALgvkanvekkAHSKPLPSDIAVIMYTSGSTGIPKGVM 298
Cdd:PRK13295 154 PALRHVVVVGGDgadsfealliTPAWEQEP--------DAPAIL---------ARLRPGPDDVTQLIYTSGTTGEPKGVM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 299 ISHSNIIASITGMARRIpRLGQitghepaaavelwrnrkvhqpaslreEDVYIGYLPLAHvlelsaeLVCLSHGCRIGYS 378
Cdd:PRK13295 217 HTANTLMANIVPYAERL-GLGA--------------------------DDVILMASPMAH-------QTGFMYGLMMPVM 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 379 SPQT--LADQSSKIKKGSKGDTSVLKPTlMAAVPEIMDriyknvMNKVNEMSAfqrnlfilaynykmeqiskgcstplcd 456
Cdd:PRK13295 263 LGATavLQDIWDPARAAELIRTEGVTFT-MASTPFLTD------LTRAVKESG--------------------------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 457 rfvfRNVRRLlggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEsTGAGTITEVWDYN---TGRVGAPLVCCEIK 533
Cdd:PRK13295 309 ----RPVSSL-----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTE-NGAVTLTKLDDPDeraSTTDGCPLPGVEVR 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 534 LKNweeggyfNTDKPHPRGEI---LIGGQNVTMGYYKNEAKTKTDFfedengQRWLCTGDIGEFDPDGCLKIIDRKKDLV 610
Cdd:PRK13295 379 VVD-------ADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGTDA------DGWFDTGDLARIDADGYIRISGRSKDVI 445
|
410 420
....*....|....*....|...
gi 2268062224 611 kLQAGEYVSLGKVEAALKNLPLI 633
Cdd:PRK13295 446 -IRGGENIPVVEIEALLYRHPAI 467
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
279-610 |
1.61e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 80.08 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 279 SDIAVIMYTSGSTGIPKGVMISHSNIIASiTGMArriprlgqitghepaaavelwrnrkVHQPASLRE-EDVYIGYLPLA 357
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSN-TLMG-------------------------VQWLYNCKEgEEVVLGVLPFF 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELvclshgcrigysspqtladqsskikkgskgDTSVLKPTLMAAVPEI-MDRIYKNVMNKVNEMSAFQRNLFI 436
Cdd:PRK06710 260 HVYGMTAVM------------------------------NLSIMQGYKMVLIPKFdMKMVFEAIKKHKVTLFPGAPTIYI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 LAYNykmeqiskgcsTPLCDRFVFrnvrrllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVW 516
Cdd:PRK06710 310 ALLN-----------SPLLKEYDI--------SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 517 DYNT-GRVGAPLVCCEIKLKNWEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFD 595
Cdd:PRK06710 371 EKRVpGSIGVPWPDTEAMIMSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETAAVL---QDG--WLHTGDVGYMD 442
|
330
....*....|....*
gi 2268062224 596 PDGCLKIIDRKKDLV 610
Cdd:PRK06710 443 EDGFFYVKDRKKDMI 457
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-640 |
1.66e-15 |
|
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: 79.79 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 276 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASitgmARRI-PRLGqitghepaaavelwrnrkvhqpasLREEDVYIGYL 354
Cdd:cd05922 114 VSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN----ARSIaEYLG------------------------ITADDRALTVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 355 PLAHVLELSaelVCLSHgcrigysspqTLADQSSKIKKGSKGDTSVLKP------TLMAAVP---EIMDRIyknvmnkvn 425
Cdd:cd05922 166 PLSYDYGLS---VLNTH----------LLRGATLVLTNDGVLDDAFWEDlrehgaTGLAGVPstyAMLTRL--------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 426 emsafqrnlfilaynykmeqISKGCSTPlcdrfvfrnvrrllggNIRLLLCGGAPLSATT-QRFmnicfcCPVGQG---- 500
Cdd:cd05922 224 --------------------GFDPAKLP----------------SLRYLTQAGGRLPQETiARL------RELLPGaqvy 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 501 --YGLTESTGAGTI--TEVWDYNTGRVGAPLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEA-KTKTD 575
Cdd:cd05922 262 vmYGQTEATRRMTYlpPERILEKPGSIGLAIPGGEFEILD-DDGTPTPPGEP---GEIVHRGPNVMKGYWNDPPyRRKEG 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2268062224 576 FFEDEngqrwLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNICAYA 640
Cdd:cd05922 338 RGGGV-----LHTGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIEAAARSIGLIIEAAAVG 396
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
278-732 |
2.95e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 79.46 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIA-SITGMArriprlgqITGHEpaaavelwrnrkvhqpaslrEEDVYIGYLPL 356
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVqSLAKIA--------IVGYG--------------------EDDVYLHTAPL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 357 AHVLELSAELVCLSHG-CRIGYSspqtladqsskiKKGSKGDTSVLKP---TLMAAVPEIM-Driyknvmnkvnemsafq 431
Cdd:PLN02860 223 CHIGGLSSALAMLMVGaCHVLLP------------KFDAKAALQAIKQhnvTSMITVPAMMaD----------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 432 rnlfILAYNyKMEQISKGcstplcdrfvFRNVRRLL--GGNIRLLLcggapLSATTQRFMnicfCCPVGQGYGLTES--- 506
Cdd:PLN02860 274 ----LISLT-RKSMTWKV----------FPSVRKILngGGSLSSRL-----LPDAKKLFP----NAKLFSAYGMTEAcss 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 507 ------------TGAGTITEVWDYNTGRVGAPLVCC--------EIKLKnweeggyfnTDKPHPRGEILIGGQNVTMGYY 566
Cdd:PLN02860 330 ltfmtlhdptleSPKQTLQTVNQTKSSSVHQPQGVCvgkpaphvELKIG---------LDESSRVGRILTRGPHVMLGYW 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 567 KNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNicayansyhSY 646
Cdd:PLN02860 401 GQNSETASVLSNDG----WLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVAS---------VV 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 647 VIGfvVPNQKeLTELA----RTKGfKGTWEELCNSSEMENEVL--KVLSEAAISASLEKFEIPLKIRLSPDPWTpetglV 720
Cdd:PLN02860 467 VVG--VPDSR-LTEMVvacvRLRD-GWIWSDNEKENAKKNLTLssETLRHHCREKNLSRFKIPKLFVQWRKPFP-----L 537
|
490
....*....|..
gi 2268062224 721 TDAFKLKRKELK 732
Cdd:PLN02860 538 TTTGKIRRDEVR 549
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
152-637 |
5.98e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 78.46 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 152 QMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSLvpRL 231
Cdd:PRK08314 54 QECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNL--RL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 232 RHII--------TVDG--KPPTWSEFPKGVIVHTMAAVQAL--GVKANVEKKAHSkPLPSDIAVIMYTSGSTGIPKGVMI 299
Cdd:PRK08314 132 RHVIvaqysdylPAEPeiAVPAWLRAEPPLQALAPGGVVAWkeALAAGLAPPPHT-AGPDDLAVLPYTSGTTGVPKGCMH 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 300 SHSNIIASITGMArriprlgqitghepaaaveLWRNrkvhqpasLREEDVYIGYLPLAHVLelsaelvclshGCRIGYSS 379
Cdd:PRK08314 211 THRTVMANAVGSV-------------------LWSN--------STPESVVLAVLPLFHVT-----------GMVHSMNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 380 PqtladqsskIKKGSkgdTSVLKPTL-MAAVPEIMDRiYKnVMNKVNeMSAFQRNLFilaynykmeqiskgcSTPLCDRF 458
Cdd:PRK08314 253 P---------IYAGA---TVVLMPRWdREAAARLIER-YR-VTHWTN-IPTMVVDFL---------------ASPGLAER 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 459 VFRNVRrLLGGnirlllcGGAPL-SATTQRFM---NICFCcpvgQGYGLTEsTGAGTITEVWDyntgrvgAP-LVCCEIK 533
Cdd:PRK08314 303 DLSSLR-YIGG-------GGAAMpEAVAERLKeltGLDYV----EGYGLTE-TMAQTHSNPPD-------RPkLQCLGIP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 534 LknweeggyFNTD---------KPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDEnGQRWLCTGDIGEFDPDGCLK 601
Cdd:PRK08314 363 T--------FGVDarvidpetlEELPPgevGEIVVHGPQVFKGYWNRPEATAEAFIEID-GKRFFRTGDLGRMDEEGYFF 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 2268062224 602 IIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNIC 637
Cdd:PRK08314 434 ITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEAC 468
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
278-660 |
6.23e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 78.56 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASItgmarriprlgqitghEPAAAVelwrnrkvHQPASLREEDVYIGYLPLA 357
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANL----------------EQAKAA--------YGPLLHPGKELVVTALPLY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVCLSHgcrigysspqtladqsskikkgsKGDTSVL--KPTLMAAVPEIMDRIYKNVMNKVNemsafqrNLF 435
Cdd:PRK08974 261 HIFALTVNCLLFIE-----------------------LGGQNLLitNPRDIPGFVKELKKYPFTAITGVN-------TLF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 436 ILAYNYKmeqiskgcstplcdrfvfrNVRRLLGGNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLTESTG--AGTI 512
Cdd:PRK08974 311 NALLNNE-------------------EFQELDFSSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTECSPlvSVNP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TEVWDYNtGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKtDFFEDEngqrWLCTGDIG 592
Cdd:PRK08974 371 YDLDYYS-GSIGLPVPSTEIKLVD-DDG---NEVPPGEPGELWVKGPQVMLGYWQRPEATD-EVIKDG----WLATGDIA 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2268062224 593 EFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHS---YVIGFVVPNQKELTE 660
Cdd:PRK08974 441 VMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLTE 510
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
130-664 |
8.26e-15 |
|
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: 78.09 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 130 GHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFmynfqLVTLYATLGGPAIVHGLNETEVTN 209
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACV-----LAGFVPAPLTVPPTYDEPNARLRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 210 IitsKELLQTKLKDIV----SLVPRLRHIITVDGkpptwsefpkgvivHTMAAVQALGVKANVEKKAHSKPL-PSDIAVI 284
Cdd:cd05906 110 L---RHIWQLLGSPVVltdaELVAEFAGLETLSG--------------LPGIRVLSIEELLDTAADHDLPQSrPDDLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 285 MYTSGSTGIPKGVMISHSNIIASITG---MARRIPR---LGQITGHEPAAAVELwrnrkvhqpaSLReeDVYIG----YL 354
Cdd:cd05906 173 MLTSGSTGFPKAVPLTHRNILARSAGkiqHNGLTPQdvfLNWVPLDHVGGLVEL----------HLR--AVYLGcqqvHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 355 PLAHVLELSAELVCLSHGCRIGYS-SPQ----TLADQSSKIkKGSKGDTSVLKPTLMAAvpeimdriyknvmnkvnemsa 429
Cdd:cd05906 241 PTEEILADPLRWLDLIDRYRVTITwAPNfafaLLNDLLEEI-EDGTWDLSSLRYLVNAG--------------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 430 fqrnlfilaynykmEQIskgcstplcdrfVFRNVRRLLggniRLLLCGGAPlsattQRFMNICFccpvgqgyGLTEsTGA 509
Cdd:cd05906 299 --------------EAV------------VAKTIRRLL----RLLEPYGLP-----PDAIRPAF--------GMTE-TCS 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 510 GTItevWD-----YNTGR------VGAPLVCCEIKLKNWEEGGyfntdKPHPR-GEILIGGQNVTMGYYKNEAKTKTDFF 577
Cdd:cd05906 335 GVI---YSrsfptYDHSQalefvsLGRPIPGVSMRIVDDEGQL-----LPEGEvGRLQVRGPVVTKGYYNNPEANAEAFT 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 578 EDEngqrWLCTGDIGeFDPDGCLKIIDRKKDLVKLQAGEYvSLGKVEAALKNLPLIDN--ICAYA-----NSYHSYVIgF 650
Cdd:cd05906 407 EDG----WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNY-YSHEIEAAVEEVPGVEPsfTAAFAvrdpgAETEELAI-F 479
|
570
....*....|....
