|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
121-696 |
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: 832.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 LITSvellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrPTPSDMAIVMYTSG 280
Cdd:cd17639 81 IFTD--------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 281 STGRPKGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqssKIKKGS 359
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 360 KGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVKALLGGNVRMM 439
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 440 LSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYtINDKPNPRGEI 519
Cdd:cd17639 256 LSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGY-STDKPPPRGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 520 VIGGQNISMGYFKNEEKTAEDYsvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLID 599
Cdd:cd17639 334 LIRGPNVFKGYYKNPEKTKEAF----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 600 NICAFAKSDQSYVISFVVPNQKRLTLLAQQKGV-EGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPW 678
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 530422004 679 TPETGLVTDAFKLKRKEL 696
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
32-708 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 814.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 32 FLTNAKKKnamAKRIKAKPTSDKPGSPYRSvTHFDSLavIDIP--GADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQ 109
Cdd:PLN02387 17 LLRGSKKG---KKRGVPVDVGGEPGYAIRN-ARFPEL--VETPweGATTLAALFEQSCKKYSDKRLLGTRKLISREFETS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 110 PNGKVFKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAV 189
Cdd:PLN02387 91 SDGRKFEKLHLGEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 190 VHGLNESEASYLITSVEllesKLKTaLLDIS----CVKHIIYVDNKAINKAEYPEGFE---IHSMQSVEELG-SNPenlg 261
Cdd:PLN02387 171 CHSLNETEVTTVICDSK----QLKK-LIDISsqleTVKRVIYMDDEGVDSDSSLSGSSnwtVSSFSEVEKLGkENP---- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIG 341
Cdd:PLN02387 242 VDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 342 YSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKK------GY 415
Cdd:PLN02387 322 YGSPLTLTDTSNKIKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGswfgawGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 416 DAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICC 495
Cdd:PLN02387 402 EKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCC 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 496 EIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PLN02387 482 YVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 576 KLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIR 654
Cdd:PLN02387 562 KLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLS 641
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 530422004 655 EAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 708
Cdd:PLN02387 642 KAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
121-708 |
0e+00 |
|
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: 535.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNT--IAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEA 198
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 199 SylitsvellesklktalldiscvkhIIYVDnkainkaeypEGFEIHSMQSVEELGSNPEnlgIPPSRPTPSDMAIVMYT 278
Cdd:cd05927 81 S-------------------------IVFCD----------AGVKVYSLEEFEKLGKKNK---VPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 279 SGSTGRPKGVMMHHSNLIAGMTGQC---ERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSS--PLTLSDqss 353
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 354 kikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKG--YDAPLCNLLLFKKVKAL 431
Cdd:cd05927 200 --------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 432 LGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTIND 511
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 512 kPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAA 591
Cdd:cd05927 352 -PNPRGEVCIRGPNVFSGYYKDPEKTAE--ALDEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 592 LKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQK-GVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIK 670
Cdd:cd05927 427 YARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKA 506
|
570 580 590
....*....|....*....|....*....|....*...
gi 530422004 671 VRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 708
Cdd:cd05927 507 IHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-711 |
6.90e-153 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 456.48 E-value: 6.90e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 72 DIPGADTLDKLFDHAVSKFGKKDSLGTREilseenemqpngkvfkkliLGNYKWMNYLEVNRRVNNFGSGLTALGLKPKN 151
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKE-------------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 152 TIAIFCETRAEWMIA--------AQTcfkynfplVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVK 223
Cdd:COG1022 67 RVAILSDNRPEWVIAdlailaagAVT--------VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 224 HIIYVDNKAInkaeyPEGFEIHSMQSVEELG---SNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT 300
Cdd:COG1022 139 HIVVLDPRGL-----RDDPRLLSLDELLALGrevADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 301 GQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYS-SPLTLSDqsskikkgskgDCTVLKPTLMAAVPEIMD 379
Cdd:COG1022 214 ALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------DLREVKPTFMLAVPRVWE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 380 RIYKNVMSKVQEMNYIQKTLF----KIGYDYKlEQIKKGYDAP--------LCNLLLFKKVKALLGGNVRMMLSGGAPLS 447
Cdd:COG1022 282 KVYAGIQAKAEEAGGLKRKLFrwalAVGRRYA-RARLAGKSPSlllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 448 PQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKlkdwqeggytINDKpnprGEIVIGGQ 524
Cdd:COG1022 361 PELARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK----------IAED----GEILVRGP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 525 NISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAF 604
Cdd:COG1022 423 NVMKGYYKNPEATAE--AFDADG--WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVV 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 605 AkSDQSYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEPWTPETG 683
Cdd:COG1022 499 G-DGRPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEV-DRANA-GLSRAEQIKRFRLLPKEFTIENG 575
|
650 660
....*....|....*....|....*...
gi 530422004 684 LVTDAFKLKRKELRNHYLKDIERMYGGK 711
Cdd:COG1022 576 ELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
56-708 |
7.29e-153 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 458.41 E-value: 7.29e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 56 GSPYRSVTHFDslaviDIPGADTLDKLFDHAVSKFGKKDSLGTReilseeneMQPNGKVfkklilGNYKWMNYLEVNRRV 135
Cdd:PLN02736 28 RSPLKLVSRFP-----DHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 136 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLkTA 215
Cdd:PLN02736 89 TAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLL-SC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 216 LLDISCVKHIIYV--DNKAINKAEYPEGFEIHSMQSVEELG-SNPEnlgiPPSRPTPSDMAIVMYTSGSTGRPKGVMMHH 292
Cdd:PLN02736 168 LSEIPSVRLIVVVggADEPLPSLPSGTGVEIVTYSKLLAQGrSSPQ----PFRPPKPEDVATICYTSGTTGTPKGVVLTH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 293 SNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSP--LTLSDqsskikkgskgDCTVLKPTL 370
Cdd:PLN02736 244 GNLIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGdnLKLMD-----------DLAALRPTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 371 MAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD-APLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQ 449
Cdd:PLN02736 312 FCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 450 THRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMG 529
Cdd:PLN02736 392 VMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 530 YFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:PLN02736 472 YYKDEVQTRE--VIDEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLN 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 610 SYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDA 688
Cdd:PLN02736 548 SSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPT 627
|
650 660
....*....|....*....|
gi 530422004 689 FKLKRKELRNHYLKDIERMY 708
Cdd:PLN02736 628 FKVKRPQAKAYFAKAISDMY 647
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
124-708 |
7.96e-144 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 436.72 E-value: 7.96e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 124 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT 203
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 204 S---VELLESKLKTALLDiSCVkhIIYVDnkainkaEYPEGFEIHSMQ-----SVEELG-SNPENLgiPPSRPTPSD-MA 273
Cdd:PTZ00216 200 NgknVPNLLRLMKSGGMP-NTT--IIYLD-------SLPASVDTEGCRlvawtDVVAKGhSAGSHH--PLNIPENNDdLA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 274 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGL-GPK---DTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLS 349
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGPPeedETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 350 DQSSKikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVK 429
Cdd:PTZ00216 348 DTFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 430 ALLGGNVRMMLSGGAPLSPQTHRFMNVCFcCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEggYTI 509
Cdd:PTZ00216 424 AVLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEE--YKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 510 NDKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVE 589
Cdd:PTZ00216 501 TDTPEPRGEILLRGPFLFKGYYKQEELTRE--VLDEDG--WFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALE 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 590 AALKNCPLIDN--ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEI 667
Cdd:PTZ00216 577 ALYGQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 530422004 668 PIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 708
Cdd:PTZ00216 657 VRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
121-696 |
1.83e-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: 406.60 E-value: 1.83e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 LITSvellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrpTPSDMAIVMYTSG 280
Cdd:cd05907 81 LFVE---------------------------------------------------------------DPDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 281 STGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRIGYSSPL-TLSDQSSKIkkg 358
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAeTLLDDLSEV--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 359 skgdctvlKPTLMAAVPEIMDRIYKNVmsKVQEMNYIQKTLFKIGydykleqikkgydaplcnlllfkkvkalLGGNVRM 438
Cdd:cd05907 174 --------RPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLA----------------------------VGGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 439 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytindkpnpRGE 518
Cdd:cd05907 216 AASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--------------DGE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 519 IVIGGQNISMGYFKNEEKTAEDysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 598
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAEA--LDADG--WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLI 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 599 DNICAFAkSDQSYVISFVVPNQKRLTLLAQQKGVEGTWV-DICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEP 677
Cdd:cd05907 357 SQAVVIG-DGRPFLVALIVPDPEALEAWAEEHGIAYTDVaELAANPAVRAEIEAAV-EAANA-RLSRYEQIKKFLLLPEP 433
|
570
....*....|....*....