gi 2268062224 651 VVPNQKELTELART 664
Cdd:cd05906 480 FVPEYDLQDALSET 493
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
125-631 |
2.33e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 76.44 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 125 KKVILGHYNWLSYEDVFIRALDFGNGLQM-LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLN 203
Cdd:PRK06839 18 RIAIITEEEEMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 204 ETEVTNIITSKELLQTKLKdivslvprLRHIITVdgKPPTWSEFPKGVIVHTmaavqalgvKANVEKKAHSKPLpsdiaV 283
Cdd:PRK06839 98 DSGTTVLFVEKTFQNMALS--------MQKVSYV--QRVISITSLKEIEDRK---------IDNFVEKNESASF-----I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 284 IMYTSGSTGIPKGVMISHSNIiasitgmarriprlgqitghepaaaveLWRnrKVHQPAS--LREEDVYIGYLPLAHV-- 359
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENM---------------------------FWN--ALNNTFAidLTMHDRSIVLLPLFHIgg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAeLVCLSHGCRIgysspqTLADQSSKIKKGSKGDTSvlKPTLMAAVPEIMDRIYKnvmnkvnemsafqrnlfilay 439
Cdd:PRK06839 205 IGLFA-FPTLFAGGVI------IVPRKFEPTKALSMIEKH--KVTVVMGVPTIHQALIN--------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 440 nykmeqiskgcstplCDRFVFRNVRrllggNIRLLLCGGAPLSAT-TQRFMNICFccPVGQGYGLTESTGAGTITEVWDY 518
Cdd:PRK06839 255 ---------------CSKFETTNLQ-----SVRWFYNGGAPCPEElMREFIDRGF--LFGQGFGMTETSPTVFMLSEEDA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 519 --NTGRVGAPLVCCEIKL-----KNWEEGGYfntdkphprGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDI 591
Cdd:PRK06839 313 rrKVGSIGKPVLFCDYELidenkNKVEVGEV---------GELLIRGPNVMKEYWNRPDATEETI---QDG--WLCTGDL 378
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2268062224 592 GEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 631
Cdd:PRK06839 379 ARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLS 417
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
181-630 |
2.75e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.93 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 181 MYNFqlvtlyaTLGGPAIVHGLNETEVTNIITSKELL-QTKLKDIVSLVPRLRHIITVDgkpptwsEFPKGVivHTMAAV 259
Cdd:PRK06814 711 MINF-------SAGIANILSACKAAQVKTVLTSRAFIeKARLGPLIEALEFGIRIIYLE-------DVRAQI--GLADKI 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 260 QAL--GVKANVEKKAHSkplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrk 337
Cdd:PRK06814 775 KGLlaGRFPLVYFCNRD---PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID--------------------- 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 338 vhqpasLREEDVYIGYLPLAHVLELSAELVC-LSHGCRIG-YSSPQTladqsskikkgskgdtsvlkptlMAAVPEImdr 415
Cdd:PRK06814 831 ------FSPEDKVFNALPVFHSFGLTGGLVLpLLSGVKVFlYPSPLH-----------------------YRIIPEL--- 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 416 IYknvmnKVNEMSAFQRNLFILAY-NYkmeqiskgcstplCDRFVFRnvrrllggNIRLLLCGGAPLSATTQRFMNICFC 494
Cdd:PRK06814 879 IY-----DTNATILFGTDTFLNGYaRY-------------AHPYDFR--------SLRYVFAGAEKVKEETRQTWMEKFG 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 495 CPVGQGYGLTEStgagtiTEVWDYNT------GRVGAPLVCCEIKLK---NWEEGgyfntdkphprGEILIGGQNVTMGY 565
Cdd:PRK06814 933 IRILEGYGVTET------APVIALNTpmhnkaGTVGRLLPGIEYRLEpvpGIDEG-----------GRLFVRGPNVMLGY 995
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2268062224 566 YKNEAKTKTDffEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNL 630
Cdd:PRK06814 996 LRAENPGVLE--PPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKI-AGEMISLAAVEELAAEL 1055
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
272-627 |
3.74e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.41 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 272 AHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMArriprlgqitghepaaavELWRnrkvhqpasLREEDVYI 351
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALA------------------EAWQ---------WTADDVLV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 352 GYLPLAHVlelsaelvclsHGC--------RIGYS-------SPQTLADQSSkikkgskgdtsvLKPTLMAAVPEIMDRI 416
Cdd:PRK07787 174 HGLPLFHV-----------HGLvlgvlgplRIGNRfvhtgrpTPEAYAQALS------------EGGTLYFGVPTVWSRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 417 YKNvmnkvnEMSAfqrnlfilaynykmeqiskgcstplcdrfvfrnvrRLLGGnIRLLLCGGAPLSATT-QRFMNICFCC 495
Cdd:PRK07787 231 AAD------PEAA-----------------------------------RALRG-ARLLVSGSAALPVPVfDRLAALTGHR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 496 PVgQGYGLTE-----STGA-GtitevwDYNTGRVGAPLVCCEIKLKnwEEGGyfnTDKPHPR---GEILIGGQNVTMGYY 566
Cdd:PRK07787 269 PV-ERYGMTEtlitlSTRAdG------ERRPGWVGLPLAGVETRLV--DEDG---GPVPHDGetvGELQVRGPTLFDGYL 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2268062224 567 KNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKK-DLVKlqAGEY-VSLGKVEAAL 627
Cdd:PRK07787 337 NRPDATAAAFTADG----WFRTGDVAVVDPDGMHRIVGREStDLIK--SGGYrIGAGEIETAL 393
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
150-610 |
3.95e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 75.62 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 150 GLQMLGQKPKANIAIFCETRAEWmiaaqacfmynfqLVTLYAT--LG------GPA-----IVHGLNETEVTNIITSK-- 214
Cdd:PRK08315 59 GLLALGIEKGDRVGIWAPNVPEW-------------VLTQFATakIGailvtiNPAyrlseLEYALNQSGCKALIAADgf 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ------ELLQT---KLKDIV------SLVPRLRHIITVDGKPP----TWSEfpkgvivhtmaaVQALGVKANVEK-KAHS 274
Cdd:PRK08315 126 kdsdyvAMLYElapELATCEpgqlqsARLPELRRVIFLGDEKHpgmlNFDE------------LLALGRAVDDAElAARQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 275 KPLPSDIAV-IMYTSGSTGIPKGVMISHSNII--ASITGMARRiprlgqitghepaaavelwrnrkvhqpasLREED--- 348
Cdd:PRK08315 194 ATLDPDDPInIQYTSGTTGFPKGATLTHRNILnnGYFIGEAMK-----------------------------LTEEDrlc 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 349 --VyigylPLAH----VLelsAELVCLSHGCRIGYSSP--------QTLADQSSKIKKG--------------SKGDTSV 400
Cdd:PRK08315 245 ipV-----PLYHcfgmVL---GNLACVTHGATMVYPGEgfdplatlAAVEEERCTALYGvptmfiaeldhpdfARFDLSS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 401 LKPTLMAAVP---EIMdriyKNVMNKVNemsafqrnlfilaynykMEQISkgcstplcdrfvfrnvrrllggnirlllcg 477
Cdd:PRK08315 317 LRTGIMAGSPcpiEVM----KRVIDKMH-----------------MSEVT------------------------------ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 478 gaplsattqrfmnICfccpvgqgYGLTESTGAGTITEVWD---YNTGRVGAPLVCCEIKLKNWEEGgyfNTDKPHPRGEI 554
Cdd:PRK08315 346 -------------IA--------YGMTETSPVSTQTRTDDpleKRVTTVGRALPHLEVKIVDPETG---ETVPRGEQGEL 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2268062224 555 LIGGQNVTMGYYKNEAKTKtdffE--DENGqrWLCTGDIGEFDPDGCLKIIDRKKDLV 610
Cdd:PRK08315 402 CTRGYSVMKGYWNDPEKTA----EaiDADG--WMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
230-631 |
5.26e-14 |
|
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: 74.93 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 230 RLRHIITvDGKPP---TWSEFPKGVIVHTMAAVQALGVKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIa 306
Cdd:cd12117 85 RLAFMLA-DAGAKvllTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVV- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 307 sitgmarripRLGQITGHepaaavelwrnrkvhqpASLREEDVYIGYLPL---AHVLELsaeLVCLSHGCRIGYSSPQTL 383
Cdd:cd12117 163 ----------RLVKNTNY-----------------VTLGPDDRVLQTSPLafdASTFEI---WGALLNGARLVLAPKGTL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 384 ADQSSkikkgskgdtsvlkptLMAAVPEimdriyknvmNKVNEM---SAfqrnLF-ILAynykmeQISKGCstplcdrfv 459
Cdd:cd12117 213 LDPDA----------------LGALIAE----------EGVTVLwltAA----LFnQLA------DEDPEC--------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 460 FRNVRRLL-GGN------IRLLLCGGAPLsattqRFMNicfccpvgqGYGLTESTGAGT---ITEVwDYNTGRV--GAPL 527
Cdd:cd12117 248 FAGLRELLtGGEvvspphVRRVLAACPGL-----RLVN---------GYGPTENTTFTTshvVTEL-DEVAGSIpiGRPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 528 VcceiklknweeggyfNTD--------KPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEF 594
Cdd:cd12117 313 A---------------NTRvyvldedgRPVPPgvpGELYVGGDGLALGYLNRPALTAERFVADpfGPGERLYRTGDLARW 377
|
410 420 430
....*....|....*....|....*....|....*..
gi 2268062224 595 DPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 631
Cdd:cd12117 378 LPDGRLEFLGRIDDQVKIR-GFRIELGEIEAALRAHP 413
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
276-653 |
5.40e-14 |
|
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: 75.00 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 276 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIP-----RLGQITghepaaavelwrnrkvhqPASLreeDVy 350
Cdd:cd17646 135 PRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPlgpgdRVLQKT------------------PLSF---DV- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 351 igylplaHVLELsaeLVCLSHGCRIGYSSPQTLADqsskikkgskgdtsvlkptlMAAVPEIMDRIYKNVMNKVNEMSAf 430
Cdd:cd17646 193 -------SVWEL---FWPLVAGARLVVARPGGHRD--------------------PAYLAALIREHGVTTCHFVPSMLR- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 431 qrnLFIlaynykmEQISKGCSTPLcdrfvfrnvrrllggniRLLLCGGAPLSA-TTQRFMNIcFCCPVGQGYGLTESTga 509
Cdd:cd17646 242 ---VFL-------AEPAAGSCASL-----------------RRVFCSGEALPPeLAARFLAL-PGAELHNLYGPTEAA-- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 510 gtITEVWDYNTGRVGAPLVccEIKLKNWEEGGYFNTD--KPHPRG---EILIGGQNVTMGYYKNEAKTKTDFFED--ENG 582
Cdd:cd17646 292 --IDVTHWPVRGPAETPSV--PIGRPVPNTRLYVLDDalRPVPVGvpgELYLGGVQLARGYLGRPALTAERFVPDpfGPG 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2268062224 583 QRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 653
Cdd:cd17646 368 SRMYRTGDLARWRPDGALEFLGRSDDQVKIR-GFRVEPGEIEAALAAHPAVTHAVVVAraaPAGAARLVGYVVP 440
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
256-633 |
5.56e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 75.23 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 256 MAAVQALGVKANVEKKAHSKPLPSD-IAVIMYTSGSTGIPKGVMISHSNIIASitgmARRIPRLGQITGHEpaaavelwr 334
Cdd:PRK09088 111 VEDLAAFIASADALEPADTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQT----AHNFGVLGRVDAHS--------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 335 nrkvhqpaslreedVYIGYLPLAHVLELSAEL-VCLSHGCRI----GYSSPQTLadqsskikkGSKGDTSvLKPTLMAAV 409
Cdd:PRK09088 178 --------------SFLCDAPMFHIIGLITSVrPVLAVGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 410 PEIMDRIYknvmnkvnemsafqrnlfilaynykmeqiskgcSTPlcdRFVFRNVRRLLGgnirlLLCGGAPLSATTQRFM 489
Cdd:PRK09088 234 PQMAQAFR---------------------------------AQP---GFDAAALRHLTA-----LFTGGAPHAAEDILGW 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 490 nICFCCPVGQGYGLTEstgAGTI------TEVWDYNTGRVGAPLVCCEIKLKNWEEggyfNTDKPHPRGEILIGGQNVTM 563
Cdd:PRK09088 273 -LDDGIPMVDGFGMSE---AGTVfgmsvdCDVIRAKAGAAGIPTPTVQTRVVDDQG----NDCPAGVPGELLLRGPNLSP 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 564 GYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLI 633
Cdd:PRK09088 345 GYWRRPQATARAF--TGDG--WFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
278-655 |
7.65e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.97 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiPRLGQITghepaaavelwRNRKVHQPASlreeDVYigylpla 357
Cdd:PRK12467 655 PDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADD-----------SMLMVSTFAF----DLG------- 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 hVLELsaeLVCLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSVLKptlmaAVPeimdriyknvmnkvnemSAFQRNLfil 437
Cdd:PRK12467 712 -VTEL---FGALASGATLHLLPPDCARDAEAFAALMADQGVTVLK-----IVP-----------------SHLQALL--- 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 438 aynykmeqiSKGCSTPlcdrfvfrnVRRLlggniRLLLCGGAPLS-ATTQRFMNICFCCPVGQGYGLTESTGAGTITEV- 515
Cdd:PRK12467 763 ---------QASRVAL---------PRPQ-----RALVCGGEALQvDLLARVRALGPGARLINHYGPTETTVGVSTYELs 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 516 ---WDYNTGRVGAPLVCCEIKLKNweegGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTG 589
Cdd:PRK12467 820 deeRDFGNVPIGQPLANLGLYILD----HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgADGGRLYRTG 895
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2268062224 590 DIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPNQ 655
Cdd:PRK12467 896 DLARYRADGVIEYLGRMDHQVKIR-GFRIELGEIEARLLAQPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
278-665 |
7.66e-14 |
|
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: 74.27 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGmARRIPRLGQ----ITGHEPA---AAVELWrnrkvhqpaslreedvy 350
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEddvwTLFHSYAfdfSVWEIW----------------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 351 igyLPLAHvlelSAELVCLSHGCRigySSPQTLADQsskIKKGskgdtsvlKPTLMAAVPeimdriyknvmnkvnemSAF 430
Cdd:cd17643 154 ---GALLH----GGRLVVVPYEVA---RSPEDFARL---LRDE--------GVTVLNQTP-----------------SAF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 431 QRnlFILAynykmeqiskgcstplcdrfVFRNVRRLLggNIRLLLCGGAPLSATTQRFMNICFCCPVGQ---GYGLTEST 507
Cdd:cd17643 196 YQ--LVEA--------------------ADRDGRDPL--ALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 508 GAGTITEV-----WDYNTGRVGAPLVCCEIKLKNweeggyfNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED 579
Cdd:cd17643 252 VHVTFRPLdaadlPAAAASPIGRPLPGLRVYVLD-------ADGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVAN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 580 EN---GQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYANSYH---SYVIGFVVP 653
Cdd:cd17643 325 PFggpGSRMYRTGDLARRLPDGELEYLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDEpgdTRLVAYVVA 403
|
410
....*....|....*...
gi 2268062224 654 NQK------ELTELARTK 665
Cdd:cd17643 404 DDGaaadiaELRALLKEL 421
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
135-627 |
9.05e-14 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 74.49 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQTkLKDIVSLVPRLRHIITVDGKPPTWSEFpkgvivhtmaaVQALGVKANVEKKAHSKPlpSDIAVIMYTSGSTGIP 294
Cdd:TIGR02262 111 ALLPV-IKAALGKSPHLEHRVVVGRPEAGEVQL-----------AELLATESEQFKPAATQA--DDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 295 KGVMISHSNIIASITGMARriPRLGqitghepaaavelwrnrkvhqpasLREEDVYigylplahvleLSAELVCLSHGCR 374
Cdd:TIGR02262 177 KGVVHTHSNPYWTAELYAR--NTLG------------------------IREDDVC-----------FSAAKLFFAYGLG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 375 IGYSSPQTLadqsskikkgskGDTSVL---KPTlMAAVPEIMDRiyknvmnkvnemsaFQRNLFIlaynykmeqiskGCS 451
Cdd:TIGR02262 220 NALTFPMSV------------GATTVLmgeRPT-PDAVFDRLRR--------------HQPTIFY------------GVP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 452 TPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTE------STGAGtitevwDYNTGRVGA 525
Cdd:TIGR02262 261 TLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEmlhiflSNLPG------DVRYGTSGK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 526 PLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDR 605
Cdd:TIGR02262 335 PVPGYRLRLVG-DGGQDVADGEP---GELLISGPSSATMYWNNRAKSRDTFQGE-----WTRSGDKYVRNDDGSYTYAGR 405
|
490 500
....*....|....*....|..
gi 2268062224 606 KKDLVKLqAGEYVSLGKVEAAL 627
Cdd:TIGR02262 406 TDDMLKV-SGIYVSPFEIESAL 426
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
135-665 |
2.52e-13 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 73.22 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFmynfQL----VTLYATLGGPAIVHGLNETEVTNI 210
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACA----RIgavhSPVFPGFGAEALADRIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 211 ITSKEL--------LQTKLKDIVSLVPRLRHIITVD--GKPPTWSEfpkgviVHTMAAVQAlgvkaNVEKKAHSKPLPS- 279
Cdd:COG0365 116 ITADGGlrggkvidLKEKVDEALEELPSLEHVIVVGrtGADVPMEG------DLDWDELLA-----AASAEFEPEPTDAd 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprLGqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHV 359
Cdd:COG0365 185 DPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV--LD------------------------LKPGDVFWCTADIGWA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAELV-CLSHGC-------RIGYSSPQTLADQSSKikkgskgdtsvLKPTLMAAVPeimdRIYKNVMNKVNEMSAfQ 431
Cdd:COG0365 239 TGHSYIVYgPLLNGAtvvlyegRPDFPDPGRLWELIEK-----------YGVTVFFTAP----TAIRALMKAGDEPLK-K 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 432 RNLfilaynykmeqiskgcSTplcdrfvfrnvrrllggnIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGA-G 510
Cdd:COG0365 303 YDL----------------SS------------------LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 511 T---ITEVWDyntGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTM--GYYKNEAKTKTDFFEDENGqrW 585
Cdd:COG0365 349 SnlpGLPVKP---GSMGKPVPGYDVAVVD-EDG---NPVPPGEEGELVIKGPWPGMfrGYWNDPERYRETYFGRFPG--W 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 586 LCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNiCAyansyhsyVIG------------FVVP 653
Cdd:COG0365 420 YRTGDGARRDEDGYFWILGRSDDVINV-SGHRIGTAEIESALVSHPAVAE-AA--------VVGvpdeirgqvvkaFVVL 489
|
570 580
....*....|....*....|.