gi 530422004 678 WTPETGLVTDAFKLKRKEL 696
Cdd:cd05907 434 FTIENGELTPTLKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
44-708 |
2.84e-122 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 379.54 E-value: 2.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 44 KRIKAKPTSdkpGSPYRSVTHFDSLAVIDiPGADTLDKLFDHAVSKFGKKDSLGTREILseenemqpNGKVfkklilGNY 123
Cdd:PLN02430 13 KGKDGKPSV---GPVYRNLLSKKGFPPID-SDITTAWDIFSKSVEKYPDNKMLGWRRIV--------DGKV------GPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 124 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEasylIT 203
Cdd:PLN02430 75 MWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAE----ID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 204 SVELLESKLKtALLDISC-----VKHIIYVDN---KAINKAEyPEGFEIHSMQSVEELG-SNPENlgipPSRPTPSDMAI 274
Cdd:PLN02430 151 FVFVQDKKIK-ELLEPDCksakrLKAIVSFTSvteEESDKAS-QIGVKTYSWIDFLHMGkENPSE----TNPPKPLDICT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 275 VMYTSGSTGRPKGVMMHHSNLIAGMTG------QCEriPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltl 348
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGvdlfmeQFE--DKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYH---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 349 SDQSSKikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLLL 424
Cdd:PLN02430 299 GDLNAL-----RDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 FKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPLICCEIKLKDWQ 503
Cdd:PLN02430 374 FRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 504 EGGYTINDKPnPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYV 583
Cdd:PLN02430 454 EMGYDPLGEP-PRGEICVRGKCLFSGYYKNPELTEE---VMKDG--WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 584 SLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLE 663
Cdd:PLN02430 528 ALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLR 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 530422004 664 RFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 708
Cdd:PLN02430 608 GFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
47-708 |
2.72e-116 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 364.16 E-value: 2.72e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 47 KAKPTSD-KP--GSPYRSVTHFDSLavIDIP-GADTLDKLFDHAVSKFGKKDSLGTREILseenemqpNGKVfkklilGN 122
Cdd:PLN02861 11 ESRPATGgKPsaGPVYRSIYAKDGL--LDLPaDIDSPWQFFSDAVKKYPNNQMLGRRQVT--------DSKV------GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 123 YKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASylI 202
Cdd:PLN02861 75 YVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 203 TSVEllESKLKTALldiSCVKH--------IIYVDNKAINKAEYPE-GFEIHSMQSVEELGSNPENLgiPPSRPTpsDMA 273
Cdd:PLN02861 153 AFVQ--ESKISSIL---SCLPKcssnlktiVSFGDVSSEQKEEAEElGVSCFSWEEFSLMGSLDCEL--PPKQKT--DIC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 274 IVMYTSGSTGRPKGVMMHHSNLIAG------MTGQCERIpgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSplt 347
Cdd:PLN02861 224 TIMYTSGTTGEPKGVILTNRAIIAEvlstdhLLKVTDRV--ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQ--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 lSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLL 423
Cdd:PLN02861 299 -GDIRYLME-----DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 424 LFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGaGTVTEVTDY--TTGRVGAPLICCEIKLKD 501
Cdd:PLN02861 373 VFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANVfsMVGTVGVPMTTIEARLES 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 502 WQEGGY-TINDKPnpRGEIVIGGQNISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 580
Cdd:PLN02861 452 VPEMGYdALSDVP--RGEICLRGNTLFSGYHKRQDLTEEVLI-----DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQG 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 581 EYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM 660
Cdd:PLN02861 525 EYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 530422004 661 KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 708
Cdd:PLN02861 605 QLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
48-708 |
2.57e-113 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 356.64 E-value: 2.57e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 48 AKPTSD-KP--GSPYRSVTHFDSLAViDIPGADTLDKLFDHAVSKFGKKDSLGTREILseenemqpNGKVfkklilGNYK 124
Cdd:PLN02614 14 GKEGSDgRPsvGPVYRSIFAKDGFPN-PIEGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 125 WMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 204
Cdd:PLN02614 79 WQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 205 VELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE--GFEIHSMQSVEELGSNPEnLGIPPSRPtpSDMAIVMYTSGST 282
Cdd:PLN02614 159 EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLGEGKQ-YDLPIKKK--SDICTIMYTSGTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 283 GRPKGVMMHHSNLIAGMTGQCERI----PGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQSSKIKkg 358
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAGVIRLLksanAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR----GDVKLLIE-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 359 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLLLFKKVKALLGG 434
Cdd:PLN02614 310 ---DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 435 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCgAGTVTEVTDY--TTGRVGAPLICCEIKLKDWQEGGYTINDK 512
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVDIRLESVPEMEYDALAS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 513 pNPRGEIVIGGQNISMGYFKNEEKTAEDYsVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAAL 592
Cdd:PLN02614 466 -TPRGEICIRGKTLFSGYYKREDLTKEVL-IDG----WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIY 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 593 KNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVR 672
Cdd:PLN02614 540 GEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIH 619
|
650 660 670
....*....|....*....|....*....|....*.
gi 530422004 673 LSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 708
Cdd:PLN02614 620 LDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
118-578 |
2.75e-112 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 345.45 E-value: 2.75e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 118 LILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESE 197
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 198 ASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEypegfeihsmqSVEELGSNPENLGIPPSRPTPSDMAIVMY 277
Cdd:pfam00501 94 AKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 278 TSGSTGRPKGVMMHHSNLIAGMTGQ---CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSPLTLSDQss 353
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALDP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 354 kikKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmskvqemnyiqktlfkigydykleqikkgydaplcnlllfKKVKALLG 433
Cdd:pfam00501 241 ---AALLELIERYKVTVLYGVPTLLNMLLEA-----------------------------------------GAPKRALL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 434 GNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDWQEGGYTin 510
Cdd:pfam00501 277 SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPlplDEDLRSLGSVGRPLPGTEVKIVDDETGEPV-- 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530422004 511 dKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQ 578
Cdd:pfam00501 355 -PPGEPGELCVRGPGVMKGYLNDPELTAEAFDED----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
121-693 |
1.04e-70 |
|
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: 238.03 E-value: 1.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFkynfplvtlyaTLGKEAVVHGLNES--EA 198
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIM-----------ALGAVDVVRGSDSSveEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 199 SYLITSVEllesklktalldisCVkhIIYVDNkainkaeypegfeihsmqsveelgsnpenlgippsrpTPSDMAIVMYT 278
Cdd:cd17640 70 LYILNHSE--------------SV--ALVVEN-------------------------------------DSDDLATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 279 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGlGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkg 358
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPP-QPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKD-------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 359 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIgydykleqikkgydaplcnlllfkkvkALLGGNVRM 438
Cdd:cd17640 168 ---DLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF---------------------------FLSGGIFKF 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 439 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTindKPNPRGE 518
Cdd:cd17640 218 GISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVL---PPGEKGI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 519 IVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 598
Cdd:cd17640 294 VWVRGPQVMKGYYKNPEATSK--VLDSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFI 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 599 DNICAFAKsDQSYVISFVVPNQKRLTLLAQQKGV---EGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSP 675
Cdd:cd17640 370 EQIMVVGQ-DQKRLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLE 448
|
570
....*....|....*...
gi 530422004 676 EPWTpETGLVTDAFKLKR 693
Cdd:cd17640 449 EPFI-ENGEMTQTMKIKR 465
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
126-703 |
7.47e-64 |
|
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: 219.30 E-value: 7.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpsdmAIVMYTSGSTGRP 285
Cdd:COG0318 103 -------------------------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI---GYSSPLTLSDQsskIKKGskg 361
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAAL-GLTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLvllPRFDPERVLEL---IERE--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 362 dctvlKPTLMAAVPEIMDRiyknvmskvqemnyiqktlfkigydykleqikkgydapLCNLLLFKKVKAllgGNVRMMLS 441
Cdd:COG0318 189 -----RVTVLFGVPTMLAR--------------------------------------LLRHPEFARYDL---SSLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 442 GGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDwqeggytINDKPNPR-- 516
Cdd:COG0318 223 GGAPLPPELlERFEER-FGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVD-------EDGRELPPge 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 517 -GEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNC 595
Cdd:COG0318 295 vGEIVVRGPNVMKGYWNDPEATAE---AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAH 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 596 PLIDNICAFAKSDQSY---VISFVVPNqkrltllaqqkgvEGTWVDicnnpamEAEILKEIREaanamKLERFEIPIKVR 672
Cdd:COG0318 369 PGVAEAAVVGVPDEKWgerVVAFVVLR-------------PGAELD-------AEELRAFLRE-----RLARYKVPRRVE 423
|
570 580 590
....*....|....*....|....*....|..
gi 530422004 673 LSPE-PWTPeTGlvtdafKLKRKELRNHYLKD 703
Cdd:COG0318 424 FVDElPRTA-SG------KIDRRALRERYAAG 448
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
125-665 |
8.87e-61 |
|
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: 213.82 E-value: 8.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 125 WMNYLEvnrRVNNFGSGLTALGLKPKNTIAIFCETRAEW---MIAAQTCFKYNFPLvtlYATLGKEAVVHGLNESEASYL 201
Cdd:cd17641 14 WADYAD---RVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALSLGI---YQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPEgfeIHSMQSVEELG-----SNPENLGIPPSRPTPSDMAIVM 276
Cdd:cd17641 88 IAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPR---LISFEDVVALGraldrRDPGLYEREVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 277 YTSGSTGRPKGVMMHHSNLIaGMTGQCERIPGLGPKDTYIGYLPLAHVLELT-----AEISCFTYGCrigYSSPLTLsdq 351
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFL-GHCAAYLAADPLGPGDEYVSVLPLPWIGEQMysvgqALVCGFIVNF---PEEPETM--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 352 sskikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYD--YK-LEQIKKGYDAP--------LC 420
Cdd:cd17641 238 --------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKlgLRaLDRGKRGRPVSlwlrlaswLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 421 NLLLFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCE 496
Cdd:cd17641 310 DALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 497 IKLKDwqeggytindkpnpRGEIVIGGQNISMGYFKNEEKTAEDysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 576
Cdd:cd17641 386 VRIDE--------------VGEILVRSPGVFVGYYKNPEATAED--FDEDG--WLHTGDAGYFKENGHLVVIDRAKDVGT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 577 LQAGEYVSLGKVEAALKNCPLIDNICAFAKsDQSYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIRE 655
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAEAVVLGA-GRPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEK 526
|
570
....*....|....
gi 530422004 656 A----ANAMKLERF 665
Cdd:cd17641 527 VnaslPEAQRIRRF 540
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
121-700 |
2.04e-56 |
|
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: 200.39 E-value: 2.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 LITSvellesKLKtalldiscvkhiiyvDNKAInKAEYPEGFEIHSMQSVEELGSNPENLGI----PPS----RPTPSDM 272
Cdd:cd05932 82 LFVG------KLD---------------DWKAM-APGVPEGLISISLPPPSAANCQYQWDDLiaqhPPLeerpTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 273 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTA-EISCFTYGCRIGYSSPLTLSDQ 351
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 352 sskikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKV--QEMNyiqkTLFKIgydykleqikkgydaPLCNLLLFKKVK 429
Cdd:cd05932 219 ----------DVQRARPTLFFSVPRLWTKFQQGVQDKIpqQKLN----LLLKI---------------PVVNSLVKRKVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 430 ALLGGN-VRMMLSGGAPLSPQT-HRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggy 507
Cdd:cd05932 270 KGLGLDqCRLAGCGSAPVPPALlEWYRSLGL--NILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 508 tindkpnpRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGK 587
Cdd:cd05932 342 --------DGEILVRSPALMMGYYKDPEATAE--AFTADG--FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAP 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 588 VEAALKNCPLIDNICAFAkSDQSYVISFVVPNQK-RLTLLAQQKGvegtwvdicnnpAMEAEiLKEIREAANAmKLERFE 666
Cdd:cd05932 410 IENKLAEHDRVEMVCVIG-SGLPAPLALVVLSEEaRLRADAFARA------------ELEAS-LRAHLARVNS-TLDSHE 474
|
570 580 590
....*....|....*....|....*....|....
gi 530422004 667 IPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHY 700
Cdd:cd05932 475 QLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
271-620 |
4.20e-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: 186.34 E-value: 4.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI---GYSSPLT 347
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LSDqssKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQIK-KGYDAPlcnlllfk 426
Cdd:cd04433 80 ALE---LIER--------EKVTILLGVPTLLARL--------------------------LKAPEsAGYDLS-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 427 kvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwQE 504
Cdd:cd04433 115 --------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPVPGVEVRIVD-PD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 505 GGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVS 584
Cdd:cd04433 186 GGEL---PPGEIGELVVRGPSVMKGYWNNPEATAA---VDEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVY 256
|
330 340 350
....*....|....*....|....*....|....*....