gi 2268062224 654 NQ---------KELTELARTK 665
Cdd:COG0365 490 KPgvepsdelaKELQAHVREE 510
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
134-640 |
6.13e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 72.10 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 134 WLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITS 213
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 214 KELLQtKLKDIVSLVPRLRHIITVDGkPPTWSeFPKGVIVHTMAAVQALGVKANVEkkahskplPSDIAVIMYTSGSTGI 293
Cdd:PRK06155 126 AALLA-ALEAADPGDLPLPAVWLLDA-PASVS-VPAGWSTAPLPPLDAPAPAAAVQ--------PGDTAAILYTSGTTGP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 294 PKGVMISHsniiasitgmarriprlgqitghepaaAVELWRNRKVHQPASLREEDVYIGYLPLAHVLELSAELVCLSHGC 373
Cdd:PRK06155 195 SKGVCCPH---------------------------AQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RIgysspqtladqsskikkgskgdtsVLKPTLMAAvpeimdRIYknvmnkvnemSAFQRNLFILAYnYKMEQISKGCSTP 453
Cdd:PRK06155 248 TY------------------------VLEPRFSAS------GFW----------PAVRRHGATVTY-LLGAMVSILLSQP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 454 LCDRFVFRNVRRLLGGnirlllcGGAP--LSATTQRfmnicFCCPVGQGYGLTESTG--AGTITEVWDYNTGRVgAPLVc 529
Cdd:PRK06155 287 ARESDRAHRVRVALGP-------GVPAalHAAFRER-----FGVDLLDGYGSTETNFviAVTHGSQRPGSMGRL-APGF- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 530 cEIKLKNwEEGGYFNTDKPhprGEILIGGQN---VTMGYYKNEAKTKTDFfedenGQRWLCTGDIGEFDPDGCLKIIDRK 606
Cdd:PRK06155 353 -EARVVD-EHDQELPDGEP---GELLLRADEpfaFATGYFGMPEKTVEAW-----RNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510
....*....|....*....|....*....|....
gi 2268062224 607 KDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA 640
Cdd:PRK06155 423 KDAIRRR-GENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
501-674 |
1.05e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 71.08 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 501 YGLTESTGAGT---IT-EVWD-YNTGRVGAPLVCCEIKLKNWEEGGYFNTDKphprGEILIGGQNVTMGYYKNEAKTKTD 575
Cdd:PRK04813 293 YGPTEATVAVTsieITdEMLDqYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQ----GEIVISGPSVSKGYLNNPEKTAEA 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 576 FFEdENGQRWLCTGDIGEFDpDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNICA---YANSYHSYVIGFVV 652
Cdd:PRK04813 369 FFT-FDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVESAVVvpyNKDHKVQYLIAYVV 445
|
170 180
....*....|....*....|...
gi 2268062224 653 PNQKELT-ELARTKGFKgtwEEL 674
Cdd:PRK04813 446 PKEEDFErEFELTKAIK---KEL 465
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
275-610 |
1.15e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 70.98 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 275 KPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprlgqitghepaaavelwrnrkvhqpaSLREEDVYIGYL 354
Cdd:cd05908 102 CELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST---------------------------EWKTKDRILSWM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 355 PLAHVLELSA-ELVCLSHGCRigysspQTLADQSSKIKKgskgdtsvlkPTLMaavpeimdrIYKNVMNKVNEMSA--FQ 431
Cdd:cd05908 155 PLTHDMGLIAfHLAPLIAGMN------QYLMPTRLFIRR----------PILW---------LKKASEHKATIVSSpnFG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 432 RNLFI------LAYNYKMEQI------SKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLS-ATTQRFMNICFCCPVG 498
Cdd:cd05908 210 YKYFLktlkpeKANDWDLSSIrmilngAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASvGASLPKAQSPFKTITL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 499 QGYGLTESTGAGTI--TEVWDYNTGRVGAPLVCCEIKLKNWE----EGGYFntdkphprGEILIGGQNVTMGYYKNEAKT 572
Cdd:cd05908 290 GRRHVTHGEPEPEVdkKDSECLTFVEVGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEAT 361
|
330 340 350
....*....|....*....|....*....|....*...
gi 2268062224 573 KTDFFEDEngqrWLCTGDIGeFDPDGCLKIIDRKKDLV 610
Cdd:cd05908 362 AKVFTDDG----WLKTGDLG-FIRNGRLVITGREKDII 394
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
280-627 |
1.36e-12 |
|
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: 70.57 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprLGqitghepaaavelwrnrkvhqpasLREEDV-------YIG 352
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA--LG------------------------LTPGDRvfssakmFFG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 353 YlplahvlelsaelvCLSHGCRIGYSSpqtladqsskikkgskGDTSVLKPTlmAAVPEimdriykNVMNKvneMSAFQR 432
Cdd:cd05919 146 Y--------------GLGNSLWFPLAV----------------GASAVLNPG--WPTAE-------RVLAT---LARFRP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 433 NLFIlaynykmeqiskgcSTPLcdrfVFRNVRRLLGG------NIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES 506
Cdd:cd05919 184 TVLY--------------GVPT----FYANLLDSCAGspdalrSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 507 TGAGTITEVWDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWL 586
Cdd:cd05919 246 GHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG---HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-----WY 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2268062224 587 CTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAAL 627
Cdd:cd05919 317 RTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLI 356
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
248-744 |
1.59e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 70.68 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 248 PKGVIVHTMAAVQALGVKANVEKkAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGqitgHEPa 327
Cdd:PRK08180 179 VPGRAATPFAALLATPPTAAVDA-AHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLA----EEP- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 328 aavelwrnrkvhqPaslreedVYIGYLPLAHVLELSAEL-VCLSHGcriGysspqTLAdqsskIKKGskgdtsvlKPT-- 404
Cdd:PRK08180 253 -------------P-------VLVDWLPWNHTFGGNHNLgIVLYNG---G-----TLY-----IDDG--------KPTpg 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 405 LMAA----VPEIMDRIYKNVmNKVNEMsafqrnlfILAYnykMEQiskgcSTPLCDRFvFRNVRrllggnirLLLCGGAP 480
Cdd:PRK08180 292 GFDEtlrnLREISPTVYFNV-PKGWEM--------LVPA---LER-----DAALRRRF-FSRLK--------LLFYAGAA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 481 LSATT----QRF-MNIC-----FCCpvgqGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKnwEEGGYFntdkphp 550
Cdd:PRK08180 346 LSQDVwdrlDRVaEATCgerirMMT----GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLV--PVGGKL------- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 551 rgEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEF-DPDgclkiiDRKKDLV---------KLQAGEYVSL 620
Cdd:PRK08180 413 --EVRVKGPNVTPGYWRAPELTAEAF--DEEG--YYRSGDAVRFvDPA------DPERGLMfdgriaedfKLSSGTWVSV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 621 GKVEAALKNL--PLIDNICAyANSYHSYVIGFVVPNQKELTELARTKGFkGTWEELCNSSEMEN---EVLKVLSEAAISA 695
Cdd:PRK08180 481 GPLRARAVSAgaPLVQDVVI-TGHDRDEIGLLVFPNLDACRRLAGLLAD-ASLAEVLAHPAVRAafrERLARLNAQATGS 558
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2268062224 696 SLEkfeiPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMYG 744
Cdd:PRK08180 559 STR----VARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVEALYA 603
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
278-653 |
1.69e-12 |
|
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: 70.04 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASItgmarriprlgQITGHEPAAavelwrnrkvhqpaslrEEdvyigylpLA 357
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFL-----------QWAAAAFSA-----------------EE--------LA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVL-------ELSA-ELVC-LSHGCRIgysspqTLADQS-SKIKKGSKGDTSVLK--PTLMAAVPEiMDRIYKNV--MNK 423
Cdd:cd12115 148 GVLastsicfDLSVfELFGpLATGGKV------VLADNVlALPDLPAAAEVTLINtvPSAAAELLR-HDALPASVrvVNL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 424 VNEmsAFQRNLfiLAYNYKMEQIskgcstplcdrfvfRNVRRLLGgnirlllcggaPLSATTQRFMnicfcCPVGQGYGL 503
Cdd:cd12115 221 AGE--PLPRDL--VQRLYARLQV--------------ERVVNLYG-----------PSEDTTYSTV-----APVPPGASG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 504 TESTG---AGTITEVWDyntgRVGAPLvcceiklknweeggyfntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED- 579
Cdd:cd12115 267 EVSIGrplANTQAYVLD----RALQPV-------------------PLGVPGELYIGGAGVARGYLGRPGLTAERFLPDp 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2268062224 580 -ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 653
Cdd:cd12115 324 fGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVR-GFRIELGEIEAALRSIPGVREAVVVAigdAAGERRLVAYIVA 400
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
279-706 |
1.79e-12 |
|
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: 70.06 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 279 SDIAVIMYTSGSTGIPKGVMISHSNIIASITGMArriprlgqitghepaaaveLWRNrkvhqpasLREEDVYIgylplah 358
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAA-------------------YWLG--------LRPDDIHW------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 359 vlelsaelvclshgcrigysspqTLADqsSKIKKGSKGdtSVLKPTLMAAVpeimdriykNVMNKVNEMSAfqRNLFILA 438
Cdd:cd05972 127 -----------------------NIAD--PGWAKGAWS--SFFGPWLLGAT---------VFVYEGPRFDA--ERILELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 439 YNYKmeqISKGCSTPLcdrfVFRNVRRLLG-----GNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTIT 513
Cdd:cd05972 169 ERYG---VTSFCGPPT----AYRMLIKQDLssykfSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 514 EVWDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTM--GYYKNEAKTKTDFFEDengqrWLCTGDI 591
Cdd:cd05972 242 PDMPVKPGSMGRPTPGYDVAIID-DDG---RELPPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD-----YYLTGDR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 592 GEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIdNICAYANS----YHSYVIGFVVpnqkeltelaRTKGF 667
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAV-AEAAVVGSpdpvRGEVVKAFVV----------LTSGY 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2268062224 668 KGTwEELCNssEMENEVLKVLSEAAISASLEkF--EIPLKI 706
Cdd:cd05972 381 EPS-EELAE--ELQGHVKKVLAPYKYPREIE-FveELPKTI 417
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
277-665 |
1.99e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 70.30 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 277 LPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMarriprlgqITGHEpaaavelwrnrkvhqpasLREEDVYIGYLPL 356
Cdd:PRK05852 174 LRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAI---------ITGYR------------------LSPRDATVAVMPL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 357 AHVLELSAELVC-LSHGCRI-----GYSSPQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDriyknvmnkvnemsaf 430
Cdd:PRK05852 227 YHGHGLIAALLAtLASGGAVllparGRFSAHTFWD-----------DIKAVGATWYTAVPTIHQ---------------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 431 qrnlfILAYNYKMEQISKGcstplcdRFVFRNVRRllggnirlllCGgAPLSATTQRFMNICFCCPVGQGYGLTESTGAG 510
Cdd:PRK05852 280 -----ILLERAATEPSGRK-------PAALRFIRS----------CS-APLTAETAQALQTEFAAPVVCAFGMTEATHQV 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 511 TITEV-WDYNT----------GRVGAPlvccEIKLKNwEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED 579
Cdd:PRK05852 337 TTTQIeGIGQTenpvvstglvGRSTGA----QIRIVG-SDGLPL---PAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 580 engqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSY---VIGFVVPNQ- 655
Cdd:PRK05852 409 -----WLRTGDLGSLSAAGDLSIRGRIKELIN-RGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPREs 482
|
410
....*....|....*
gi 2268062224 656 -----KELTELARTK 665
Cdd:PRK05852 483 apptaEELVQFCRER 497
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
280-631 |
2.10e-12 |
|
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: 69.07 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIasitgmarriprlgqitghEPAAAvelWRNRkvhqpASLREEDVYIGYLPLAHV 359
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL-------------------RAAAA---WADC-----ADLTEDDRYLIINPFFHT 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAE-LVCLSHGCRIgysSPQTLADQSSKIKKGSKGDTSVL--KPTLmaavpeimdriyknvmnkvnemsaFQRNLfi 436
Cdd:cd17638 54 FGYKAGiVACLLTGATV---VPVAVFDVDAILEAIERERITVLpgPPTL------------------------FQSLL-- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 laynykmeqiskgcSTPLCDRFVFrnvrrllgGNIRLLLCGGAPLSATTQR-------FMNicfccpVGQGYGLTEStGA 509
Cdd:cd17638 105 --------------DHPGRKKFDL--------SSLRAAVTGAATVPVELVRrmrselgFET------VLTAYGLTEA-GV 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 510 GTITEVWDYNT---GRVGAPLVCCEIKLKNweeggyfntdkphpRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWL 586
Cdd:cd17638 156 ATMCRPGDDAEtvaTTCGRACPGFEVRIAD--------------DGEVLVRGYNVMQGYLDDPEATAEAI--DADG--WL 217
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2268062224 587 CTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 631
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHP 261
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
220-625 |
3.55e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 69.69 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 220 KLKDIVSLV-PRL----------RHIITVDGKPPTW---SEFPKGVIVHTMAAVQALGVKANVEKkAHSKPLPSDIAVIM 285
Cdd:PRK12582 148 KLKHLFDLVkPRVvfaqsgapfaRALAALDLLDVTVvhvTGPGEGIASIAFADLAATPPTAAVAA-AIAAITPDTVAKYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 286 YTSGSTGIPKGVMISHSNIIASITGMARRIPRLgqiTGHEPAAAVElWrnrkvhqpaslreedvyigyLPLAHVLELSAE 365
Cdd:PRK12582 227 FTSGSTGMPKAVINTQRMMCANIAMQEQLRPRE---PDPPPPVSLD-W--------------------MPWNHTMGGNAN 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 366 LvclsHGCRIGYSspqTLADQSSKIKKGSKGDTsvlkptlMAAVPEIMDRIYKNVMnkvnemsafqrnlfiLAYNYKMEQ 445
Cdd:PRK12582 283 F----NGLLWGGG---TLYIDDGKPLPGMFEET-------IRNLREISPTVYGNVP---------------AGYAMLAEA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 446 ISKgcSTPLCDRFvFRNvrrllggnIRLLLCGGAPLS-------------ATTQRFmnicfccPVGQGYGLTEStgAGTI 512
Cdd:PRK12582 334 MEK--DDALRRSF-FKN--------LRLMAYGGATLSddlyermqalavrTTGHRI-------PFYTGYGATET--APTT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TEV-WDYN-TGRVGAPLVCCEIKLKnweeggyfntdkphPRG---EILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLC 587
Cdd:PRK12582 394 TGThWDTErVGLIGLPLPGVELKLA--------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAF--DEEG--FYR 455
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2268062224 588 TGDIGEF-DPDGCLK--IID-RKKDLVKLQAGEYVSLGKVEA 625
Cdd:PRK12582 456 LGDAARFvDPDDPEKglIFDgRVAEDFKLSTGTWVSVGTLRP 497
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
135-631 |
4.78e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 69.14 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFM---------YNF---QLVTLYATLGGPAIVHgl 202
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKaravpvnvnYRYvedELRYLLDDSDAVALVY-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 203 nETEvtniitskelLQTKLKDIVSLVPRLRHIITVDGkpPTWSEFPKGVIVHTMAAVQALGVKANVEkkahskPLPSDIa 282
Cdd:PRK07798 107 -ERE----------FAPRVAEVLPRLPKLRTLVVVED--GSGNDLLPGAVDYEDALAAGSPERDFGE------RSPDDL- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 283 VIMYTSGSTGIPKGVMISHSNIIASITGMARRiprlgqITGHEPAAAVELWRnRKVHQPASLReedvyigyLPLAHvlel 362
Cdd:PRK07798 167 YLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDF------ATGEPIEDEEELAK-RAAAGPGMRR--------FPAPP---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 363 saelvcLSHGcrigysspqtlADQSSKIKKGSKGDTSVLKPTLM---AAVPEIMDRiyknvmNKVNEMS----AFQRnlf 435
Cdd:PRK07798 228 ------LMHG-----------AGQWAAFAALFSGQTVVLLPDVRfdaDEVWRTIER------EKVNVITivgdAMAR--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 436 ilaynykmeqiskgcstPLCDRFVFRnvRRLLGGNIRLLLCGGAPLSATT-QRFM----NICfccpVGQGYGLTEsTGAG 510
Cdd:PRK07798 282 -----------------PLLDALEAR--GPYDLSSLFAIASGGALFSPSVkEALLellpNVV----LTDSIGSSE-TGFG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 511 TITEVWDYNTGRvGAPLV-----CCEIklknwEEGGYFNTDKPHPRGEILIGGqNVTMGYYKNEAKTKTDFFEdENGQRW 585
Cdd:PRK07798 338 GSGTVAKGAVHT-GGPRFtigprTVVL-----DEDGNPVEPGSGEIGWIARRG-HIPLGYYKDPEKTAETFPT-IDGVRY 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2268062224 586 LCTGDIGEFDPDGCLKIIDRkKDLVKLQAGEYVSLGKVEAALKNLP 631
Cdd:PRK07798 410 AIPGDRARVEADGTITLLGR-GSVCINTGGEKVFPEEVEEALKAHP 454
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-631 |
6.42e-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: 67.89 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiprlgqitghepaaavelwrnrkvhqpASLREEDVYIGYLPLA 357
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALN---------------------------SLFDPDDVLLCGLPLF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVC-LSHGCRIGYSSPQtladqsskikkGSKGDTSV---------LKPTLMAAVPEIMdriyknvmnkvnem 427
Cdd:cd05944 54 HVNGSVVTLLTpLASGAHVVLAGPA-----------GYRNPGLFdnfwklverYRITSLSTVPTVY-------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 428 safqrnlfilaynykmeqiskgcsTPLCDRFVFRNVrrllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEST 507
Cdd:cd05944 109 ------------------------AALLQVPVNADI-----SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 508 GAGTIT-EVWDYNTGRVGAPLVCCEIKLKNWE-EGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKtKTDFFEDengqRW 585
Cdd:cd05944 160 CLVAVNpPDGPKRPGSVGLRLPYARVRIKVLDgVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGN-KNAFVAD----GW 234
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2268062224 586 LCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 631
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
278-664 |
7.18e-12 |
|
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: 68.51 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGQITghepaaavelwrnrkVHQPASLREEdvyigylplA 357
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLR---------------VALFASISFD---------A 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVClSHGCRIgysspqtladqsskIKKGSKGDtsvlkptlmaaVPEIMDRIYKnvmNKVNEMSAFQRNLFIL 437
Cdd:cd17655 192 SVTEIFASLLS-GNTLYI--------------VRKETVLD-----------GQALTQYIRQ---NRITIIDLTPAHLKLL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 438 AYNykmeQISKGCStplcdrfvfrnvrrllggnIRLLLCGGAPLSATTQRFMNICFC--CPVGQGYGLTESTGAGTI--T 513
Cdd:cd17655 243 DAA----DDSEGLS-------------------LKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTETTVDASIyqY 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 514 EVWDYNTGRV--GAPLVCCEIKLKNwEEGgyfntdKPHP---RGEILIGGQNVTMGYYKNEAKTKTDFFEDE--NGQRWL 586
Cdd:cd17655 300 EPETDQQVSVpiGKPLGNTRIYILD-QYG------RPQPvgvAGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMY 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 587 CTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYANSYHS---YVIGFVVPNqKELT---- 659
Cdd:cd17655 373 RTGDLARWLPDGNIEFLGRIDHQVKIR-GYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnYLCAYIVSE-KELPvaql 450
|
....*..