gi 530422004 585 LGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 620
Cdd:cd04433 257 PAEVEAVLLGHPGVAEAAVVGVPDPEWgerVVAVVVLRP 295
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
126-608 |
1.20e-52 |
|
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: 189.35 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLEsKLKTALLDISCVKHIIYVDNKAiNKAEYPEgfeihsmQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:cd05911 91 DGLE-KVKEAAKELGPKDKIIVLDDKP-DGVLSIE-------DLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVleltaeiscftYGCRIGYSSPLtlsdqsskikkgsKGdCT 364
Cdd:cd05911 162 KGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHI-----------YGLFTTLASLL-------------NG-AT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 365 VLkptlmaavpeIMDRIYKNVMskvqeMNYIQKtlfkigydYKLEQIkkgYDAPLCNLLLFK---KVKALLGgNVRMMLS 441
Cdd:cd05911 217 VI----------IMPKFDSELF-----LDLIEK--------YKITFL---YLVPPIAAALAKsplLDKYDLS-SLRVILS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 442 GGAPLSPQTHRFMNVCFC-CPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGytiNDKPNPRGEIV 520
Cdd:cd05911 270 GGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKD---SLGPNEPGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 521 IGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDN 600
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKE--TFDEDG--WLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHPGVAD 421
|
....*...
gi 530422004 601 ICAFAKSD 608
Cdd:cd05911 422 AAVIGIPD 429
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
128-693 |
1.52e-51 |
|
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: 185.72 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSvel 207
Cdd:cd05914 10 YKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 lesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrpTPSDMAIVMYTSGSTGRPKG 287
Cdd:cd05914 87 ------------------------------------------------------------DEDDVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVLELtaeisCFTYGCRIGYSSPLTLSDQ--SSKIKKGSKGDctv 365
Cdd:cd05914 107 VMLTYRNIVSNVDG-VKEVVLLGKGDKILSILPLHHIYPL-----TFTLLLPLLNGAHVVFLDKipSAKIIALAFAQ--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LKPTLMAAVPEIMDRIYKNVmskVQEMNYIQKTLFKIGYDYKLEQIKKgydaplcnlLLFKKVKALLGGNVRMMLSGGAP 445
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMD---IIPKLTLKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 446 LSPQTHRF---MNVCFCcpigQGYGLTES----CGAGTVTEVTDyttgRVGAPLICCEIKLkdwqeggytinDKPNPR-- 516
Cdd:cd05914 246 INPDVEEFlrtIGFPYT----IGYGMTETapiiSYSPPNRIRLG----SAGKVIDGVEVRI-----------DSPDPAtg 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 517 -GEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNC 595
Cdd:cd05914 307 eGEIIVRGPNVMKGYYKNPEATAE--AFDKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNM 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 596 PLIdnicafaksdqsyVISFVVPNQKRLTLLA-------QQKGVegtwvdicNNPAMEAEILKEIREAANaMKLERFEIP 668
Cdd:cd05914 383 PFV-------------LESLVVVQEKKLVALAyidpdflDVKAL--------KQRNIIDAIKWEVRDKVN-QKVPNYKKI 440
|
570 580
....*....|....*....|....*
gi 530422004 669 IKVRLSPEPWtPETGLvtdaFKLKR 693
Cdd:cd05914 441 SKVKIVKEEF-EKTPK----GKIKR 460
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
78-596 |
6.51e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 185.39 E-value: 6.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 78 TLDKLFDHAVSKFGKKdslgtrEILSEEnemqpnGKVFkklilgnykwmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFC 157
Cdd:PRK06187 7 TIGRILRHGARKHPDK------EAVYFD------GRRT-----------TYAELDERVNRLANALRALGVKKGDRVAVFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 158 ETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESkLKTALLDISCVKHIIYVDNKAiNKAE 237
Cdd:PRK06187 64 WNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPL-LAAILPQLPTVRTVIVEGDGP-AAPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 238 YPEGFEIHSMqsveeLGSNPENLGIPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIG 317
Cdd:PRK06187 142 APEVGEYEEL-----LAAASDTFDFPD--IDENDAAAMLYTSGTTGHPKGVVLSHRNLFL-HSLAVCAWLKLSRDDVYLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 318 YLPLAHVLELTAEISCFTYGCRIGYS---SPLTLSDQsskIKKgskgdctvLKPTLMAAVPEIMdriyknvmskvqemNY 394
Cdd:PRK06187 214 IVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPTIW--------------QM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 395 IQKTLFKIGYDYkleqikkgydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCG 473
Cdd:PRK06187 269 LLKAPRAYFVDF---------------------------SSLRLVIYGGAALPPALlREFKEK-FGIDLVQGYGMTETSP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 474 AGTVTEVTDYTTGR------VGAPLICCEIKLKD--WQE---GGYTIndkpnprGEIVIGGQNISMGYFKNEEKTAEDYs 542
Cdd:PRK06187 321 VVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVDddGDElppDGGEV-------GEIIVRGPWLMQGYWNRPEATAETI- 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 530422004 543 vdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCP 596
Cdd:PRK06187 393 --DGG--WLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELEDALYGHP 441
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
121-708 |
2.09e-49 |
|
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: 182.94 E-value: 2.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKW--MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAA-QTCFKYNFpLVTLYATLGKEAVVHGLNESE 197
Cdd:cd05933 2 RGDKWhtLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAvGAIFAGGI-AVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 198 ASYLItsVE---------LLESKLKTalldiscVKHIIyvdnkainkaEYPEGFEIH-----SMQSVEELG-SNPEN-LG 261
Cdd:cd05933 81 ANILV--VEnqkqlqkilQIQDKLPH-------LKAII----------QYKEPLKEKepnlySWDEFMELGrSIPDEqLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL--IAGMTGQ-CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYG 337
Cdd:cd05933 142 AIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNItwTAKAASQhMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 338 CRIGYSSPLTLsdqsskikKGSKGDcTV--LKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLF----KIGYDYKLEQI 411
Cdd:cd05933 222 GQVYFAQPDAL--------KGTLVK-TLreVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 412 KKGYDAPLC----NLLLFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDY 483
Cdd:cd05933 293 GGESPSPLFyrlaKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 484 TTGRVGAPLICCEIKLkdwqeggytINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDG 563
Cdd:cd05933 369 RLLSCGKALPGCKTKI---------HNPDADGIGEICFWGRHVFMGYLNMEDKTEE--AIDEDG--WLHSGDLGKLDEDG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 564 CLQIIDRKKDLVKLQAGEYVSLGKVEAALKN-CPLIDNicAFAKSDQSYVISFVVP-----NQK------RLTLLA---- 627
Cdd:cd05933 436 FLYITGRIKELIITAGGENVPPVPIEDAVKKeLPIISN--AMLIGDKRKFLSMLLTlkcevNPEtgepldELTEEAiefc 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 628 QQKGVEGTWVDICNN---PAMEAEILKEIREA-----ANAMKLERFEIpikvrlSPEPWTPETGLVTDAFKLKRKELRNH 699
Cdd:cd05933 514 RKLGSQATRVSEIAGgkdPKVYEAIEEGIKRVnkkaiSNAQKIQKWVI------LEKDFSVPGGELGPTMKLKRPVVAKK 587
|
....*....
gi 530422004 700 YLKDIERMY 708
Cdd:cd05933 588 YKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
79-686 |
2.27e-49 |
|
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: 182.66 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 79 LDKLFDHAVSKFGKKDSLGTREilSEENEMQPNGKVFKKLiLGNYKWMNYLEVNRRVNNFGSGL-TALGLKPKNTIAIFC 157
Cdd:cd17632 24 LAQIIATVMTGYADRPALGQRA--TELVTDPATGRTTLRL-LPRFETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 158 ETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKtALLDISCVKHIIYVDNKA----- 232
Cdd:cd17632 101 FTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVE-AVLEGGTPPRLVVFDHRPevdah 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 233 --------INKAEYPEGFEIHSMQSVEELGSNPEnlgiPPSRPTPSDMAIVM--YTSGSTGRPKGVMMHHSNLIAGMTGQ 302
Cdd:cd17632 180 raalesarERLAAVGIPVTTLTLIAVRGRDLPPA----PLFRPEPDDDPLALliYTSGSTGTPKGAMYTERLVATFWLKV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 303 CERIPGLGPKDTYIGYLPLAHVLeltAEISCFTYGCRIGYSSPLTLSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIY 382
Cdd:cd17632 256 SSIQDIRPPASITLNFMPMSHIA---GRISLYGTLARGGTAYFAAASDMSTLFD-----DLALVRPTELFLVPRVCDMLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 383 KNVMSKVqemnyiqktlfkigyDYKLEQikkGYDAplcnLLLFKKVKA-----LLGGNVRMMLSGGAPLSPQTHRFMNVC 457
Cdd:cd17632 328 QRYQAEL---------------DRRSVA---GADA----ETLAERVKAelrerVLGGRLLAAVCGSAPLSAEMKAFMESL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 458 FCCPIGQGYGLTEscgAGTVT--------EVTDYttgrvgaplicceiKLKDWQEGGYTINDKPNPRGEIVIGGQNISMG 529
Cdd:cd17632 386 LDLDLHDGYGSTE---AGAVIldgvivrpPVLDY--------------KLVDVPELGYFRTDRPHPRGELLVKTDTLFPG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 530 YFKNEEKTAEDYsvDENGqrWFCTGDI-GEFHPDGcLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:cd17632 449 YYKRPEVTAEVF--DEDG--FYRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSE 523
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530422004 609 QSYVISFVVPNQKRLTLLAQQkgvegtwvdicnnpAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVT 686
Cdd:cd17632 524 RAYLLAVVVPTQDALAGEDTA--------------RLRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
124-575 |
1.72e-43 |
|
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: 163.50 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 124 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT 203
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 204 SVELlesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsvEELGSNPENLGIPPSRpTPSDMAIVMYTSGSTG 283
Cdd:cd05936 103 AVSF-------------------------------------------TDLLAAGAPLGERVAL-TPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 284 RPKGVMMHHSNLIAGMTgQCERI--PGLGPKDTYIGYLPLAHVLELTAeisCFTYGCRIGYS-------SPLTLSDQssk 354
Cdd:cd05936 139 VPKGAMLTHRNLVANAL-QIKAWleDLLEGDDVVLAALPLFHVFGLTV---ALLLPLALGATivliprfRPIGVLKE--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 355 IKKGskgdctvlKPTLMAAVPeimdriyknvmskvqemnyiqkTLFkIGydykleqikkgydaplcnLLLFKKVKALLGG 434
Cdd:cd05936 212 IRKH--------RVTIFPGVP----------------------TMY-IA------------------LLNAPEFKKRDFS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 435 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKDwqeggytINDKP 513
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-------DDGEE 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530422004 514 NPR---GEIVIGGQNISMGYFKNEEKTAEDYsVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:cd05936 316 LPPgevGELWVRGPQVMKGYWNRPEETAEAF-VDG----WLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
128-576 |
1.22e-40 |
|
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: 155.86 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEwmiaaqtcfkynFPLVTLYAT-LGkeAVVHGLN------------ 194
Cdd:cd05904 35 YAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIE------------FPVAFLAVLsLG--AVVTTANplstpaeiakqv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 195 -ESEASYLITSVELLEsKLKTALLDISCVkhiiyvdnkainkaeypEGFEIHSMQSVEELGSNPENlGIPPSRPTPSDMA 273
Cdd:cd05904 101 kDSGAKLAFTTAELAE-KLASLALPVVLL-----------------DSAEFDSLSFSDLLFEADEA-EPPVVVIKQDDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 274 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERI-PGLGPKDTYIGYLPLAHVLELTaeiSCFTYGCRIG--------YSS 344
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLS---SFALGLLRLGatvvvmprFDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 345 PLTLSdqssKIKKgskgdctvLKPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigydykleqikkGYDaplcnlll 424
Cdd:cd05904 239 EELLA----AIER--------YKVTHLPVVPPIVLALVKSPIVD-------------------------KYD-------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 fkkVKALlggnvRMMLSGGAPLSPQT-----HRFMNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVG-----APLIc 494
Cdd:cd05904 274 ---LSSL-----RQIMSGAAPLGKELieafrAKFPNV----DLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNV- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 495 cEIKLKDWQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDL 574
Cdd:cd05904 341 -EAKIVDPETGESL---PPNQTGELWIRGPSIMKGYLNNPEATAA--TIDKEG--WLHTGDLCYIDEDGYLFIVDRLKEL 412
|
..
gi 530422004 575 VK 576
Cdd:cd05904 413 IK 414
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
269-583 |
1.63e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 156.03 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCER--IPGLGPKdTYIGYLPLAHVLELTAEISCFTYGCRIgysspl 346
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsiFKKYNPK-THLSYLPISHIYERVIAYLSFMLGGTI------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 347 tlsDQSSK-IKKGSKgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKigydyKLEQIKKG-YDAPLCNLL- 423
Cdd:PTZ00342 376 ---NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVK-----KILSLRKSnNNGGFSKFLe 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 424 ----LFKKVKALLGGNVRMMLSGGAPLSPQTHR----FMNVCFCcpigQGYGLTESCGAGTVTEVTDYTTGRVGAPlIC- 494
Cdd:PTZ00342 447 githISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYGLTETTGPIFVQHADDNNTESIGGP-ISp 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 495 -CEIKLKDWQEggYTINDKPnPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PTZ00342 522 nTKYKVRTWET--YKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTED----GYFKTGDIVQINKNGSLTFLDRSKG 594
|
330
....*....|
gi 530422004 574 LVKLQAGEYV 583
Cdd:PTZ00342 595 LVKLSQGEYI 604
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
121-698 |
3.42e-38 |
|
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: 148.61 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAaqtcfkynfplvtLYATLGKEAVVHGLNeseASY 200
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVA-------------FLAAARAGAVVAPLN---PAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 LITSVELLESKLKTALL------DISCVKHIIYVDNKAINKAEypEGFEIHSMQSVEELGsNPENLGI---PPSRPTPSD 271
Cdd:cd05926 74 KKAEFEFYLADLGSKLVltpkgeLGPASRAASKLGLAILELAL--DVGVLIRAPSAESLS-NLLADKKnakSEGVPLPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 272 MAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEI--SCFTYGCrigysspLTLS 349
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNIT-NTYKLTPDDRTLVVMPLFHVHGLVASLlsTLAAGGS-------VVLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 350 DQSSkikkGSK--GDCTVLKPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigydykleqikkgydaplcnlllFKK 427
Cdd:cd05926 223 PRFS----ASTfwPDVRDYNATWYTAVPTIHQILLNRPEPN------------------------------------PES 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 428 VKALLggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLiccEIKLKDWQEG 505
Cdd:cd05926 263 PPPKL----RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPV---GVEVRILDED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 506 GYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSL 585
Cdd:cd05926 336 GEIL--PPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD----GWFRTGDLGYLDADGYLFLTGRIKELIN-RGGEKISP 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 586 GKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNqkrltllaqqkgvEGTWVDicnnpamEAEILKEIREaanamKL 662
Cdd:cd05926 409 LEVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLR-------------EGASVT-------EEELRAFCRK-----HL 463
|
570 580 590
....*....|....*....|....*....|....*..
gi 530422004 663 ERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRN 698
Cdd:cd05926 464 AAFKVPKKVYFVDElPKTA-TG------KIQRRKVAE 493
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
118-617 |
5.19e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 139.33 E-value: 5.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 118 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplvtlyatLGKEAVvhglnese 197
Cdd:PRK03640 21 IEFEEKKV-TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQ-----------LGAVAV-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 198 asylitsveLLESKLKTA----LLDISCVKHIIYVDnkainkaEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTPSDMA 273
Cdd:PRK03640 81 ---------LLNTRLSREellwQLDDAEVKCLITDD-------DFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 274 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLSDQ-- 351
Cdd:PRK03640 145 TIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNL-GLTEDDCWLAAVPIFHISGLSILMRSVIYGMRV------VLVEKfd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 352 SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvMSKVQEMNYiqktlfkigydykleqikkgydaplcnlllfkkvkal 431
Cdd:PRK03640 218 AEKINKLLQTG----GVTIISVVSTMLQRL----LERLGEGTY------------------------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 432 lGGNVRMMLSGGAPLSPQT------HRFmnvcfccPIGQGYGLTESCgAGTVTEVTDYTT---GRVGAPLICCEIKL-KD 501
Cdd:PRK03640 253 -PSSFRCMLLGGGPAPKPLleqckeKGI-------PVYQSYGMTETA-SQIVTLSPEDALtklGSAGKPLFPCELKIeKD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 502 WQEGgytindKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 581
Cdd:PRK03640 324 GVVV------PPFEEGEIVVKGPNVTKGYLNREDATRE---TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGE 391
|
490 500 510
....*....|....*....|....*....|....*....
gi 530422004 582 YVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 617
Cdd:PRK03640 392 NIYPAEIEEVLLSHPGVAEAGVVGVPDDKWgqvPVAFVV 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
126-575 |
1.52e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 135.42 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGKEAVVHGLNE----SEASY- 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAA-------------LGALKAGAVVVPLNTrytaDEAAYi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 -------LITSVELLESKLKTALLDISCVKHIIYVdnkAINKAEyPEGFEIHSMQSVEELGSNPENlgiPPSRpTPSDMA 273
Cdd:PRK07656 98 largdakALFVLGLFLGVDYSATTRLPALEHVVIC---ETEEDD-PHTEKMKTFTDFLAAGDPAER---APEV-DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 274 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGcrigysspltlsdqs 352
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKAGVnAPLMRG--------------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 353 skikkgskgdCTVLkPTLMAAVPEIMDRIYK---NVMSKVQEMnyiqktlfkigYDYkleqikkgydaplcnLLLFKKVK 429
Cdd:PRK07656 234 ----------ATIL-PLPVFDPDEVFRLIETeriTVLPGPPTM-----------YNS---------------LLQHPDRS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 430 ALLGGNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD---YTTGRVGAPLICCEIKLKDWQEG 505
Cdd:PRK07656 277 AEDLSSLRLAVTGAASMPVAlLERFESELGVDIVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVNELGE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 506 GYTINDKpnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK07656 357 EVPVGEV----GELLVRGPNVMKGYYDDPEATAA--AIDADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
128-618 |
3.30e-33 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 132.89 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsvel 207
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 lesklktalldiscvkhiiyvdnkainkaeyPEGFEIHSMQsveelgsnpenlgippsrPTPSDMAIVMYTSGSTGRPKG 287
Cdd:cd05903 80 -------------------------------PERFRQFDPA------------------AMPDAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaeISCFTYGcrigysspltlsdqsskikkgskgdctVLK 367
Cdd:cd05903 111 VMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAH-------QTGFVYG---------------------------FTL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 368 PTLMAAvPEIMDRIYkNVMSKVQEMNYiQKTLFKIGYDYKLEQIKKGYD---APLCNLllfkkvkallggnvRMMLSGGA 444
Cdd:cd05903 156 PLLLGA-PVVLQDIW-DPDKALALMRE-HGVTFMMGATPFLTDLLNAVEeagEPLSRL--------------RTFVCGGA 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 445 PLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD-----YTTGRVGAPLiccEIKLKDwqEGGYTIndKPNPRGEI 519
Cdd:cd05903 219 TVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrlYTDGRPLPGV---EIKVVD--DTGATL--APGVEGEL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 520 VIGGQNISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLID 599
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAAP-----EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVI 365
|
490 500
....*....|....*....|..