gi 2268062224 660 --ELART 664
Cdd:cd17655 451 reFLARE 457
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
202-660 |
8.98e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 68.17 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 202 LNETEVTNIITSKELLqtklkdivslvPRLRHIITVDGKPPtwsefpKGVIVHTMAAVQALGVKANVEKKA-------HS 274
Cdd:PRK08008 105 LQNSQASLLVTSAQFY-----------PMYRQIQQEDATPL------RHICLTRVALPADDGVSSFTQLKAqqpatlcYA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 275 KPLPS-DIAVIMYTSGSTGIPKGVMISHSNIiasitgmarriprlgQITGHEPAaavelWRNrkvhqpaSLREEDVYIGY 353
Cdd:PRK08008 168 PPLSTdDTAEILFTSGTTSRPKGVVITHYNL---------------RFAGYYSA-----WQC-------ALRDDDVYLTV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 354 LPLAHV-LELSAELVCLSHGCRI----GYSSpQTLADQSSKIKkgskgdtsvlkptlmAAVPEIMDRIYKNVMnkVNEMS 428
Cdd:PRK08008 221 MPAFHIdCQCTAAMAAFSAGATFvlleKYSA-RAFWGQVCKYR---------------ATITECIPMMIRTLM--VQPPS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 429 AFQRN------LFILAynykmeqISKGCSTPLCDRFvfrnvrrllggNIRLLlcggaplsattqrfmnicfccpvgQGYG 502
Cdd:PRK08008 283 ANDRQhclrevMFYLN-------LSDQEKDAFEERF-----------GVRLL------------------------TSYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 503 LTESTGaGTITevwDYNTGR-----VGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGG---QNVTMGYYKNEAKTKT 574
Cdd:PRK08008 321 MTETIV-GIIG---DRPGDKrrwpsIGRPGFCYEAEIRD-DHN---RPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 575 DFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIG----- 649
Cdd:PRK08008 393 VLEADG----WLHTGDTGYVDEEGFFYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIV---------VVGikdsi 458
|
490
....*....|....*....
gi 2268062224 650 -------FVVPNQKE-LTE 660
Cdd:PRK08008 459 rdeaikaFVVLNEGEtLSE 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
278-653 |
9.69e-12 |
|
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: 67.96 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITgmarriprlgqitghepaaavelWrnrkvHQPAslreedvyigylpla 357
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCE-----------------------W-----HRPY--------------- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 hvLELSAElvclshgcrigysspqtlaDQSSKIKkGSKGDTSVLK--PTLMA-AVPEIMDRIYKNVMNKVNEMsaFQRNL 434
Cdd:cd17645 140 --FGVTPA-------------------DKSLVYA-SFSFDASAWEifPHLTAgAALHVVPSERRLDLDALNDY--FNQEG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 435 FILAYnykmeqiskgCSTPLCDRFVfrnvrRLLGGNIRLLLCGGAPLSATTQRFMNICfccpvgQGYGLTESTGAGTITE 514
Cdd:cd17645 196 ITISF----------LPTGAAEQFM-----QLDNQSLRVLLTGGDKLKKIERKGYKLV------NNYGPTENTVVATSFE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 515 V-WDYNTGRVGAPLVCCEIKLKNweEGgyfNTDKPH-PRGEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGD 590
Cdd:cd17645 255 IdKPYANIPIGKPIDNTRVYILD--EA---LQLQPIgVAGELCIAGEGLARGYLNRPELTAEKFIVHpfVPGERMYRTGD 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2268062224 591 IGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 653
Cdd:cd17645 330 LAKFLPDGNIEFLGRLDQQVKIR-GYRIEPGEIEPFLMNHPLIELAAVLAkedADGRKYLVAYVTA 394
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
219-744 |
4.36e-11 |
|
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: 65.92 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 219 TKLKDIVSLV-PRL----------RHIITV--DGKPPTWS-EFPKGVIVHTMAAVQALGVKANVEKkAHSKPLPSDIAVI 284
Cdd:cd05921 92 AKLKHLFELLkPGLvfaqdaapfaRALAAIfpLGTPLVVSrNAVAGRGAISFAELAATPPTAAVDA-AFAAVGPDTVAKF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 285 MYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGQitghepaaavelwrnrkvhqpaslrEEDVYIGYLPLAHVLELSA 364
Cdd:cd05921 171 LFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGE-------------------------EPPVLVDWLPWNHTFGGNH 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 365 --ELVCLSHGcrigysspqTLADQSSKIKKGSKGDTsvlkptlMAAVPEIMDRIYKNVMNKVNEMSAFQRNlfilaynyk 442
Cdd:cd05921 226 nfNLVLYNGG---------TLYIDDGKPMPGGFEET-------LRNLREISPTVYFNVPAGWEMLVAALEK--------- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 443 meqiskgcSTPLCDRFvFRNVRrllggnirLLLCGGAPLS------------ATTQRFMnicfccPVGQGYGLTESTGAG 510
Cdd:cd05921 281 --------DEALRRRF-FKRLK--------LMFYAGAGLSqdvwdrlqalavATVGERI------PMMAGLGATETAPTA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 511 TITeVWDYN-TGRVGAPLVCCEIKLKnwEEGGYFntdkphprgEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTG 589
Cdd:cd05921 338 TFT-HWPTErSGLIGLPAPGTELKLV--PSGGKY---------EVRVKGPNVTPGYWRQPELTAQAF--DEEG--FYCLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 590 DIGEF-DPDgclkiiDRKKDLV---------KLQAGEYVSLGKVEAALKNL--PLIDN--ICAYANSYhsyvIGF-VVPN 654
Cdd:cd05921 402 DAAKLaDPD------DPAKGLVfdgrvaedfKLASGTWVSVGPLRARAVAAcaPLVHDavVAGEDRAE----VGAlVFPD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 655 QKELTELARTKGFKgtweelcnssemENEVLKVLS-EAAISASLEKFE--------IPLKIRLSPDPWTPETGLVTDAFK 725
Cdd:cd05921 472 LLACRRLVGLQEAS------------DAEVLRHAKvRAAFRDRLAALNgeatgsssRIARALLLDEPPSIDKGEITDKGY 539
|
570
....*....|....*....
gi 2268062224 726 LKRKELKTHYQADIERMYG 744
Cdd:cd05921 540 INQRAVLERRAALVERLYA 558
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
279-652 |
5.73e-11 |
|
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: 64.59 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 279 SDIAVIMYTSGSTGIPKGVMISHSNIIAsitgmarrIPRLGQITGHEpaaavelWRNrkvhqpaslreEDVYIGYLPLAH 358
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFA--------VPDILQKEGLN-------WVV-----------GDVTYLPLPATH 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 359 VLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSVLKPTLMAAVPEImdriYKNVMNKVNEMsafqrnlfila 438
Cdd:cd17635 55 IGGLWWILTCLIHGGLCVTGGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSE----LKSANATVPSL----------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 439 ynykmeqiskgcstplcdrfvfrnvrrllggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDY 518
Cdd:cd17635 120 ---------------------------------RLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 519 -NTGRVGAPLVCCEIKLKNWEEGGYFNTDKphprGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPD 597
Cdd:cd17635 167 iEINAVGRPYPGVDVYLAATDGIAGPSASF----GTIWIKSPANMLGYWNNPERTAEVLIDG-----WVNTGDLGERRED 237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2268062224 598 GCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVV 652
Cdd:cd17635 238 GFLFITGRSSESI-NCGGVKIAPDEVERIAEGVSGVQECACYEisdEEFGELVGLAVV 294
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
278-660 |
9.74e-11 |
|
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: 64.73 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprLGQITGHEpaaAVELWRNrkvhqpaslreedvyigylpla 357
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERY--FGRDNGDE---AVLFFSN---------------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELSAELVCLShgcrigYSSPQTLadqsskikkgskgdtsVLKPTLMAAVPeimDRIYKnVMNKvnemsafqrnlfil 437
Cdd:cd17648 146 YVFDFFVEQMTLA------LLNGQKL----------------VVPPDEMRFDP---DRFYA-YINR-------------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 438 aynykmEQISKGCSTP-LCDRFVFRNVRRLlggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEvw 516
Cdd:cd17648 186 ------EKVTYLSGTPsVLQQYDLARLPHL-----KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRF-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 517 dYNTGR-----VGAPL--VCCEIklknweeggyFNTD-KPHP---RGEILIGGQNVTMGYYKNEAKTKTDF----FEDE- 580
Cdd:cd17648 253 -FPGDQrfdksLGRPVrnTKCYV----------LNDAmKRVPvgaVGELYLGGDGVARGYLNRPELTAERFlpnpFQTEq 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 581 -----NGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI---------DNICAYANSyHSY 646
Cdd:cd17648 322 erargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIR-GQRIEPGEVEAALASYPGVrecavvakeDASQAQSRI-QKY 399
|
410
....*....|....
gi 2268062224 647 VIGFVVPNQKELTE 660
Cdd:cd17648 400 LVGYYLPEPGHVPE 413
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
257-743 |
1.56e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.98 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 257 AAVQALGVKANVEKKAHSKP----LPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARriprlgqitghepaaAVEL 332
Cdd:PRK12316 3170 QGVQVLDLDRGDENYAEANPairtMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ---------------AYGL 3234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 333 WRNRKVHQPASLREEdvyigylplAHVLELsaeLVCLSHGCRIGYSSPQTLADQsskikkgskgdtsvlkptlmAAVPEI 412
Cdd:PRK12316 3235 GVGDRVLQFTTFSFD---------VFVEEL---FWPLMSGARVVLAGPEDWRDP--------------------ALLVEL 3282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 413 MDRIYKNVMNKVNEMsafqrnlfilaynykmeqiskgcstpLCDRFVFRNVRRLlgGNIRLLLCGGAPLSATTQRFMNIC 492
Cdd:PRK12316 3283 INSEGVDVLHAYPSM--------------------------LQAFLEEEDAHRC--TSLKRIVCGGEALPADLQQQVFAG 3334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 493 FccPVGQGYGLTESTGAGTITEVWDYNTGR--VGAPLVCCEIKLKNweegGYFNTDKPHPRGEILIGGQNVTMGYYKNEA 570
Cdd:PRK12316 3335 L--PLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD----GSLEPVPVGALGELYLGGEGLARGYHNRPG 3408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 571 KTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYANSYHSyVI 648
Cdd:PRK12316 3409 LTAERFVPDpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LV 3486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 649 GFVVPNQKEltelartkgfkGTWEelcnssemenEVLKvlseAAISASLEKFEIPLK-IRLSPDPWTPETglvtdafKLK 727
Cdd:PRK12316 3487 AYVVPEDEA-----------GDLR----------EALK----AHLKASLPEYMVPAHlLFLERMPLTPNG-------KLD 3534
|
490
....*....|....*.