gi 530422004 600 NICAFAKSDQ---SYVISFVVP 618
Cdd:cd05903 366 EAAVVALPDErlgERACAVVVT 387
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
126-592 |
3.21e-31 |
|
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: 126.96 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEAsylitsv 205
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGA------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ellesklkTALLDiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpsDMAIVMYTSGSTGRP 285
Cdd:cd17631 94 --------KVLFD----------------------------------------------------DLALLMYTSGTTGRP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNL-----IAGMTGqceripGLGPKDTYIGYLPLAHVleltAEISCFTygcrigysSPLTLSDQSSKIKKGSK 360
Cdd:cd17631 114 KGAMLTHRNLlwnavNALAAL------DLGPDDVLLVVAPLFHI----GGLGVFT--------LPTLLRGGTVVILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 361 GDcTVL------KPTLMAAVPEIMDRIyknvmskvqemnyIQKTLFKigydykleqikkGYDAPlcnlllfkkvkallgg 434
Cdd:cd17631 176 PE-TVLdlierhRVTSFFLVPTMIQAL-------------LQHPRFA------------TTDLS---------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 435 NVRMMLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTT--GRVGAPLICCEIKLKDwqEGGYTIndK 512
Cdd:cd17631 214 SLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD--PDGREV--P 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 513 PNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 592
Cdd:cd17631 289 PGEVGEIVVRGPHVMAGYWNRPEATAAAF---RDG--WFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVL 362
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
126-608 |
2.08e-30 |
|
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: 126.05 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIA------AQTCFKYNFPLvtlyatLGKEAVVHGLNESEAS 199
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAmfgaalAGGVFVPINPL------LKAEQVAHILADCNVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 200 YLITSVELLEsKLKTALLDISCVKHIIYVDNKAiNKAEYPEGFEIHSMQSVEELGSnpenlGIPPSRPTPSDMAIVMYTS 279
Cdd:TIGR03098 100 LLVTSSERLD-LLHPALPGCHDLRTLIIVGDPA-HASEGHPGEEPASWPKLLALGD-----ADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 280 GSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGs 359
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATYLE-NRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDVLKALEKH- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 360 kgdctvlKPTLMAAVPEImdriyknvmskvqemnYIQktLFKIgyDYKLEqikkgyDAPLCNLLlfkkvkALLGGNV-RM 438
Cdd:TIGR03098 251 -------GITGLAAVPPL----------------WAQ--LAQL--DWPES------AAPSLRYL------TNSGGAMpRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 439 MLSGGAPLSPQTHRFMNvcfccpigqgYGLTESCGAGTV-TEVTDYTTGRVGAPLICCEIklkdwqeggYTINDK----- 512
Cdd:TIGR03098 292 TLSRLRSFLPNARLFLM----------YGLTEAFRSTYLpPEEVDRRPDSIGKAIPNAEV---------LVLREDgseca 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 513 PNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQR---------WfcTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYV 583
Cdd:TIGR03098 353 PGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGelhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIK-TSGYRV 429
|
490 500
....*....|....*....|....*
gi 530422004 584 SLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:TIGR03098 430 SPTEVEEVAYATGLVAEAVAFGVPD 454
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
270-621 |
3.33e-29 |
|
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: 120.53 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLS 349
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNL-GLTEDDNWLCALPLFHISGLSILMRSVIYGMTV------YLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 350 DQ--SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQIKKGYDAplcnlllfkk 427
Cdd:cd05912 150 DKfdAEQVLHLINSG----KVTIISVVPTMLQRL--------------------------LEILGEGYPN---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 428 vkallggNVRMMLSGGAPLSPQThrfMNVC--FCCPIGQGYGLTESCgAGTVTEVTDYT---TGRVGAPLICCEIKLKDw 502
Cdd:cd05912 190 -------NLRCILLGGGPAPKPL---LEQCkeKGIPVYQSYGMTETC-SQIVTLSPEDAlnkIGSAGKPLFPVELKIED- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 503 qeggytINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEY 582
Cdd:cd05912 258 ------DGQPPYEVGEILLKGPNVTKGYLNRPDATEE---SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGEN 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530422004 583 VSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQK 621
Cdd:cd05912 326 IYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvPVAFVVSERP 367
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
183-610 |
3.97e-28 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 118.59 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 183 TLGKEAVVHGLNESEASYLITSVELLEsKLK-TALLDISCVKHIIYVDN--KAINKAEYPEGFeIHSMQSVEELgsnpen 259
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQFIE-KLKlHHLFDVEYDARIVYLEDlrAKISKADKCKAF-LAGKFPPKWL------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 260 LGIPPSRPT-PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELT-AEISCFTYG 337
Cdd:cd05909 136 LRIFGVAPVqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 338 CRIG-YSSPLTLSDQSSKIKKGSkgdCTVL--KPTLMaavpeimdRIYknvmskvqeMNYIQKTLFKigydykleqikkg 414
Cdd:cd05909 215 IKVVfHPNPLDYKKIPELIYDKK---ATILlgTPTFL--------RGY---------ARAAHPEDFS------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 415 ydaplcnlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV-TEVTDYTTGRVGAPLI 493
Cdd:cd05909 262 --------------------SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 494 CCEIKLKDwQEGGytindKPNPRGE---IVIGGQNISMGYFKNEEKTAEDYsvdenGQRWFCTGDIGEFHPDGCLQIIDR 570
Cdd:cd05909 322 GMEVKIVS-VETH-----EEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF-----GDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 530422004 571 KKDLVKLqAGEYVSLGKVE-AALKNCPLIDNICAFAKSDQS 610
Cdd:cd05909 391 LSRFAKI-AGEMVSLEAIEdILSEILPEDNEVAVVSVPDGR 430
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
128-701 |
2.05e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 117.52 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 207
Cdd:COG0365 42 YAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 LE--------SKLKTALLDISCVKHIIYVDNKAiNKAEYPEGFEIHsmqsvEELGSNPENLgipPSRPTPS-DMAIVMYT 278
Cdd:COG0365 122 LRggkvidlkEKVDEALEELPSLEHVIVVGRTG-ADVPMEGDLDWD-----ELLAAASAEF---EPEPTDAdDPLFILYT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 279 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY-----IG---------YLPLAHvleltaEISCFTYGCRIGYSS 344
Cdd:COG0365 193 SGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFwctadIGwatghsyivYGPLLN------GATVVLYEGRPDFPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 345 PLTLSDQSSKikkgskgdctvLKPTLMAAVPeimdRIYKNVMskvqemnyiqktlfKIGydyklEQIKKGYDapLCNLll 424
Cdd:COG0365 267 PGRLWELIEK-----------YGVTVFFTAP----TAIRALM--------------KAG-----DEPLKKYD--LSSL-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 fkkvkallggnvRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGA-GTVTEVTDYTTGRVGAPLICCEIKLkdW 502
Cdd:COG0365 309 ------------RLLGSAGEPLNPEVwEWWYEA-VGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAV--V 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 503 QEGGYTIndKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAG 580
Cdd:COG0365 374 DEDGNPV--PPGEEGELVIKGPWPGMfrGYWNDPERYRETYFGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINV-SG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 581 EYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNqkrltllaqqKGVEGTwvdicnnPAMEAEILKEIREaa 657
Cdd:COG0365 449 HRIGTAEIESALVSHPAVAEAAVVGVPDEirgQVVKAFVVLK----------PGVEPS-------DELAKELQAHVRE-- 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 530422004 658 namKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHYL 701
Cdd:COG0365 510 ---ELGPYAYPREIEFVDElPKTR-SG------KIMRRLLRKIAE 544
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-598 |
2.51e-27 |
|
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: 116.86 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 122 NYKWMNYLEVNRRVnnfGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL 201
Cdd:cd17642 44 NYSYAEYLEMSVRL---AEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ITS------VELLESKLKTalldiscVKHIIYVDNKainkaeypegFEIHSMQSVEELGSNPENLG------IPPSRPTP 269
Cdd:cd17642 121 FCSkkglqkVLNVQKKLKI-------IKTIIILDSK----------EDYKGYQCLYTFITQNLPPGfneydfKPPSFDRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPG--LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGY----S 343
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykfE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 344 SPLTLSD-QSSKIKKgskgdcTVLKPTLMAAVPeimdriyknvmskvqemnyiqktlfkigydyKLEQIKKgYDapLCNL 422
Cdd:cd17642 264 EELFLRSlQDYKVQS------ALLVPTLFAFFA-------------------------------KSTLVDK-YD--LSNL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 423 LlfkkvkallggnvrMMLSGGAPLSPQTHRFMNVCFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 501
Cdd:cd17642 304 H--------------EIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 502 wQEGGYTINdkPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGE 581
Cdd:cd17642 370 -LDTGKTLG--PNERGELCVKGPMIMKGYVNNPEATKA--LIDKDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GY 441
|
490
....*....|....*..
gi 530422004 582 YVSLGKVEAALKNCPLI 598
Cdd:cd17642 442 QVPPAELESILLQHPKI 458
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
261-600 |
4.35e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 116.64 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 261 GIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA-GMTGQCeRIPGLGPKD-TYIGYLPLAHVLELTAeisCFTYGC 338
Cdd:PRK05605 210 DVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKA-WVPGLGDGPeRVLAALPMFHAYGLTL---CLTLAV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 339 RIG--------YSSPLTLsdqsSKIKKGskgdctvlKPTLMAAVPEimdrIYKNVMSKVQEmnyiqktlfkigydykleq 410
Cdd:PRK05605 286 SIGgelvllpaPDIDLIL----DAMKKH--------PPTWLPGVPP----LYEKIAEAAEE------------------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 411 ikKGYDaplcnlllfkkvkalLGGnVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY-TTGRVG 489
Cdd:PRK05605 331 --RGVD---------------LSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDrRPGYVG 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 490 APLICCEIKLKDWQEGGYTINDkpNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIID 569
Cdd:PRK05605 393 VPFPDTEVRIVDPEDPDETMPD--GEEGELLVRGPQVFKGYWNRPEETAK---SFLDG--WFRTGDVVVMEEDGFIRIVD 465
|
330 340 350
....*....|....*....|....*....|.
gi 530422004 570 RKKDLVkLQAGEYVSLGKVEAALKNCPLIDN 600
Cdd:PRK05605 466 RIKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
128-603 |
1.16e-26 |
|
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: 113.13 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGL-TALGLKPKNTIAIFCEtRAEWMIAAQ-TCFK----YnFPLVTLYATLGKEAVvhgLNESEASYL 201
Cdd:TIGR01733 2 YRELDERANRLARHLrAAGGVGPGDRVAVLLE-RSAELVVAIlAVLKagaaY-VPLDPAYPAERLAFI---LEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ITSVELLESKLKTALLDISCVkhiiyvdnkainkaeypegfeihsmqSVEELGSNPENLGIPP-SRPTPSDMAIVMYTSG 280
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLD--------------------------PLELAALDDAPAPPPPdAPSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 281 STGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAH---VLELTAeiscftygcrigyssPLTLsdqsskikk 357
Cdd:TIGR01733 131 STGRPKGVVVTHRSLVN-LLAWLARRYGLDPDDRVLQFASLSFdasVEEIFG---------------ALLA--------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 358 gskGDCTVLKPtlmaAVPEIMDRIYKNVMSKVQEMNYIQKTlfkigydykleqikkgydAPLCNLLLFKKVKALLGgnVR 437
Cdd:TIGR01733 186 ---GATLVVPP----EDEERDDAALLAALIAEHPVTVLNLT------------------PSLLALLAAALPPALAS--LR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 438 MMLSGGAPLSPQTH-RFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIklkdwqeggYTIND 511
Cdd:TIGR01733 239 LVILGGEALTPALVdRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRL---------YVLDD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 512 --KPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEY 582
Cdd:TIGR01733 310 dlRPVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYR 388
|
490 500
....*....|....*....|.
gi 530422004 583 VSLGKVEAALKNCPLIDNICA 603
Cdd:TIGR01733 389 IELGEIEAALLRHPGVREAVV 409
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-609 |
1.54e-26 |
|
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: 112.77 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIgysspl 346
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRF-GLGEDDVYLTVLPLFHinaqAVSVLAALSV---GATL------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 347 tlsdqsskikkgskgdctVLKPTLMAAvpeimdriykNVMSKVQE-----MNYIQKTLfkigyDYKLEQIKKGYDAplcn 421
Cdd:cd05934 152 ------------------VLLPRFSAS----------RFWSDVRRygatvTNYLGAML-----SYLLAQPPSPDDR---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 422 lllfkkvkallGGNVRmmLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 501
Cdd:cd05934 195 -----------AHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 502 wqeggytINDKPNPR---GEIVI---GGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:cd05934 262 -------DDGQELPAgepGELVIrglRGWGFFKGYYNMPEATAE---AMRNG--WFHTGDLGYRDADGFFYFVDRKKDMI 329
|
330 340 350
....*....|....*....|....*....|....
gi 530422004 576 KlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:cd05934 330 R-RRGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
128-629 |
1.92e-26 |
|
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: 116.11 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCEtRAEWMIAAqtcfkynfplvtLYATL--G-----------KEAVVHGLN 194
Cdd:COG1020 504 YAELNARANRLAHHLRALGVGPGDLVGVCLE-RSLEMVVA------------LLAVLkaGaayvpldpaypAERLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 195 ESEASYLITsvellESKLKTALLDISCvkHIIYVDNKAInkAEYPEGFeihsmqsveelgsnpenlgiPPSRPTPSDMAI 274
Cdd:COG1020 571 DAGARLVLT-----QSALAARLPELGV--PVLALDALAL--AAEPATN--------------------PPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 275 VMYTSGSTGRPKGVMMHH---SNLIAGMTGQCeripGLGPKDTYIGYLPLAH---VLELtaeISCFTYGCRIGYSSPLTL 348
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHralVNLLAWMQRRY----GLGPGDRVLQFASLSFdasVWEI---FGALLSGATLVLAPPEAR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 349 SD--------QSSKIkkgskgdcTVLK--PTLMAAVPeimdriyknvmskvqemnyiqktlfkigydykleqikkgyDAP 418
Cdd:COG1020 695 RDpaalaellARHRV--------TVLNltPSLLRALL----------------------------------------DAA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 419 LCNLLlfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPL- 492
Cdd:COG1020 727 PEALP-----------SLRLVLVGGEALPPELvRRWRARLPGARLVNLYGPTETTVDSTYYEVTppDADGGSVpiGRPIa 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 493 -ICCEIkLKDWQEggytindkPNP---RGEIVIGGQNISMGYFKNEEKTAE---DYSVDENGQRWFCTGDIGEFHPDGCL 565
Cdd:COG1020 796 nTRVYV-LDAHLQ--------PVPvgvPGELYIGGAGLARGYLNRPELTAErfvADPFGFPGARLYRTGDLARWLPDGNL 866
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530422004 566 QIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKRLTLLAQQ 629
Cdd:COG1020 867 EFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAREDAPgdkRLVAYVVPEAGAAAAAALL 932
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
271-676 |
3.50e-26 |
|
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: 112.00 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIP---GLGPKDTYIGYLPLAHVLELTAEISCFTYgCRigySSPLT 347
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAA----NVRALVdawRWTEDDVLLHVLPLHHVHGLVNALLCPLF-AG---ASVEF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LSDQSSKIKKGSKGDCTVlkpTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKigydykleqikkgydaplcnlllfkk 427
Cdd:cd05941 162 LPKFDPKEVAISRLMPSI---TVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAE-------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 428 vkallggNVRMMLSGGAPLSPQTHRFmnvcFCCPIGQG----YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQ 503
Cdd:cd05941 213 -------RLRLMVSGSAALPVPTLEE----WEAITGHTllerYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVD-E 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 504 EGGytindKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 580
Cdd:cd05941 281 ETG-----EPLPRgevGEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGVVDEDGYYWILGRSSVDIIKSGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 581 EYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqQKGVegtwvdicnnPAMEAEILKEireaA 657
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVL----------RAGA----------AALSLEELKE----W 407
|
410
....*....|....*....
gi 530422004 658 NAMKLERFEIPIKVRLSPE 676
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDE 426
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
127-596 |
3.98e-26 |
|
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: 113.11 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 127 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCetraeWmiaaqTCFKYnfpLVTLYATLGKEAVVHGLN------------ 194
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLA-----W-----NTHRH---LELYYAVPGMGAVLHTINprlfpeqiayii 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 195 -ESEASYLITSVELLesKLKTALLD-ISCVKHIIYVDNKAINKAEYPEG---FE--IHSMQSVEELGSNPENlgippsrp 267
Cdd:cd12119 94 nHAEDRVVFVDRDFL--PLLEAIAPrLPTVEHVVVMTDDAAMPEPAGVGvlaYEelLAAESPEYDWPDFDEN-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 tpsDMAIVMYTSGSTGRPKGVMM-HHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPL 346
Cdd:cd12119 164 ---TAAAICYTSGTTGNPKGVVYsHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 347 TLSDQSSKIKKGSKgdctvlkPTLMAAVPEImdriYKNVMSKVQemnyiqktlfkigydykleqiKKGYDaplcnllLFK 426
Cdd:cd12119 241 LDPASLAELIEREG-------VTFAAGVPTV----WQGLLDHLE---------------------ANGRD-------LSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 427 kvkallggnVRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTESCGAGTVTEVTDY--------------TTGRVg 489
Cdd:cd12119 282 ---------LRRVVIGGSAVPRsliEAFEERGV----RVIHAWGMTETSPLGTVARPPSEhsnlsedeqlalraKQGRP- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 490 APLIccEIKLKDwqEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIID 569
Cdd:cd12119 348 VPGV--ELRIVD--DDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEA---LTEDG--WLRTGDVATIDEDGYLTITD 418
|
490 500
....*....|....*....|....*..
gi 530422004 570 RKKDLVKlQAGEYVSLGKVEAALKNCP 596
Cdd:cd12119 419 RSKDVIK-SGGEWISSVELENAIMAHP 444
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
268-629 |
4.01e-26 |
|
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: 111.96 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPkdtyigylplahvleltaeiscftyGCRIGYSSPLT 347
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGP-------------------------GDVFLNQAPFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LsdqsskikkgskgDCTV--LKPTLMA-----AVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykleQIKKGYDAP-- 418
Cdd:cd05945 149 F-------------DLSVmdLYPALASgatlvPVPRDATADPKQLFRFLAEH-----------------GITVWVSTPsf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 419 --LCnlLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVT-----DYTTGRVGA 490
Cdd:cd05945 199 aaMC--LLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTpevldGYDRLPIGY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 491 PLICCEIKLKDwqEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDEnGQRWFCTGDIGEFHPDGCLQIIDR 570
Cdd:cd05945 277 AKPGAKLVILD--EDGRPV--PPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-GQRAYRTGDLVRLEADGLLFYRGR 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 571 KKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP----NQKRLTLLAQQ 629
Cdd:cd05945 352 LDFQVKLN-GYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVtelIAFVVPkpgaEAGLTKAIKAE 416
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
128-619 |
2.64e-25 |
|
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: 110.11 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsvel 207
Cdd:cd17655 25 YRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 lESKLKTALLDIscvKHIIYVDNKAInkAEYPEgfeihsmqsveelgsnpENLGiPPSRPtpSDMAIVMYTSGSTGRPKG 287
Cdd:cd17655 101 -QSHLQPPIAFI---GLIDLLDEDTI--YHEES-----------------ENLE-PVSKS--DDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTLSDQSSKIKKGSKGDCTVLk 367
Cdd:cd17655 155 VMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIS--FDASVT-EIFA---------SLLSGNTLYIVRKETVLDGQAL- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 368 ptlmaavpeimdriyknvmskvqeMNYIQKtlfkigydYKLEQIkkgyDAPLCNLLLFKKVKALLGGNVRMMLSGGAPLS 447
Cdd:cd17655 221 ------------------------TQYIRQ--------NRITII----DLTPAHLKLLDAADDSEGLSLKHLIVGGEALS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 448 PQT-----HRFMNvcfCCPIGQGYGLTESC-GAGT-VTEVTDYTTGRV--GAPLICCEIKLKDwQEGgytindKPNP--- 515
Cdd:cd17655 265 TELakkiiELFGT---NPTITNAYGPTETTvDASIyQYEPETDQQVSVpiGKPLGNTRIYILD-QYG------RPQPvgv 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 516 RGEIVIGGQNISMGYFKNEEKTAEDYSVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALK 593
Cdd:cd17655 335 AGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR-GYRIELGEIEARLL 413
|
490 500
....*....|....*....|....*....
gi 530422004 594 NCPLIDNICAFAKSDQS---YVISFVVPN 619
Cdd:cd17655 414 QHPDIKEAVVIARKDEQgqnYLCAYIVSE 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
268-620 |
1.01e-24 |
|
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: 107.61 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI------G 341
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLvvlpeeV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 342 YSSPLTLSD--QSSKIkkgskgdcTVLK--PTLMAAVpeimdriyknvmskvqeMNYIQKTLFKigydykleqikkgyda 417
Cdd:cd05930 170 RKDPEALADllAEEGI--------TVLHltPSLLRLL-----------------LQELELAALP---------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 418 plcnlllfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPL 492
Cdd:cd05930 209 -----------------SLRLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATYYRVPpdDEEDGRVpiGRPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 493 ICCEIKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQI 567
Cdd:cd05930 272 PNTRVYVLD-------ENLRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPNpfGPGERMYRTGDLVRWLPDGNLEF 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 568 IDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 620
Cdd:cd05930 345 LGRIDDQVKI-RGYRIELGEIEAALLAHPGVREAAVVAREDgdgEKRLVAYVVPDE 399
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
126-609 |
3.20e-24 |
|
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: 106.02 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELlesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpSDMAIVMYTSGSTGRP 285
Cdd:cd05935 82 EL--------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCriGYSSPLTLSDQSSKIKKGSKGDCTV 365
Cdd:cd05935 100 KGCMHTHFSAAANALQSA-VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG--GTYVLMARWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LkptlMAAVPEIMDriyknVMSKVQEMNYIQKTLfkigydykleqikkgydaplcnlllfkkvkallggnvRMMLSGGAP 445
Cdd:cd05935 177 W----TNIPTMLVD-----LLATPEFKTRDLSSL-------------------------------------KVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 446 LSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGgytINDKPNPRGEIVIGGQN 525
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETG---RELPPNEVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 526 ISMGYFKNEEKTAEDYSVDeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFA 605
Cdd:cd05935 288 IFKGYWNRPEETEESFIEI-KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
....