gi 2268062224 728 RKELKTHYQADIERMY 743
Cdd:PRK12316 3535 RKALPRPDAALLQQDY 3550
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
135-631 |
4.13e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.02 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLqTKLKDIVSLVPRLRHIIT-VDGKPPTWSEFPkgvivhTMAAVqalgVKANVEKKAHSKPLPSDIaVIMyTSGSTGI 293
Cdd:PRK07788 155 EFT-DLLSALPPDLGRLRAWGGnPDDDEPSGSTDE------TLDDL----IAGSSTAPLPKPPKPGGI-VIL-TSGTTGT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 294 PKGVMISHSNIIASITGMARRIPrlgqitghepaaavelWRNRKVHQPASlreedvyigylPLAHVLELSAELVCLSHGC 373
Cdd:PRK07788 222 PKGAPRPEPSPLAPLAGLLSRVP----------------FRAGETTLLPA-----------PMFHATGWAHLTLAMALGS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 374 RI----GYSSPQTLADqsskIKKgskgdtsvLKPTLMAAVPeimdriyknVMnkvnemsaFQRNLFILAynykmEQISK- 448
Cdd:PRK07788 275 TVvlrrRFDPEATLED----IAK--------HKATALVVVP---------VM--------LSRILDLGP-----EVLAKy 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 449 GCStplcdrfvfrnvrrllggNIRLLLCGGAPLSATT-QRFMN-----ICfccpvgQGYGLTESTGAgTIT--EVWDYNT 520
Cdd:PRK07788 321 DTS------------------SLKIIFVSGSALSPELaTRALEafgpvLY------NLYGSTEVAFA-TIAtpEDLAEAP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 521 GRVGAPLVCCEIKLknweeggYFNTDKPHPRGE---ILIGGqNVTMGYYKNeAKTKtdffEDENGqrWLCTGDIGEFDPD 597
Cdd:PRK07788 376 GTVGRPPKGVTVKI-------LDENGNEVPRGVvgrIFVGN-GFPFEGYTD-GRDK----QIIDG--LLSSGDVGYFDED 440
|
490 500 510
....*....|....*....|....*....|....
gi 2268062224 598 GCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 631
Cdd:PRK07788 441 GLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHP 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
278-731 |
4.31e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.82 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprlgQITGHEPAAAVelwrnrkvhQPASLrEEDVYIGYLPLA 357
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY----GLGVGDTVLQK---------TPFSF-DVSVWEFFWPLM 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HvlelsaelvclshGCRIGYSSPQTLADqsskikkgskgdtsvlkptlMAAVPEIMDRIYKNVMNKVNEM-SAFQRNLFI 436
Cdd:PRK12316 720 S-------------GARLVVAAPGDHRD--------------------PAKLVELINREGVDTLHFVPSMlQAFLQDEDV 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 laynykmeqiskgcstPLCDrfvfrnvrrllggNIRLLLCGGAPLSATTQ-RFMNICFCCPVGQGYGLTESTGAGT---- 511
Cdd:PRK12316 767 ----------------ASCT-------------SLRRIVCSGEALPADAQeQVFAKLPQAGLYNLYGPTEAAIDVThwtc 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 512 ITEVWDynTGRVGAPL--VCCEIKLKNWEeggyfntdkPHP---RGEILIGGQNVTMGYYKNEAKTKTDFFEDE--NGQR 584
Cdd:PRK12316 818 VEEGGD--SVPIGRPIanLACYILDANLE---------PVPvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPfvAGER 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 585 WLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYANSYHSYViGFVVPnqkeltelart 664
Cdd:PRK12316 887 MYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLAVDGKQLV-GYVVL----------- 953
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2268062224 665 kgfkgtweelcnssEMENEVLKVLSEAAISASLEKFEIPLKI-RLSPDPWTPETglvtdafKLKRKEL 731
Cdd:PRK12316 954 --------------ESEGGDWREALKAHLAASLPEYMVPAQWlALERLPLTPNG-------KLDRKAL 1000
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
192-624 |
4.53e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 63.19 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 192 TLGGPAIVHGLNETEVTNIITSKELLQT-KLKDIVSLVPRLRHIITVDGKPPTWSEFPKGVIVHTMAAVQALgvkanVEK 270
Cdd:PRK08043 288 TAGVKGLTSAITAAEIKTIFTSRQFLDKgKLWHLPEQLTQVRWVYLEDLKDDVTTADKLWIFAHLLMPRLAQ-----VKQ 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 271 KahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITgmarriprlgQItghepaaavelwrnRKVhqpASLREEDVY 350
Cdd:PRK08043 363 Q------PEDAALILFTSGSEGHPKGVVHSHKSLLANVE----------QI--------------KTI---ADFTPNDRF 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 351 IGYLPLAHVLELSAELVC-LSHGCRIG-YSSPQTladqsskikkgskgdtsvlkptlMAAVPEIMdriyknvmnkvnems 428
Cdd:PRK08043 410 MSALPLFHSFGLTVGLFTpLLTGAEVFlYPSPLH-----------------------YRIVPELV--------------- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 429 aFQRNLFILAynykmeqiskGCSTPL--CDRFVF-RNVRRLlggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTE 505
Cdd:PRK08043 452 -YDRNCTVLF----------GTSTFLgnYARFANpYDFARL-----RYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 506 STGAGTITEVWDYNTGRVGAPLVCCE---IKLKNWEEGGyfntdkphprgEILIGGQNVTMGYYKNEA--KTKTDFFEDE 580
Cdd:PRK08043 516 CAPVVSINVPMAAKPGTVGRILPGMDarlLSVPGIEQGG-----------RLQLKGPNIMNGYLRVEKpgVLEVPTAENA 584
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2268062224 581 NGQR---WLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVE 624
Cdd:PRK08043 585 RGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKI-AGEMVSLEMVE 630
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
278-631 |
8.05e-10 |
|
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: 61.62 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlgqitghepaaavelwrnrkvhqpasLREEDVYIGYLPL- 356
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG---------------------------LTPGDRELQFASFn 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 357 --AHVLELSAELVClshGCRIGYSSPQTLADQsskikkgskgdtsvlkptlmAAVPEIMDRIYKNVMNkvnemsafqrnl 434
Cdd:cd17649 146 fdGAHEQLLPPLIC---GACVVLRPDELWASA--------------------DELAEMVRELGVTVLD------------ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 435 FILAYNYKMEQiskgcstplcdrfVFRNVRRLLGGNIRLLLCGGAPLSATTQR--FMNICFCCpvgQGYGLTEstgaGTI 512
Cdd:cd17649 191 LPPAYLQQLAE-------------EADRTGDGRPPSLRLYIFGGEALSPELLRrwLKAPVRLF---NAYGPTE----ATV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TE-VWDYNTGR--------VGAPLvcceiklknweeGGY----FNTD-KPHPR---GEILIGGQNVTMGYYKNEAKTKTD 575
Cdd:cd17649 251 TPlVWKCEAGAaragasmpIGRPL------------GGRsayiLDADlNPVPVgvtGELYIGGEGLARGYLGRPELTAER 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2268062224 576 FFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 631
Cdd:cd17649 319 FVPDpfgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIR-GFRIELGEIEAALLEHP 376
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
278-653 |
1.58e-09 |
|
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: 60.91 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARriprlgqitghepaaAVELWRNRKVHQPASLreedvyigylpla 357
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIK---------------EYGITSSDRVLQFASI------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 hVLELSAELVClshgcrigysspQTLAdqsskikkgsKGDTSVLKPTLMAAVPEIM-DRIYKNvmnkvnemsafQRNLFI 436
Cdd:cd17644 157 -AFDVAAEEIY------------VTLL----------SGATLVLRPEEMRSSLEDFvQYIQQW-----------QLTVLS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 LAYNYKMEQISKGcSTPLCDrfvfrnvrrlLGGNIRLLLCGG-APLSATTQRFMNIcfccpVGQ------GYGLTESTGA 509
Cdd:cd17644 203 LPPAYWHLLVLEL-LLSTID----------LPSSLRLVIVGGeAVQPELVRQWQKN-----VGNfiqlinVYGPTEATIA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 510 GTITEVWDYNTGRVGAPLVCCEI-KLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDF----FEDENGQR 584
Cdd:cd17644 267 ATVCRLTQLTERNITSVPIGRPIaNTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFishpFNSSESER 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2268062224 585 WLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 653
Cdd:cd17644 347 LYKTGDLARYLPDGNIEYLGRIDNQVKIR-GFRIELGEIEAVLSQHNDVKTAVVIVredQPGNKRLVAYIVP 417
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
278-631 |
1.64e-09 |
|
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: 60.82 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRlgqitghEPAAAVELWRNrkVHQPASLREedvyIgYLPLA 357
Cdd:cd17651 135 ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSL-------GPGARTLQFAG--LGFDVSVQE----I-FSTLC 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HvlelSAELVCLSHGCRigySSPQTLADQSSKikkgsKGDTSVLKPTLMA-AVPEIMDRIyknvmnkvnemsafqrnlfi 436
Cdd:cd17651 201 A----GATLVLPPEEVR---TDPPALAAWLDE-----QRISRVFLPTVALrALAEHGRPL-------------------- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 437 laynykmeqiskgcSTPLCDrfvfrnvrrllggnIRLLLCGGAPLSAT--------TQRFMNICFccpvgqGYGLTEST- 507
Cdd:cd17651 249 --------------GVRLAA--------------LRYLLTGGEQLVLTedlrefcaGLPGLRLHN------HYGPTETHv 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 508 -GAGTITEVWDYNTGR--VGAPLVCCEIK-LKNWeeggyfntDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDE 580
Cdd:cd17651 295 vTALSLPGDPAAWPAPppIGRPIDNTRVYvLDAA--------LRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDP 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2268062224 581 --NGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 631
Cdd:cd17651 367 fvPGARMYRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALARHP 418
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
278-731 |
1.73e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIP-----RLGQITGHEPAAAVELWrnrkvhqpaslreedvyig 352
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYEltpddRVLQFMSFSFDGSHEGL------------------- 4753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 353 YLPLAHvlelSAELVCLSHGcrigYSSPQTLADQSSKikkgskgdtsvLKPTLMAAVPeimdriyknvmnkvnemSAFQr 432
Cdd:PRK12316 4754 YHPLIN----GASVVIRDDS----LWDPERLYAEIHE-----------HRVTVLVFPP-----------------VYLQ- 4796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 433 nlfilaynykmeQISKGCStplcdrfvfrnvRRLLGGNIRLLLCGGAPLSATTQRFMnICFCCPVG--QGYGLTESTGAG 510
Cdd:PRK12316 4797 ------------QLAEHAE------------RDGEPPSLRVYCFGGEAVAQASYDLA-WRALKPVYlfNGYGPTETTVTV 4851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 511 TITEVWDYNT-GRVGAPLvccEIKLKNweEGGYFNTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFFED---EN 581
Cdd:PRK12316 4852 LLWKARDGDAcGAAYMPI---GTPLGN--RSGYVLDGQLNPLpvgvaGELYLGGEGVARGYLERPALTAERFVPDpfgAP 4926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 582 GQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPNQKELT 659
Cdd:PRK12316 4927 GGRLYRTGDLARYRADGVIDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREavVIAQEGAVGKQLVGYVVPQDPALA 5005
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2268062224 660 ElartkgfkgtweelcnSSEMENEVLKVLsEAAISASLEKFEIPLK-IRLSPDPWTPETglvtdafKLKRKEL 731
Cdd:PRK12316 5006 D----------------ADEAQAELRDEL-KAALRERLPEYMVPAHlVFLARMPLTPNG-------KLDRKAL 5054
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
231-633 |
2.19e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 60.68 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 231 LRHIITVDGKpptwsEFPKGVIVHTMAAVQALGVKANVEKKahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITg 310
Cdd:PRK09274 137 VRRLVTVGGR-----LLWGGTTLATLLRDGAAAPFPMADLA------PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIE- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 311 marripRLGQITGHEPAaavelwrnrkvhqpaslrEEDvyigyLPLAHVLELSAelVCLshgcrigysspqtladqsski 390
Cdd:PRK09274 205 ------ALREDYGIEPG------------------EID-----LPTFPLFALFG--PAL--------------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 391 kkgskGDTSVLkPTLMAAVPEIMD--RIYKnvmnkvnemsAFQR----NLFIL-AYnykMEQISKGCSTplcDRFVFRNV 463
Cdd:PRK09274 233 -----GMTSVI-PDMDPTRPATVDpaKLFA----------AIERygvtNLFGSpAL---LERLGRYGEA---NGIKLPSL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 464 RRLLggnirlllCGGAPLSATT-QRF---MNicfccPVGQ---GYGLTESTGAGTI---------TEVWDYNTGR-VGAP 526
Cdd:PRK09274 291 RRVI--------SAGAPVPIAViERFramLP-----PDAEiltPYGATEALPISSIesreilfatRAATDNGAGIcVGRP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 527 LVCCEIKL--------KNWEEggyfntDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDENGQRWLCTGDIGEFD 595
Cdd:PRK09274 358 VDGVEVRIiaisdapiPEWDD------ALRLATgeiGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLD 431
|
410 420 430
....*....|....*....|....*....|....*...
gi 2268062224 596 PDGCLKIIDRKKDLVKLQAGEYVSLgKVEAALKNLPLI 633
Cdd:PRK09274 432 AQGRLWFCGRKAHRVETAGGTLYTI-PCERIFNTHPGV 468
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
278-631 |
2.83e-09 |
|
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: 59.96 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIasitGMARRIPRLGQITGHEpaaavelwrnrKVHQPASLrEEDVYIGYLPLA 357
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLA----NLAAAQIAAFDVGPGS-----------RVLQFASP-SFDASVWELLMA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 hvLELSAELVCLSHGCRIgysSPQTLAD--QSSKIkkgskgDTSVLKPTLMAAVP--EIMDRiyknvmnkvnemsafqRN 433
Cdd:cd17652 156 --LLAGATLVLAPAEELL---PGEPLADllREHRI------THVTLPPAALAALPpdDLPDL----------------RT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 434 LfilaynykmeqISKG--CSTPLCDRFvfrnvrrllggnirlllcggaplsATTQRFMNicfccpvgqGYGLTESTGAGT 511
Cdd:cd17652 209 L-----------VVAGeaCPAELVDRW------------------------APGRRMIN---------AYGPTETTVCAT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 512 ITEVW-DYNTGRVGAPLVCCEIklknweeggYFNTDKPHP-----RGEILIGGQNVTMGYYKNEAKTKTDFFED---ENG 582
Cdd:cd17652 245 MAGPLpGGGVPPIGRPVPGTRV---------YVLDARLRPvppgvPGELYIAGAGLARGYLNRPGLTAERFVADpfgAPG 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2268062224 583 QRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 631
Cdd:cd17652 316 SRMYRTGDLARWRADGQLEFLGRADDQVKIR-GFRIELGEVEAALTEHP 363
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
186-627 |
2.83e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 60.35 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 186 LVTLYATLGGPAIVHGLNETEVTNIITSKELLQTkLKDIVSLVPRLrHIITVDGKPPtwsEFPKGVIVHTMAAVQALgvk 265
Cdd:PRK08162 95 LNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEV-AREALALLPGP-KPLVIDVDDP---EYPGGRFIGALDYEAFL--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 266 anvekkAHSKP-----LPSD----IAvIMYTSGSTGIPKGVMISH--------SNIIAsiTGMARRiprlgqitghepaa 328
Cdd:PRK08162 167 ------ASGDPdfawtLPADewdaIA-LNYTSGTTGNPKGVVYHHrgaylnalSNILA--WGMPKH-------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 329 AVELWRnrkvhqpaslreedvyigyLPLAHvlelsaelvclshgCRiGYSSPQTLAdqsskikkgskgdtsvlkptLMAA 408
Cdd:PRK08162 224 PVYLWT-------------------LPMFH--------------CN-GWCFPWTVA--------------------ARAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 409 VpeimdriykNV-MNKVNEMSAFQrnlFIlaynyKMEQISKGCSTPLCDRFVFR---NVRRLLGGNIRLLLCGGAPLSAT 484
Cdd:PRK08162 250 T---------NVcLRKVDPKLIFD---LI-----REHGVTHYCGAPIVLSALINapaEWRAGIDHPVHAMVAGAAPPAAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 485 TQRFMNICFCcpVGQGYGLTESTGAGTIT---EVWD--------YNTGRVGAPLVCCE-IKLKNWEeggyfnTDKPHPR- 551
Cdd:PRK08162 313 IAKMEEIGFD--LTHVYGLTETYGPATVCawqPEWDalplderaQLKARQGVRYPLQEgVTVLDPD------TMQPVPAd 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 552 ----GEILIGGqNVTM-GYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAA 626
Cdd:PRK08162 385 getiGEIMFRG-NIVMkGYLKNPKATEEAF---AGG--WFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDV 457
|
.
gi 2268062224 627 L 627
Cdd:PRK08162 458 L 458
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
523-656 |
6.71e-09 |
|
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: 59.02 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 523 VGAPLVCCEIKLKNWEEggyfntdKPHPRG---EILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPD 597
Cdd:cd17656 303 IGKPISNTWIYILDQEQ-------QLQPQGivgELYISGASVARGYLNRQELTAEKFFPDpfDPNERMYRTGDLARYLPD 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2268062224 598 GCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSY-HSYVIGFVVPNQK 656
Cdd:cd17656 376 GNIEFLGRADHQVKIR-GYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
249-610 |
7.79e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.85 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 249 KGVIVHTMAAVQALGVKANVEKKahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprlgqitGHEPaa 328
Cdd:PRK07768 128 KGIRVLTVADLLAADPIDPVETG------EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAA-------EFDV-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 329 avelwrnrkvhqpaslrEEDVYIGYLPLAHVLELSAEL-VCLSHGCRIGYSSP-QTLADqsskikkgskgdtsvlkPTLM 406
Cdd:PRK07768 193 -----------------ETDVMVSWLPLFHDMGMVGFLtVPMYFGAELVKVTPmDFLRD-----------------PLLW 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 407 aavPEIMDRiYKNVMnkvnemsafqrnlfILAYNYKMEQISkgcstplcdrfvfrnvRRLLGG---------NIRLLLCG 477
Cdd:PRK07768 239 ---AELISK-YRGTM--------------TAAPNFAYALLA----------------RRLRRQakpgafdlsSLRFALNG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 478 GAPLS-ATTQRFmnicfcCPVGQG-----------YGLTESTGAGTItevwdyntGRVGAPLVCCEIKLKNWEEGGYF-N 544
Cdd:PRK07768 285 AEPIDpADVEDL------LDAGARfglrpeailpaYGMAEATLAVSF--------SPCGAGLVVDEVDADLLAALRRAvP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 545 TDKPHPR-----------------------------GEILIGGQNVTMGYykneakTKTDFFE---DENGqrWLCTGDIG 592
Cdd:PRK07768 351 ATKGNTRrlatlgpplpglevrvvdedgqvlpprgvGVIELRGESVTPGY------LTMDGFIpaqDADG--WLDTGDLG 422
|
410
....*....|....*...
gi 2268062224 593 EFDPDGCLKIIDRKKDLV 610
Cdd:PRK07768 423 YLTEEGEVVVCGRVKDVI 440
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-631 |
9.86e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 57.78 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 284 IMYTSGSTGIPKGVMISHSNIIASITGmarriprlGQITGHEPAAAVELWRNRKVHQPASlreedVYIGYLPLAHVLELS 363
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMG--------GADFGTGEFTPSEDAHKAAAAAAGT-----VMFPAPPLMHGTGSW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 364 AELVCLSHGCRIGYSSPQTLADqsskikkgskgdtsvlkptlmaavpEIMDRIYKNvmnKVNEMS----AFQRNLfilay 439
Cdd:cd05924 75 TAFGGLLGGQTVVLPDDRFDPE-------------------------EVWRTIEKH---KVTSMTivgdAMARPL----- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 440 nykMEQISKGCSTPLcdrfvfrnvrrllgGNIRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESTGAGTItevwdY 518
Cdd:cd05924 122 ---IDALRDAGPYDL--------------SSLFAISSGGALLSPEVkQGLLELVPNITLVDAFGSSETGFTGSG-----H 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 519 NTGRV--GAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGqNVTMGYYKNEAKTKTDFFEdENGQRWLCTGDIGEFDP 596
Cdd:cd05924 180 SAGSGpeTGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETFPE-VDGVRYAVPGDRATVEA 257
|
330 340 350
....*....|....*....|....*....|....*
gi 2268062224 597 DGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLP 631
Cdd:cd05924 258 DGTVTLLGRGSVCIN-TGGEKVFPEEVEEALKSHP 291
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
154-610 |
1.19e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 58.07 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 154 LGQKPKANIAIFCETRAE-WMIAAQACFMyNFQLVTLYAtLGGPA-IVHGLNETEVTNIITSKELLQTKLKDIVSLVPRL 231
Cdd:PRK06188 57 LGLGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHP-LGSLDdHAYVLEDAGISTLIVDPAPFVERALALLARVPSL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 232 RHIITVDgkpptwsEFPKGVIVHTMAAVQAlgvkanvEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSniiaSITGM 311
Cdd:PRK06188 135 KHVLTLG-------PVPDGVDLLAAAAKFG-------PAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHR----SIATM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 312 ArriprlgQITghepAAAVELwrnrkvhqPASLReedvYIGYLPLAHVlelSAELVClshgcrigyssPqTLAdqsskik 391
Cdd:PRK06188 197 A-------QIQ----LAEWEW--------PADPR----FLMCTPLSHA---GGAFFL-----------P-TLL------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 392 kgsKGDTSVLKP-----TLMAAVPEimDRIykNVMNKVNEMsafqrnLFILaynykMEqiskgcstplCDRFVFRNVRRL 466
Cdd:PRK06188 232 ---RGGTVIVLAkfdpaEVLRAIEE--QRI--TATFLVPTM------IYAL-----LD----------HPDLRTRDLSSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 467 lggniRLLLCGGAPLSAT-----TQRFMNIcfccpVGQGYGLTESTGAGTITEVWDYNTGRV------GAPLVCCEIKLK 535
Cdd:PRK06188 284 -----ETVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALL 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2268062224 536 NwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLV 610
Cdd:PRK06188 354 D-EDGREVAQGEV---GEICVRGPLVMDGYWNRPEETAEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKDMI 419
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
469-659 |
1.19e-08 |
|
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: 58.11 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 469 GNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEstGAGTIT------EVWDYNTGRVGAPLVccEIKLknWEEGGy 542
Cdd:cd05920 255 SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTrlddpdEVIIHTQGRPMSPDD--EIRV--VDEEG- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 543 fNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGK 622
Cdd:cd05920 328 -NPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRIKDQIN-RGGEKIAAEE 401
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2268062224 623 VEAALKNLPLIDNiCAYANSYHSY----VIGFVVPNQKELT 659
Cdd:cd05920 402 VENLLLRHPAVHD-AAVVAMPDELlgerSCAFVVLRDPPPS 441
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
278-653 |
1.60e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.43 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiprlgqitghepaaavelwrnrkvhqpASLREEDVYIGYLPLA 357
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER---------------------------YELSPADCELQFMSFS 2197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 hvLELSAE--LVCLSHGCRI-----GYSSPQTLADQSSKikkgsKGDTSVLKPTLMaavpeimdriyknvmnkvnemsaf 430
Cdd:PRK12316 2198 --FDGAHEqwFHPLLNGARVlirddELWDPEQLYDEMER-----HGVTILDFPPVY------------------------ 2246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 431 qrnlfilaynykMEQISKGCStplcdrfvfRNVRRLlggNIRLLLCGGAPLSAT----------TQRFMNicfccpvgqG 500
Cdd:PRK12316 2247 ------------LQQLAEHAE---------RDGRPP---AVRVYCFGGEAVPAAslrlawealrPVYLFN---------G 2293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 501 YGLTESTGAGTI-TEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED 579
Cdd:PRK12316 2294 YGPTEAVVTPLLwKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPD 2373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2268062224 580 ---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVP 653
Cdd:PRK12316 2374 pfsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR-GFRIELGEIEARLQAHPAVREavVVAQDGASGKQLVAYVVP 2451
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
433-660 |
1.83e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.31 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 433 NLFILayNYKMEQISKGCSTPLCDRF---VFRNVRRLLGGNI------RLLLCGGAP----LsATTQRFMNIcfccPVGQ 499
Cdd:PRK07445 187 KLVIL--PYKRLKSGQELPPNPSDFFlslVPTQLQRLLQLRPqwlaqfRTILLGGAPawpsL-LEQARQLQL----RLAP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 500 GYGLTEStgAGTIT-----EVWDYNTGrVGAPLVCCEIKLKNweeggyfntdkpHPRGEILIGGQNVTMGYYKNEaktkt 574
Cdd:PRK07445 260 TYGMTET--ASQIAtlkpdDFLAGNNS-SGQVLPHAQITIPA------------NQTGNITIQAQSLALGYYPQI----- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 575 dffedENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICAY--ANSY-HSYVIGFV 651
Cdd:PRK07445 320 -----LDSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLglPDPHwGEVVTAIY 393
|
....*....
gi 2268062224 652 VPNQKELTE 660
Cdd:PRK07445 394 VPKDPSISL 402
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
280-638 |
4.39e-08 |
|
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: 56.33 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLgqitghepaaavelwrnrkvhqpaslREEDVYIGYLPLAHV 359
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRL--------------------------REDDRFVGSPPLAFT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAELVCLSHGCRIGYSSPQTLADQSSKIkkgskgdTSVLKPTLMAAVPeimdriyknvmnkvNEMSAfqrnlfILAY 439
Cdd:cd05958 152 FGLGGVLLFPFGVGASGVLLEEATPDLLLSA-------IARYKPTVLFTAP--------------TAYRA------MLAH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 440 NYKMEQiskgcstplcdrfvfrnvrrlLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYN 519
Cdd:cd05958 205 PDAAGP---------------------DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 520 TGRVGAPLVCCEIKLKNwEEGgyfntdKPHPRGEIliGGQNVT--MGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPD 597
Cdd:cd05958 264 PGATGKPVPGYEAKVVD-DEG------NPVPDGTI--GRLAVRgpTGCRYLADKRQRTYVQGG----WNITGDTYSRDPD 330
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2268062224 598 GCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNiCA 638
Cdd:cd05958 331 GYFRHQGRSDDMIVS-GGYNIAPPEVEDVLLQHPAVAE-CA 369
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
277-633 |
1.01e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 55.17 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 277 LPSDI-AVIMYTSGSTGIPKGVMISHSNIIA-SITGmarrIPRLGQITGHEpaaavelwrnrkvhqpaslreedvyIGYL 354
Cdd:PRK07786 171 IPNDSpALIMYTSGTTGRPKGAVLTHANLTGqAMTC----LRTNGADINSD-------------------------VGFV 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 355 --PLAHVLELSAELVCLSHGCRI-----GYSSPQTLAD--QSSKIkkgskgdTSV-LKPTLMAAVpeimdriyknvmnkV 424
Cdd:PRK07786 222 gvPLFHIAGIGSMLPGLLLGAPTviyplGAFDPGQLLDvlEAEKV-------TGIfLVPAQWQAV--------------C 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 425 NEMSAFQRNLfilaynykmeqiskgcstplcdrfvfrnvrrllggNIRLLLCGGAPLSATTQRFMNICFccPVGQ---GY 501
Cdd:PRK07786 281 AEQQARPRDL-----------------------------------ALRVLSWGAAPASDTLLRQMAATF--PEAQilaAF 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 502 GLTESTgagTITEVWD-----YNTGRVGAPLVCCEIKLKNWEeggyFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDF 576
Cdd:PRK07786 324 GQTEMS---PVTCMLLgedaiRKLGSVGKVIPTVAARVVDEN----MNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 577 fedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLI 633
Cdd:PRK07786 397 ---AGG--WFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDI 447
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
129-743 |
1.43e-07 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 55.25 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 129 LGHYNWLSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATlgGPAIVHGLNETEVT 208
Cdd:PTZ00297 452 SGESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPLVGK--GSTMRTLIDEHKIK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 209 NIITSKellqtklKDIVSLVP-RLRHIITVdgkpptwsefpkgVIVHTM------AAVQALGVK----ANVEKKAHSKPL 277
Cdd:PTZ00297 530 VVFADR-------NSVAAILTcRSRKLETV-------------VYTHSFydeddhAVARDLNITlipyEFVEQKGRLCPV 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 P-----SDIAVIMY-----TSGSTGIPKGVMISHSNIIASItgmarripRLGQITGHEPaaavelwrnrkvhqpaSLREE 347
Cdd:PTZ00297 590 PlkehvTTDTVFTYvvdntTSASGDGLAVVRVTHADVLRDI--------STLVMTGVLP----------------SSFKK 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 348 DVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKIkkgskgdtsvlKPTLMAAVPEIMDRIYKNVMNKVNEM 427
Cdd:PTZ00297 646 HLMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVKF-----------QPTILVAAPSLFSTSRLQLSRANERY 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 428 SAFQRNLFILAYNYKMEQIS-KGCSTPLCDRFVFRNVRRLLGGNIR-LLLC-GGAPLSATTQRFMNICFcCPVGQGYGLT 504
Cdd:PTZ00297 715 SAVYSWLFERAFQLRSRLINiHRRDSSLLRFIFFRATQELLGGCVEkIVLCvSEESTSFSLLEHISVCY-VPCLREVFFL 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 505 ESTGAGTITevwdyntgrvGAPLVCCEIKLKNWEEggyfntdkphPRGEILIGGQNVTMgyyKNEAKTKTDFFEDENGQR 584
Cdd:PTZ00297 794 PSEGVFCVD----------GTPAPSLQVDLEPFDE----------PSDGAGIGQLVLAK---KGEPRRTLPIAAQWKRDR 850
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 585 WLCTgdIGEfdPDGCLKIIdrkkdlvklqAGEYVSLGKVEAALKNLPLIDNICAYANSYHSyVIGFVVPN---------Q 655
Cdd:PTZ00297 851 TLRL--LGP--PLGILLPV----------AYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNrdtvefewrQ 915
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 656 KELTELARTKGFKGTWEELcnSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHY 735
Cdd:PTZ00297 916 SHCMGEGGGPARQLGWTEL--VAYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYF 993
|
....*...
gi 2268062224 736 QADIERMY 743
Cdd:PTZ00297 994 SSVIERFY 1001
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
135-312 |
1.80e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.50 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQA-------CFMYNFQLVtlyatlgGPAIVHGLNETEV 207
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGlaklgavVALLNTQQR-------GAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 208 TNIITSKELLQTklkdIVSLVPrlrhiiTVDGKPPTWSEFPK-GVIVHTMAAVQALGVKANVEKKAHSKPLPS-DIAVIM 285
Cdd:PRK08279 136 KHLIVGEELVEA----FEEARA------DLARPPRLWVAGGDtLDDPEGYEDLAAAAAGAPTTNPASRSGVTAkDTAFYI 205
|
170 180
....*....|....*....|....*..