gi 530422004 606 KSDQ 609
Cdd:cd05935 366 VPDE 369
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
264-575 |
7.35e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.39 E-value: 7.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 264 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPG--LGP-KDTYIGYLPLAHvleltaeISCFTYGCRI 340
Cdd:PRK05677 201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANML-QCRALMGsnLNEgCEILIAPLPLYH-------IYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 341 gysspLTLSdqsskikkgskGDCTVLKPTlmaavPEIMDRIYKnVMSKVQEMNYIQ-KTLFkigydykleqikkgydAPL 419
Cdd:PRK05677 273 -----MMLI-----------GNHNILISN-----PRDLPAMVK-ELGKWKFSGFVGlNTLF----------------VAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 420 CNLLLFKKV--KALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEI 497
Cdd:PRK05677 315 CNNEAFRKLdfSAL-----KLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLC 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530422004 498 KLKDwQEGgytiNDKP-NPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK05677 390 KVID-DDG----NELPlGEVGELCVKGPQVMKGYWQRPEATDE--ILDSDG--WLKTGDIALIQEDGYMRIVDRKKDMI 459
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
271-700 |
1.27e-23 |
|
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: 102.41 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysSPLTLSD 350
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVGGLAILVRSLLAG------AELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 351 QSSKIKKgskgDCTVLKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEqikkgYDAPLCNLLLFKKVka 430
Cdd:cd17630 74 RNQALAE----DLAPPGVTHVSLVPTQLQRL--------------------------LD-----SGQGPAALKSLRAV-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 431 llggnvrmmLSGGAPLSPQ-THRFMnvCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggyti 509
Cdd:cd17630 117 ---------LLGGAPIPPElLERAA--DRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 510 ndkpnpRGEIVIGGQNISMGYFKNEEKTAedysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVE 589
Cdd:cd17630 178 ------DGEIWVGGASLAMGYLRGQLVPE----FNEDG--WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 590 AALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqqkgvegtwvdicNNPAMEAEILKEIREaanamKLERFE 666
Cdd:cd17630 245 AALAAHPAVRDAFVVGVPDEELgqrPVAVIVG----------------------RGPADPAELRAWLKD-----KLARFK 297
|
410 420 430
....*....|....*....|....*....|....
gi 530422004 667 IPIkvRLSPEPWTPETGLVtdafKLKRKELRNHY 700
Cdd:cd17630 298 LPK--RIYPVPELPRTGGG----KVDRRALRAWL 325
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
128-625 |
1.02e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 102.52 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVel 207
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPT-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 LESKLKTALLDISCV------KHIIYVDNKAinkaeyPEgfeiHSMQSVEELGSNPENLGIPPsrPTPSD-MAIVMYTSG 280
Cdd:PRK06087 130 LFKQTRPVDLILPLQnqlpqlQQIVGVDKLA------PA----TSSLSLSQIIADYEPLTTAI--TTHGDeLAAVLFTSG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 281 STGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRigySSPLTLSDQSSKIKKGS 359
Cdd:PRK06087 198 TEGLPKGVMLTHNNILASERAYCARL-NLTWQDVFMMPAPLGHATGfLHGVTAPFLIGAR---SVLLDIFTPDACLALLE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 360 KGDCTvlkpTLMAAVPEIMDriyknvmskvqemnyIQKTLFKIGYDykleqikkgydaplcnlllfkkVKALlggnvRMM 439
Cdd:PRK06087 274 QQRCT----CMLGATPFIYD---------------LLNLLEKQPAD----------------------LSAL-----RFF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 440 LSGGAP----LSPQTHRFmNVCFCcpigQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDWqeggytiNDKP 513
Cdd:PRK06087 308 LCGGTTipkkVARECQQR-GIKLL----SVYGSTESSPHAVVNldDPLSRFMHTDGYAAAGVEIKVVDE-------ARKT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 514 NPRG---EIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEA 590
Cdd:PRK06087 376 LPPGcegEEASRGPNVFMGYLDEPELTAR--ALDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVED 450
|
490 500 510
....*....|....*....|....*....|....*...
gi 530422004 591 ALKNCPLIDNICAFAKSDQSY---VISFVVPNQKRLTL 625
Cdd:PRK06087 451 ILLQHPKIHDACVVAMPDERLgerSCAYVVLKAPHHSL 488
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
126-620 |
1.76e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.05 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK----YNfPLVTLYAtlgKEAVVHGLNESEASYL 201
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRigavLN-PLMPIFR---ERELSFMLKHAESKVL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 IT-------SVELLESKLKTALLDIscvKHIIYVDnkainkAEYPEGFEIHSMQSVEELGSNPENLgIPPSRPTPSDMAI 274
Cdd:PRK13295 132 VVpktfrgfDHAAMARRLRPELPAL---RHVVVVG------GDGADSFEALLITPAWEQEPDAPAI-LARLRPGPDDVTQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 275 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleLTAeiscFTYGCRIgyssPLTLsdqssk 354
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASPMAH---QTG----FMYGLMM----PVML------ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 355 ikkgskGDCTVLK----PTL-------------MAAVPEIMDriyknvMSKVQEMNyiqktlfkigydykleqikkGYDA 417
Cdd:PRK13295 264 ------GATAVLQdiwdPARaaelirtegvtftMASTPFLTD------LTRAVKES--------------------GRPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 418 PlcnlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEsCGAGTVT------EVTDYTTGRvgaP 491
Cdd:PRK13295 312 S----------------SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE-NGAVTLTklddpdERASTTDGC---P 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 492 LICCEIKLKDwqeggytINDKPNPRGEI---VIGGQNISMGYFKNEEKTAEDysvdenGQRWFCTGDIGEFHPDGCLQII 568
Cdd:PRK13295 372 LPGVEVRVVD-------ADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGTD------ADGWFDTGDLARIDADGYIRIS 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 530422004 569 DRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 620
Cdd:PRK13295 439 GRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDerlGERACAFVVPRP 492
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
126-611 |
2.76e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 101.39 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS- 204
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 205 -----------VELLESKLKTALLDISC-----VKHIIYVDnkainkAEYPEGFEI-HSMQSVEElGSNPENLGIPPSRP 267
Cdd:PRK12583 126 afktsdyhamlQELLPGLAEGQPGALACerlpeLRGVVSLA------PAPPPGFLAwHELQARGE-TVSREALAERQASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYss 344
Cdd:PRK12583 199 DRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVA--ESL-GLTEHDRLCVPVPLYHCFGMVlANLGCMTVGACLVY-- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 345 PLTLSDQSSKIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIQKTLFKIGydykleqikkgydaplcnl 422
Cdd:PRK12583 274 PNEAFDPLATLQAVEEERCTALYgvPTMFIA-----------------ELDHPQRGNFDLS------------------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 423 llfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD------YTTGRVGAPLicc 495
Cdd:PRK12583 318 ------------SLRTGIMAGAPCPIEVmRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADdlerrvETVGRTQPHL--- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 496 EIKLKDwqEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK12583 383 EVKVVD--PDGATV--PRGEIGELCTRGYSVMKGYWNNPEATAE--SIDEDG--WMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510
....*....|....*....|....*....|....*.
gi 530422004 576 kLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY 611
Cdd:PRK12583 455 -IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
271-608 |
1.48e-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: 96.57 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLI-AGMtgQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCR---IGYSSPL 346
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 347 TLSD--QSSKIkkgskgdctvlkpTLMAAVPEIMDRIyknvmskvqeMNYIQKTlfkiGYDYKLEQIKKGYDAPlcnlll 424
Cdd:cd17637 79 EALEliEEEKV-------------TLMGSFPPILSNL----------LDAAEKS----GVDLSSLRHVLGLDAP------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 fKKVKALlggnvrmmlsggaplspqtHRFMNVCFCCpigqGYGLTESCGAGTVTEVTDyTTGRVGAPLICCEIKLKDwqe 504
Cdd:cd17637 126 -ETIQRF-------------------EETTGATFWS----LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVD--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 505 ggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRK--KDLVKlQA 579
Cdd:cd17637 178 ----DNDRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTF---RNG--WHHTGDLGRFDEDGYLWYAGRKpeKELIK-PG 247
|
330 340
....*....|....*....|....*....