gi 2268062224 286 YTSGSTGIPKGVMISHSNIIASITGMA 312
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLKAMGGFG 232
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
552-631 |
2.40e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 54.17 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 552 GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLP 631
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF---RGG--WFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVASREVEEALYTHP 441
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
501-633 |
2.49e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 53.89 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 501 YGLTESTGAGTIT---EVWDYN-TGR---VGAPLVCCEIKLKNweeggyFNTDKPHP---RGEILIGGQNVTMGYYKNEA 570
Cdd:PRK06178 360 WGMTETHTCDTFTagfQDDDFDlLSQpvfVGLPVPGTEFKICD------FETGELLPlgaEGEIVVRTPSLLKGYWNKPE 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2268062224 571 KTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI 633
Cdd:PRK06178 434 ATAEAL---RDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAV 490
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
266-732 |
2.54e-07 |
|
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: 53.59 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 266 ANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHsniiasitgmarRIprlgqITGHEPAaaVELWRNrkvhqpASLR 345
Cdd:cd05971 75 SNSGASALVTDGSDDPALIIYTSGTTGPPKGALHAH------------RV-----LLGHLPG--VQFPFN------LFPR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 346 EEDVY--------IGYLplahvleLSAELVCLSHGCRI-GYSSPQTLADQSSKIKKGSKGDTSVLKPT---LMAAVPEIM 413
Cdd:cd05971 130 DGDLYwtpadwawIGGL-------LDVLLPSLYFGVPVlAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkMMRQQGEQL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 414 DRiyknvmnkvnemsaFQRNLfilaynykmeqiskgcstplcdrfvfrnvrrllggniRLLLCGGAPLSATTQRFMNICF 493
Cdd:cd05971 203 KH--------------AQVKL-------------------------------------RAIATGGESLGEELLGWAREQF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 494 CCPVGQGYGLTESTGA-GTITEVWDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQN-VTM-GYYKNEA 570
Cdd:cd05971 232 GVEVNEFYGQTECNLViGNCSALFPIKPGSMGKPIPGHRVAIVD-DNG---TPLPPGEVGEIAVELPDpVAFlGYWNNPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 571 KTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIGf 650
Cdd:cd05971 308 ATEKKMAGD-----WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMAA---------VVG- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 651 vVPNQkeltelARTKGFKGtWEELcNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGlvtdafKLKRKE 730
Cdd:cd05971 372 -IPDP------IRGEIVKA-FVVL-NPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATG------KIRRRE 436
|
..
gi 2268062224 731 LK 732
Cdd:cd05971 437 LR 438
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
278-660 |
4.20e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.01 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprlgqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLA 357
Cdd:PRK12467 1717 PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY---------------------------QLSAADVVLQFTSFA 1769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 ---HVLELSAELVclsHGCRIGYSSPQTLADQSSKIkkgskgdtsvlkptlmaavpEIMDRIYKNVMNKVNemSAFQRNL 434
Cdd:PRK12467 1770 fdvSVWELFWPLI---NGARLVIAPPGAHRDPEQLI--------------------QLIERQQVTTLHFVP--SMLQQLL 1824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 435 filaynyKMEQISKGCSTplcdrfvfrnvrrllggnIRLLLCGGAPLSATTQRFMNICFCcPVG--QGYGLTEST---GA 509
Cdd:PRK12467 1825 -------QMDEQVEHPLS------------------LRRVVCGGEALEVEALRPWLERLP-DTGlfNLYGPTETAvdvTH 1878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 510 GTITEVWDynTGRVGAPLvccEIKLKNWeeGGYF--NTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED---EN 581
Cdd:PRK12467 1879 WTCRRKDL--EGRDSVPI---GQPIANL--STYIldASLNPVPIgvaGELYLGGVGLARGYLNRPALTAERFVADpfgTV 1951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 582 GQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPNQKELT 659
Cdd:PRK12467 1952 GSRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLV 2030
|
.
gi 2268062224 660 E 660
Cdd:PRK12467 2031 D 2031
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
278-733 |
4.76e-07 |
|
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: 52.82 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMIShsniiasitgmARRIPRLGQITGHEpaaavelwrnrkvhqpASLREEDVYIGYLPLA 357
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAIS-----------WRRTLVTSNLLSHD----------------LNLKNGDRTYTCMPLY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 H-VLELSAELVCLSHGCRIGYSS--------PQTLADQSSKIKKGSKgdtsvLKPTLMAAVPEIMDRiyknvMNKVnems 428
Cdd:cd05937 139 HgTAAFLGACNCLMSGGTLALSRkfsasqfwKDVRDSGATIIQYVGE-----LCRYLLSTPPSPYDR-----DHKV---- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 429 afqrnlfILAYnykmeqiSKGCSTPLCDRFvfrnvrrllggnirlllcggaplsatTQRFmNIcfccP-VGQGYGLTEST 507
Cdd:cd05937 205 -------RVAW-------GNGLRPDIWERF--------------------------RERF-NV----PeIGEFYAATEGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 508 GAgtiteVWDYNTGRVGAPLVCCEIKLKNWE-EGGYF------NTDKPHPR--------------GEIL--IGGQNVTM- 563
Cdd:cd05937 240 FA-----LTNHNVGDFGAGAIGHHGLIRRWKfENQVVlvkmdpETDDPIRDpktgfcvrapvgepGEMLgrVPFKNREAf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 564 -GYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEaalknlpliDNICAYA 640
Cdd:cd05937 315 qGYLHNEDATESKLVRDvfRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 641 NSYHSYVIGFVVPNQKeltELARTKGFKGTweelcNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDpwtpetGLV 720
Cdd:cd05937 385 DIAEANVYGVKVPGHD---GRAGCAAITLE-----ESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VAT 450
|
490
....*....|...
gi 2268062224 721 TDAFKLKRKELKT 733
Cdd:cd05937 451 TDNHKQQKGVLRD 463
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
545-633 |
4.86e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 53.31 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 545 TDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVS 619
Cdd:PLN02479 391 TMKPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF---ANG--WFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENIS 464
|
90
....*....|....
gi 2268062224 620 LGKVEAALKNLPLI 633
Cdd:PLN02479 465 SLEVENVVYTHPAV 478
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
280-610 |
4.94e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.19 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 280 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIprlgqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLAHV 359
Cdd:PRK07769 181 TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDAL---------------------------EGQEGDRGVSWLPFFHD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 360 LELSAELVCLSHGCRIGYSSPQTLADQSSK-IKKgskgdtsvlkptlMAAVPEIMDRIYKNVMNKVNEMSAfQRNLfila 438
Cdd:PRK07769 234 MGLITVLLPALLGHYITFMSPAAFVRRPGRwIRE-------------LARKPGGTGGTFSAAPNFAFEHAA-ARGL---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 439 ynykmeqiSKGCSTPLcDRfvfrnvrrllgGNIRLLLCGGAPLSATTQRFMNICFcCPVG-------QGYGLTEST---- 507
Cdd:PRK07769 296 --------PKDGEPPL-DL-----------SNVKGLLNGSEPVSPASMRKFNEAF-APYGlpptaikPSYGMAEATlfvs 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 508 ------------------GAGTITEVWDYNTGRVgAPLVCCEIKLKNWEEGGYFNTDKPHPR---GEILIGGQNVTMGYY 566
Cdd:PRK07769 355 ttpmdeeptviyvdrdelNAGRFVEVPADAPNAV-AQVSAGKVGVSEWAVIVDPETASELPDgqiGEIWLHGNNIGTGYW 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 567 KNEAKTKTDFFE-------------DENGQRWLCTGDIGEFdPDGCLKIIDRKKDLV 610
Cdd:PRK07769 434 GKPEETAATFQNilksrlseshaegAPDDALWVRTGDYGVY-FDGELYITGRVKDLV 489
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
229-305 |
8.10e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.74 E-value: 8.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 229 PRLrhIITVDGKPPTWSEFPKGVIVhTMAAVQALGvkanvEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNII 305
Cdd:PRK10252 556 PSL--LITTADQLPRFADVPDLTSL-CYNAPLAPQ-----GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
278-627 |
2.25e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.97 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASitgmarriprlgqitghepaaavelwrnrkvhQPASLR-----EEDVYIG 352
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLAN--------------------------------QRACLKffspkEDDVMMS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 353 YLPLAHVLEL-SAELVCLSHGCRIGYSS----PQTLADQSSKIKKgskgdtsvlkpTLMAAVPEIMDRIYKNVMNKVNEM 427
Cdd:PRK06334 230 FLPPFHAYGFnSCTLFPLLSGVPVVFAYnplyPKKIVEMIDEAKV-----------TFLGSTPVFFDYILKTAKKQESCL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 428 SAFqrnlfilaynykmeqiskgcstplcdRFVfrnvrrLLGGNIRlllcgGAPLSATTQR-FMNICfccpVGQGYGLTES 506
Cdd:PRK06334 299 PSL--------------------------RFV------VIGGDAF-----KDSLYQEALKtFPHIQ----LRQGYGTTEC 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 507 TGAGTITEVwdyNTGR----VGAPLVCCEIKLKNWEeggyfnTDKPHPRGE---ILIGGQNVTMGYYKNEaktKTDFFED 579
Cdd:PRK06334 338 SPVITINTV---NSPKhescVGMPIRGMDVLIVSEE------TKVPVSSGEtglVLTRGTSLFSGYLGED---FGQGFVE 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2268062224 580 ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAAL 627
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI-GAEMVSLEALESIL 452
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
282-619 |
2.40e-06 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 50.91 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 282 AVIMYTSGSTGIPKGVMISH-SNIIASItgMARRIPRLGqitghepaaavelwrnrkvhqpasLREEDVYIGYLPLAHvl 360
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVLHAL--MANNGDALG------------------------TSAADTMLPVVPLFH-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 361 elsaelvclSHGCRIGYSSPQTLADQsskIKKGSKGD-TSVL------KPTLMAAVPEIMdriyknvmnkvnemsafqrn 433
Cdd:PRK06018 232 ---------ANSWGIAFSAPSMGTKL---VMPGAKLDgASVYelldteKVTFTAGVPTVW-------------------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 434 LFILAYnykMEQisKGCSTPlcdrfvfrnvrrllggNIRLLLCGGAPL-SATTQRFMNicFCCPVGQGYGLTESTGAGTI 512
Cdd:PRK06018 280 LMLLQY---MEK--EGLKLP----------------HLKMVVCGGSAMpRSMIKAFED--MGVEVRHAWGMTEMSPLGTL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 513 TEV---WDYNTG--------RVGAPLVCCEIKLKNweeggyfNTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKtdf 576
Cdd:PRK06018 337 AALkppFSKLPGdarldvlqKQGYPPFGVEMKITD-------DAGKELPWdgktfGRLKVRGPAVAAAYYRVDGEIL--- 406
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2268062224 577 feDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVS 619
Cdd:PRK06018 407 --DDDG--FFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWIS 444
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
552-624 |
2.96e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 50.48 E-value: 2.96e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2268062224 552 GEILIGGQNVTMGYYKNEAKTKTDffedengqRWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVE 624
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASPLVD--------GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
278-610 |
3.43e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASiTGMARRIPRLgqitghepaaavelwrnrkvhqpaSLREEDVYIGYLPLA 357
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVAN-EQLIRHGFGI------------------------DLNPDDVIVSWLPLY 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 358 HVLELsaelvclshgcrIGysspqtladqsskikkgskgdtSVLKPtLMAAVPEIMdriyknvmnkvneMSAfqrNLFIL 437
Cdd:PRK05691 220 HDMGL------------IG----------------------GLLQP-IFSGVPCVL-------------MSP---AYFLE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 438 AYNYKMEQISKGCST----P-----LC-DRFVFRNVRRLLGGNIRLLLCGGAP-----LSATTQRFMNiC-------FCC 495
Cdd:PRK05691 249 RPLRWLEAISEYGGTisggPdfayrLCsERVSESALERLDLSRWRVAYSGSEPirqdsLERFAEKFAA-CgfdpdsfFAS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 496 pvgqgYGLTEST--------GAG-TITEVWDYNTGR------VGAPLVCC-------EIKLKNWEEGGYFNTDKPhprGE 553
Cdd:PRK05691 328 -----YGLAEATlfvsggrrGQGiPALELDAEALARnraepgTGSVLMSCgrsqpghAVLIVDPQSLEVLGDNRV---GE 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2268062224 554 ILIGGQNVTMGYYKN-EAKTKTdfFEDENGQRWLCTGDIGeFDPDGCLKIIDRKKDLV 610
Cdd:PRK05691 400 IWASGPSIAHGYWRNpEASAKT--FVEHDGRTWLRTGDLG-FLRDGELFVTGRLKDML 454
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
135-633 |
3.47e-06 |
|
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: 50.19 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK 214
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 215 ELLQtklkdivslvprlrhiitvdgkpptwsefpkgvivhtmaavqalgvkanvekkahsKPLPSDIAVIMYTSGSTGIP 294
Cdd:cd05969 81 ELYE--------------------------------------------------------RTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 295 KGVMISHSNIIAS-ITGmarriprlgqitghepaaavelwrnrkvHQPASLREEDVYIGYLPLAHVLELSAELVC-LSHG 372
Cdd:cd05969 105 KGVLHVHDAMIFYyFTG----------------------------KYVLDLHPDDIYWCTADPGWVTGTVYGIWApWLNG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 373 CrigysspQTLADQSSKIKKGSKGDTSVLKPTLMAAVPEIMDRIyknvMNKVNEMSAfqrnlfilayNYKMEqiskgcst 452
Cdd:cd05969 157 V-------TNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRML----MKEGDELAR----------KYDLS-------- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 453 plcdrfvfrnvrrllggNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEsTGAGTITEV--WDYNTGRVGAPLVCC 530
Cdd:cd05969 208 -----------------SLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTE-TGSIMIANYpcMPIKPGSMGKPLPGV 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 531 EIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTM--GYYKNEAKTKTDFFedeNGqrWLCTGDIGEFDPDGCLKIIDRKKD 608
Cdd:cd05969 270 KAAVVD-ENG---NELPPGTKGILALKPGWPSMfrGIWNDEERYKNSFI---DG--WYLTGDLAYRDEDGYFWFVGRADD 340
|
490 500
....*....|....*....|....*
gi 2268062224 609 LVKLqAGEYVSLGKVEAALKNLPLI 633
Cdd:cd05969 341 IIKT-SGHRVGPFEVESALMEHPAV 364
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
475-653 |
3.50e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 50.26 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 475 LCGGA--PLSATTQ-RFMNI-CFCcpvgqGYGLTEStgAGTITEVWDYNTGRVGAPLVCCEIKLKNweeggyfntdkphp 550
Cdd:PRK09029 246 LLGGAaiPVELTEQaEQQGIrCWC-----GYGLTEM--ASTVCAKRADGLAGVGSPLPGREVKLVD-------------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 551 rGEILIGGQNVTMGYYKNEAKTKtdfFEDENGqrWLCTGDIGEFDpDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNL 630
Cdd:PRK09029 305 -GEIWLRGASLALGYWRQGQLVP---LVNDEG--WFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQH 376
|
170 180
....*....|....*....|...
gi 2268062224 631 PLIDNIcayansyhsyvigFVVP 653
Cdd:PRK09029 377 PLVQQV-------------FVVP 386
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
471-741 |
3.83e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 50.08 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 471 IRLLLCGGAPLSATTQRFMnICFCCPV-GQGYGLTEStgaGTIT----EVWDYNTGRVGAPLVCCEIKLKNwEEGgyfnt 545
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAM-IEWWGPViYEYYGSTES---GAVTfatsEDALSHPGTVGKAAPGAELRFVD-EDG----- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 546 dKPHPRGEI------LIGGQNVTmgyYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVS 619
Cdd:PRK12406 343 -RPLPQGEIgeiysrIAGNPDFT---YHNKPEKRAEIDRGG----FITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIY 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 620 LGKVEAALKNLPLIDNiCAYansyhsyvigFVVPNQkeltELArtkgfkgtwEELCNSSEMENEVlkVLSEAAISASLE- 698
Cdd:PRK12406 414 PAEIEAVLHAVPGVHD-CAV----------FGIPDA----EFG---------EALMAVVEPQPGA--TLDEADIRAQLKa 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2268062224 699 ---KFEIPLKIRLSPDpwTPEtglvTDAFKLKRKELKTHYQADIER 741
Cdd:PRK12406 468 rlaGYKVPKHIEIMAE--LPR----EDSGKIFKRRLRDPYWANAGR 507
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
237-320 |
4.17e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 49.66 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 237 VDGKPPTWSEFPKGVIVHTMAAVQALGVkanvekkahSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIP 316
Cdd:PRK07824 2 LAGRAPALLPVPAQDERRAALLRDALRV---------GEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG 72
|
....
gi 2268062224 317 RLGQ 320
Cdd:PRK07824 73 GPGQ 76
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
564-663 |
6.21e-06 |
|
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: 49.37 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 564 GYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDN-------- 635
Cdd:COG1021 393 GYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENLLLAHPAVHDaavvampd 467
|
90 100 110
....*....|....*....|....*....|....*.
gi 2268062224 636 ------ICAyansyhsyvigFVVPNQKELT--ELAR 663
Cdd:COG1021 468 eylgerSCA-----------FVVPRGEPLTlaELRR 492
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
499-621 |
1.43e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 48.50 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 499 QGYGLTESTGAGTIT-----EVWDYNTGRVGaplvCC-------EIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYY 566
Cdd:PRK07470 310 QYFGLGEVTGNITVLppalhDAEDGPDARIG----TCgfertgmEVQIQD-DEG---RELPPGETGEICVIGPAVFAGYY 381
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2268062224 567 KN-EAKTKTdfFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLvklqageYVSLG 621
Cdd:PRK07470 382 NNpEANAKA--FRDG----WFRTGDLGHLDARGFLYITGRASDM-------YISGG 424
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
258-306 |
1.50e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.40 E-value: 1.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2268062224 258 AVQALGVKANVEKKAHSKPLPSdIAVIMYTSGSTGIPKGVMISHSNIIA 306
Cdd:PRK05850 140 EVDLLDLDSPRGSDARPRDLPS-TAYLQYTSGSTRTPAGVMVSHRNVIA 187
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
501-610 |
3.10e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 47.21 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 501 YGLTESTGAGTIT-EVWDYNTGRVGAPLVCceiKLKNWEEGGyfntdKPHPRGEI-LI----GGQNVTmgYYKNEAKTKt 574
Cdd:PRK08276 294 YASSEGGGVTVITsEDWLAHPGSVGKAVLG---EVRILDEDG-----NELPPGEIgTVyfemDGYPFE--YHNDPEKTA- 362
|
90 100 110
....*....|....*....|....*....|....*.
gi 2268062224 575 dffEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLV 610
Cdd:PRK08276 363 ---AARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI 395
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
552-656 |
3.23e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.08 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 552 GEILIGGQNVTMGYYKNEAKTKT--------DFFEDENGQ----RWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVs 619
Cdd:PRK05620 386 GEIQVRGNWVTASYYHSPTEEGGgaastfrgEDVEDANDRftadGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWI- 463
|
90 100 110
....*....|....*....|....*....|....*..
gi 2268062224 620 lgkVEAALKNLplidnICAYANSYHSYVIGFvvPNQK 656
Cdd:PRK05620 464 ---YSAQLENY-----IMAAPEVVECAVIGY--PDDK 490
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
135-312 |
3.93e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 47.05 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWMIAAQACfmynfqlvtlyATLGgpAIVHGLN----ETEVTNI 210
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 211 ITSKE----LLQTKLKDI----------VSLVPRLRHIITVDGKPPTWSEFPKGVIV-----HTMAAVQALGVKANVekk 271
Cdd:PRK06164 103 LGRGRarwlVVWPGFKGIdfaailaavpPDALPPLRAIAVVDDAADATPAPAPGARVqlfalPDPAPPAAAGERAAD--- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2268062224 272 ahskplPSDIAVIMYTSGSTGIPKGVM------ISHSNIIASITGMA 312
Cdd:PRK06164 180 ------PDAGALLFTTSGTTSGPKLVLhrqatlLRHARAIARAYGYD 220
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
248-615 |
7.39e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.91 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 248 PKGVIVHTMAAVQALGVKANVEKKAHSKPlpsdiAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiprlgqiTGHEPA 327
Cdd:PRK05851 126 DSSVTVHDLATAAHTNRSASLTPPDSGGP-----AVLQGTAGSTGTPRTAILSPGAVLSNLRGLNAR-------VGLDAA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 328 aavelwrnrkvhqpaslreEDVYIGYLPLAHVLELSAELVCLSHGCRIgYSSPqTLADQSSKIKKGSKGDTSvlKPTLMA 407
Cdd:PRK05851 194 -------------------TDVGCSWLPLYHDMGLAFLLTAALAGAPL-WLAP-TTAFSASPFRWLSWLSDS--RATLTA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 408 AvPEimdriyknvmnkvnemsafqrnlfiLAYNykmeqiskgcstplcdrFVFRNVRRLLG---GNIRLLLCGGAPLS-A 483
Cdd:PRK05851 251 A-PN-------------------------FAYN-----------------LIGKYARRVSDvdlGALRVALNGGEPVDcD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 484 TTQRFMNIcfCCPVG-------QGYGLTESTGAGT---------ITEVWDYNTG------RVGAPLVCCEIKLKNWEEGG 541
Cdd:PRK05851 288 GFERFATA--MAPFGfdagaaaPSYGLAESTCAVTvpvpgiglrVDEVTTDDGSgarrhaVLGNPIPGMEVRISPGDGAA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2268062224 542 YFNTdkpHPRGEILIGGQNvTMGYYKNEAKTKTDffedengqRWLCTGDIGEFdPDGCLKIIDRKKDLVKLqAG 615
Cdd:PRK05851 366 GVAG---REIGEIEIRGAS-MMSGYLGQAPIDPD--------DWFPTGDLGYL-VDGGLVVCGRAKELITV-AG 425
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
469-631 |
7.42e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 469 GNIRLLLCGGAPLSATTQ-RFMNICFCCPVGQGYGLTEStgAGTIT----EVWDYNTGRVGAPL--VCCEIKlknweeGG 541
Cdd:PRK05691 1388 TSLRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTET--AINVThwqcQAEDGERSPIGRPLgnVLCRVL------DA 1459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 542 YFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYV 618
Cdd:PRK05691 1460 ELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDplgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLR-GFRV 1538
|
170
....*....|...
gi 2268062224 619 SLGKVEAALKNLP 631
Cdd:PRK05691 1539 EPEEIQARLLAQP 1551
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
500-654 |
1.40e-04 |
|
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: 44.60 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 500 GYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEaktktdffeD 579
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDG---REVPDGEVGEIVARGPTVMAGYWNRP---------E 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2268062224 580 ENGQR----WLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIGfvVPN 654
Cdd:cd17636 209 VNARRtrggWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAA---------VIG--VPD 275
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
216-682 |
1.65e-04 |
|
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: 44.81 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 216 LLQTKLK--DIVSLVPR--LRHIITVDGKPPTWSEFPKGVIVHTMAAVQALGVKANVEKKAHSKPL-PSDIAVIMYTSGS 290
Cdd:cd05923 82 LINPRLKaaELAELIERgeMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPRePEQPAFVFYTSGT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 291 TGIPKGVMISHSNIIASITGMArriprlgqitghepaaavelwrnrkvHQpASLR--EEDVYIGYLPLAHVLELSAELV- 367
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMS--------------------------TQ-AGLRhgRHNVVLGLMPLYHVIGFFAVLVa 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 368 CLSHG---CRIGYSSPQTLADQSSKikkgskgdtsvLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFilaynykme 444
Cdd:cd05923 215 ALALDgtyVVVEEFDPADALKLIEQ-----------ERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTF--------- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 445 qisKGCSTPlcdRFVFRNVRRLLGGnirlllcggaplsattqRFMNIcfccpvgqgYGLTEstgAGTITEVWDYNTGRVG 524
Cdd:cd05923 275 ---AGATMP---DAVLERVNQHLPG-----------------EKVNI---------YGTTE---AMNSLYMRDARTGTEM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 525 APLVCCEIKLKNWeEGGYFNTDKPHPRGEILI--GGQNVTMGYYKNEAKTKTDFFEdengqRWLCTGDIGEFDPDGCLKI 602
Cdd:cd05923 320 RPGFFSEVRIVRI-GGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQD-----GWYRTGDVGYVDPSGDVRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 603 IDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVPNQKELTELArtkgfkgtWEELCNSSE 679
Cdd:cd05923 394 LGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvadERWGQSVTACVVPREGTLSADE--------LDQFCRASE 464
|
...
gi 2268062224 680 MEN 682
Cdd:cd05923 465 LAD 467
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
552-654 |
1.84e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.15 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 552 GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALK 628
Cdd:PRK12467 3436 GELYIGGVGLARGYHQRPSLTAERFVADpfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIEARLL 3514
|
90 100
....*....|....*....|....*...
gi 2268062224 629 NLPLIDN--ICAYANSYHSYVIGFVVPN 654
Cdd:PRK12467 3515 QHPSVREavVLARDGAGGKQLVAYVVPA 3542
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
268-654 |
1.87e-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: 44.59 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 268 VEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASiTGMARriprlgqITGhepaaavelwrnrkvhqpasLREE 347
Cdd:cd05938 133 VPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQC-SGFLS-------LCG--------------------VTAD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 348 DVYIGYLPLAHVlelSAELVCLsHGCrigysspqtladqsskIKKGSkgdTSVLKPTLMAAvpEIMDRIYK-NVmnkvne 426
Cdd:cd05938 185 DVIYITLPLYHS---SGFLLGI-GGC----------------IELGA---TCVLKPKFSAS--QFWDDCRKhNV------ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 427 mSAFQrnlfilaynYKMEQISKGCSTPLCDRFVFRNVRRLLGGNIRlllcggaplsATT-----QRFMNICFCcpvgQGY 501
Cdd:cd05938 234 -TVIQ---------YIGELLRYLCNQPQSPNDRDHKVRLAIGNGLR----------ADVwreflRRFGPIRIR----EFY 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 502 GLTESTgAGTItevwDYnTGRVGA-PLVCCEIKLKNWEEGGYFNTDKPHP------------RGE--ILIG---GQNVTM 563
Cdd:cd05938 290 GSTEGN-IGFF----NY-TGKIGAvGRVSYLYKLLFPFELIKFDVEKEEPvrdaqgfcipvaKGEpgLLVAkitQQSPFL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 564 GYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNicayAN 641
Cdd:cd05938 364 GYAGDKEQTEKKLLRDvfKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWK-GENVATTEVADVLGLLDFLQE----VN 438
|
410
....*....|...
gi 2268062224 642 SYhsyviGFVVPN 654
Cdd:cd05938 439 VY-----GVTVPG 446
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
135-733 |
2.71e-04 |
|
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: 44.27 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 135 LSYEDVFIRALDFGNGLQMLGQKPKANIAIFCETRAEWmiaaqacfmynfqLVTLYAT--LGGPAivhglnetevtniit 212
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEY-------------VLLWLGLvkIGAVA--------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 213 skELLQTKLKDIVslvprLRHIITVDGkpptwsefPKGVIVhtmaavqalgvkanvekkahskplpsDIAVIMYTSGSTG 292
Cdd:cd05940 56 --ALINYNLRGES-----LAHCLNVSS--------AKHLVV--------------------------DAALYIYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 293 IPKGVMISHsniiasitgmaRRIPRLGQITGHEPAAAvelwrnrkvhqpaslrEEDVYIGYLPLAHVlelSAELVCLsHG 372
Cdd:cd05940 95 LPKAAIISH-----------RRAWRGGAFFAGSGGAL----------------PSDVLYTCLPLYHS---TALIVGW-SA 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 373 CRIGysspqtladqsskikkgskGDTSVLKPTLMAavpeimdriyknvmnkvnemSAFQRNlfILAYNYKMEQ-ISKGC- 450
Cdd:cd05940 144 CLAS-------------------GATLVIRKKFSA--------------------SNFWDD--IRKYQATIFQyIGELCr 182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 451 ---STPLCDRFVFRNVRRLLGGNIRlllcgGAPLSATTQRFMNICFCcpvgQGYGLTESTGA--------GTITEVWDYN 519
Cdd:cd05940 183 yllNQPPKPTERKHKVRMIFGNGLR-----PDIWEEFKERFGVPRIA----EFYAATEGNSGfinffgkpGAIGRNPSLL 253
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 520 TGRVGAPLVCCEIK----LKNweEGGYFntdKPHPRGE--ILIG----GQNVTmGYYKN---EAKTKTDFFEDenGQRWL 586
Cdd:cd05940 254 RKVAPLALVKYDLEsgepIRD--AEGRC---IKVPRGEpgLLISrinpLEPFD-GYTDPaatEKKILRDVFKK--GDAWF 325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 587 CTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNicayANSYhsyviGFVVPNqkeltelarTKG 666
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWK-GENVSTTEVAAVLGAFPGVEE----ANVY-----GVQVPG---------TDG 386
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2268062224 667 FKGTweELCNSSEMENEVLKVLSeAAISASLEKFEIPLKIRLSPDPWTPETglvtdaFKLKRKELKT 733
Cdd:cd05940 387 RAGM--AAIVLQPNEEFDLSALA-AHLEKNLPGYARPLFLRLQPEMEITGT------FKQQKVDLRN 444
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-321 |
3.13e-04 |
|
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: 43.99 E-value: 3.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2268062224 276 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRI-PRLGQI 321
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYgIRPGEV 128
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
552-610 |
3.91e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.78 E-value: 3.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 552 GEILIGGQNVTMGYYKNEAKTKTDFfedeNGQ-----------RWLCTGDIGeFDPDGCLKIIDRKKDLV 610
Cdd:PRK05850 398 GEIWVHGDNVAAGYWQKPEETERTF----GATlvdpspgtpegPWLRTGDLG-FISEGELFIVGRIKDLL 462
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
554-633 |
5.47e-04 |
|
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: 43.19 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 554 ILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLI 633
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDG----FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLENALMGHPKV 437
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
274-313 |
7.64e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 42.68 E-value: 7.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2268062224 274 SKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 313
Cdd:PRK09192 171 PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISH 210
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
552-663 |
7.86e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 552 GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALK 628
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAERFVADpfaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIR-GFRIELGEIESRLL 2611
|
90 100 110
....*....|....*....|....*....|....*..
gi 2268062224 629 NLPLIDN--ICAYANSYHSYVIGFVVPNQKELTELAR 663
Cdd:PRK05691 2612 EHPAVREavVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
277-304 |
9.63e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 9.63e-04
10 20
....*....|....*....|....*...
gi 2268062224 277 LPSDIAVIMYTSGSTGIPKGVMISHSNI 304
Cdd:PRK05691 2331 LPQHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
278-312 |
1.56e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 42.07 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|....*
gi 2268062224 278 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMA 312
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIA 3270
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
278-299 |
2.12e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 2.12e-03
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
552-668 |
3.63e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.92 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2268062224 552 GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALK 628
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFVPHpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIR-GYRIELGEIEARLH 4145
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2268062224 629 NLPLIDN--ICAYANSYHSYVIGFVVPNQKELTELARTKGFK 668
Cdd:PRK05691 4146 EQAEVREaaVAVQEGVNGKHLVGYLVPHQTVLAQGALLERIK 4187
|
|
| |