gi 530422004 580 GEYVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:cd17637 248 GENVYPAEVEKVILEHPAIAEVCVIGVPD 276
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
263-618 |
1.98e-21 |
|
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: 98.11 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHH---SNLIAGMTgqcERIpGLGPKDTYIGYLPLAH---VLELTAEIScfty 336
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISHraaLNTILDIN---RRF-AVGPDDRVLALSSLSFdlsVYDIFGALS---- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 337 gcrIGYSspLTLSDQsskikkGSKGDCTVLKP-------TLMAAVPEIMDRIyknvmskvqeMNYiqktlfkigydykLE 409
Cdd:cd12114 191 ---AGAT--LVLPDE------ARRRDPAHWAElierhgvTLWNSVPALLEML----------LDV-------------LE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 410 QIkkgyDAPLCNLllfkkvkallggnvRM-MLSG---GAPLSPQTHRFmnVCFCCPIGQGyGLTESCGAGTVTEVTDYTT 485
Cdd:cd12114 237 AA----QALLPSL--------------RLvLLSGdwiPLDLPARLRAL--APDARLISLG-GATEASIWSIYHPIDEVPP 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 486 GRV----GAPLI--CCEIkLKDWQeggytiNDKPN-PRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGE 558
Cdd:cd12114 296 DWRsipyGRPLAnqRYRV-LDPRG------RDCPDwVPGELWIGGRGVALGYLGDPELTAARFVTHPDGERLYRTGDLGR 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530422004 559 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD--QSYVISFVVP 618
Cdd:cd12114 369 YRPDGTLEFLGRRDGQVKVR-GYRIELGEIEAALQAHPGVARAVVVVLGDpgGKRLAAFVVP 429
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
260-625 |
2.72e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 98.36 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 260 LGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP---------KDTYIGYLPLAHVLELTAE 330
Cdd:PRK12492 197 LSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplmkegQEVMIAPLPLYHIYAFTAN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 331 ISCFTYgcrigysspltlsdqsskikkgsKGDCTVLKpTLMAAVPEIMDRIYKNVMSKVQEMNyiqkTLFkigydykleq 410
Cdd:PRK12492 277 CMCMMV-----------------------SGNHNVLI-TNPRDIPGFIKELGKWRFSALLGLN----TLF---------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 411 ikkgydAPLCNLLLFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVTDYTT----G 486
Cdd:PRK12492 319 ------VALMDHPGFKDLDF---SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTET---SPVASTNPYGElarlG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 487 RVGAPLICCEIKLKDwQEGgytiNDKP-NPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCL 565
Cdd:PRK12492 387 TVGIPVPGTALKVID-DDG----NELPlGERGELCIKGPQVMKGYWQQPEATAE--ALDAEG--WFKTGDIAVIDPDGFV 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530422004 566 QIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKRLTL 625
Cdd:PRK12492 458 RIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDErsgEAVKLFVVARDPGLSV 519
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
125-609 |
3.15e-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: 97.36 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 125 WMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 204
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 205 VELLESklktalldiscvkhiiyvdnkainkaeYPEGFEIhsmqsVEELGSNPENLGIPPSRPT-PSDMAIVMYTSGSTG 283
Cdd:cd12116 92 DALPDR---------------------------LPAGLPV-----LLLALAAAAAAPAAPRTPVsPDDLAYVIYTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 284 RPKGVMMHHSNLIAGMTGQCERiPGLGPKDTYIGYLPLA---HVLELTAEISCftyGCRIGYSSPLTLSDqsskikkgsk 360
Cdd:cd12116 140 RPKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAVTTYAfdiSLLELLLPLLA---GARVVIAPRETQRD---------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 361 gdctvlkPTLMAAvpeIMDRIYKNVMskvqemnyiQKTlfkigydykleqikkgydaPLCNLLLFkkvKALLGGNVRM-M 439
Cdd:cd12116 206 -------PEALAR---LIEAHSITVM---------QAT-------------------PATWRMLL---DAGWQGRAGLtA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 440 LSGGAPLSPQTHRFmnvcFCCPIGQG---YGLTESCGAGTVTEVTDYTTG-RVGAPLICCEIKLKDwqEGGytindKPNP 515
Cdd:cd12116 245 LCGGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAAAGPiPIGRPLANTQVYVLD--AAL-----RPVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 516 R---GEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 589
Cdd:cd12116 314 PgvpGELYIGGDGVAQGYLGRPALTAERFVPDpfaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIR-GHRIELGEIE 392
|
490 500
....*....|....*....|
gi 530422004 590 AALKNCPLIDNICAFAKSDQ 609
Cdd:cd12116 393 AALAAHPGVAQAAVVVREDG 412
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-618 |
3.44e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 97.62 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 119 ILGNYKWMNYLEVNRRVNNFGSGLT-ALGLKPKNTIAIFcetraewmiaAQTCFKYnfpLVTLYATLGKEAVVHGLN--- 194
Cdd:PRK06839 21 IITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAIL----------SQNSLEY---IVLLFAIAKVECIAVPLNirl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 195 -ESEASYLI----TSVELLESKLKTALLDI---SCVKHIIYVdnkainkaEYPEGFEIHSMQSVEElgsnpenlgippsr 266
Cdd:PRK06839 88 tENELIFQLkdsgTTVLFVEKTFQNMALSMqkvSYVQRVISI--------TSLKEIEDRKIDNFVE-------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltAEISCFTY-----GCRIG 341
Cdd:PRK06839 146 KNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHI----GGIGLFAFptlfaGGVII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 342 YSSPLTLSDQSSKIKKGskgdctvlKPTLMAAVPEIMDRIyknvmskvqemnyIQKTLFkigydykleqIKKGYDaplcn 421
Cdd:PRK06839 221 VPRKFEPTKALSMIEKH--------KVTVVMGVPTIHQAL-------------INCSKF----------ETTNLQ----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 422 lllfkkvkallggNVRMMLSGGAPLS-PQTHRFMNVCFccPIGQGYGLTEScgAGTV----TEVTDYTTGRVGAPLICCE 496
Cdd:PRK06839 265 -------------SVRWFYNGGAPCPeELMREFIDRGF--LFGQGFGMTET--SPTVfmlsEEDARRKVGSIGKPVLFCD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 497 IKLKDWQEGgytiNDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 576
Cdd:PRK06839 328 YELIDENKN----KVEVGEVGELLIRGPNVMKEYWNRPDATEETI---QDG--WLCTGDLARVDEDGFVYIVGRKKEMI- 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 530422004 577 LQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 618
Cdd:PRK06839 398 ISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeiPIAFIVK 442
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
263-698 |
3.61e-21 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 97.37 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 263 PPSRPTPSDMAIVM-YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltAEISC 333
Cdd:cd12118 125 EWIPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylnalANILEW---------EMKQHPVYLWTLPMFH-----CNGWC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 334 FTYGcrigysspltlsdqsskikkgskgdctvlkptlMAAV------------PEIMDRIYKNvmsKVQEMNyiqktlfk 401
Cdd:cd12118 191 FPWT---------------------------------VAAVggtnvclrkvdaKAIYDLIEKH---KVTHFC-------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 402 igydykleqikkgyDAPLCNLLLF---KKVKALLGGNVRMMlSGGAPLSPQTHRFMNvcfccPIG----QGYGLTESCGA 474
Cdd:cd12118 227 --------------GAPTVLNMLAnapPSDARPLPHRVHVM-TAGAPPPAAVLAKME-----ELGfdvtHVYGLTETYGP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 475 GTV-----------TEVTDYTTGRVGAPLICCE-IKLKDWQEGgytindKPNPR-----GEIVIGGQNISMGYFKNEEKT 537
Cdd:cd12118 287 ATVcawkpewdelpTEERARLKARQGVRYVGLEeVDVLDPETM------KPVPRdgktiGEIVFRGNIVMKGYLKNPEAT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 538 AEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS--- 614
Cdd:cd12118 361 AEAF---RGG--WFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVpca 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 615 FVvpnqkrlTLlaqQKGVEGTwvdicnnpamEAEILKEIREaanamKLERFEIPIKVRLSPEPWTPeTGlvtdafKLKRK 694
Cdd:cd12118 435 FV-------EL---KEGAKVT----------EEEIIAFCRE-----HLAGFMVPKTVVFGELPKTS-TG------KIQKF 482
|
....
gi 530422004 695 ELRN 698
Cdd:cd12118 483 VLRD 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-696 |
3.74e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.65 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLEsKLKTAlLDISCVkhiiyvdnkAINKAEYPEGFEIHSmqsveelgsnpenlgiPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 4657 HLLQ-RLPIP-DGLASL---------ALDRDEDWEGFPAHD----------------PAVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERiPGLGPKDTYIGYLPLAhvLELTAEiscftygcriGYSSPLTlsdqsskikkgsKGDCTV 365
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFS--FDGSHE----------GLYHPLI------------NGASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LKPTLMAAVPEIMDRIYKNVMSKVQemnyiqktlFKIGYDYKLEQikkgYDAPLCNLLLFKKV----KALLGGNVRMMLS 441
Cdd:PRK12316 4765 IRDDSLWDPERLYAEIHEHRVTVLV---------FPPVYLQQLAE----HAERDGEPPSLRVYcfggEAVAQASYDLAWR 4831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 442 GGAPLSpqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPlicceIKLKDWQEGGYTINDKPNPR---- 516
Cdd:PRK12316 4832 ALKPVY--------------LFNGYGPTETTVTVLLWKARDGDAcGAAYMP-----IGTPLGNRSGYVLDGQLNPLpvgv 4892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 517 -GEIVIGGQNISMGYFKNEEKTAEDY---SVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAAL 592
Cdd:PRK12316 4893 aGELYLGGEGVARGYLERPALTAERFvpdPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIR-GFRIELGEIEARL 4971
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 593 KNCPLIDNICAFAK--SDQSYVISFVVPNQKRLTllaqqkgvegtwvdicNNPAMEAEILKEIREAANAmKLERFEIPIK 670
Cdd:PRK12316 4972 REHPAVREAVVIAQegAVGKQLVGYVVPQDPALA----------------DADEAQAELRDELKAALRE-RLPEYMVPAH 5034
|
570 580
....*....|....*....|....*..
gi 530422004 671 -VRLSPEPWTPETglvtdafKLKRKEL 696
Cdd:PRK12316 5035 lVFLARMPLTPNG-------KLDRKAL 5054
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
127-698 |
7.32e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 96.94 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 127 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkYNFP-----LVTLYATLGKEAVVHGLNESEASYL 201
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA-MVEAH----FGVPmagavLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ITSVELleSKLKTALLDISCVKHIIYVDnkaINKAEYPEGFEIHSMqSVEEL--GSNPEnlgIPPSRPTPSDMAIVM-YT 278
Cdd:PRK08162 120 IVDTEF--AEVAREALALLPGPKPLVID---VDDPEYPGGRFIGAL-DYEAFlaSGDPD---FAWTLPADEWDAIALnYT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 279 SGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltaeiscftygCRiGYSSPLTLsd 350
Cdd:PRK08162 191 SGTTGNPKGVVYHHrgaylnalSNILAW---------GMPKHPVYLWTLPMFH--------------CN-GWCFPWTV-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 351 qsskikkgskgdctvlkpTLMAAVpeimdriykNV-MSKVQEmnyiqKTLFKIGYDyklEQIKKGYDAP-----LCNLLl 424
Cdd:PRK08162 245 ------------------AARAGT---------NVcLRKVDP-----KLIFDLIRE---HGVTHYCGAPivlsaLINAP- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 fKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCcpIGQGYGLTESCGAGTV----TEVTDYTTGRvgapliccEIKLK 500
Cdd:PRK08162 289 -AEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD--LTHVYGLTETYGPATVcawqPEWDALPLDE--------RAQLK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 501 DWQ------EGGYTIND----KPNPR-----GEIVIGGqNISM-GYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGC 564
Cdd:PRK08162 358 ARQgvryplQEGVTVLDpdtmQPVPAdgetiGEIMFRG-NIVMkGYLKNPKATEEAF---AGG--WFHTGDLAVLHPDGY 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 565 LQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVvpnqkrlTLlaqQKGVEGTwvdicn 641
Cdd:PRK08162 432 IKIKDRSKDII-ISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWgevPCAFV-------EL---KDGASAT------ 494
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 530422004 642 npamEAEILKEIREaanamKLERFEIPIKVRLSPEPWTpETGlvtdafKLKRKELRN 698
Cdd:PRK08162 495 ----EEEIIAHCRE-----HLAGFKVPKAVVFGELPKT-STG------KIQKFVLRE 535
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
128-620 |
1.17e-20 |
|
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: 95.90 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 207
Cdd:cd05959 32 YAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 LEsKLKTAL-LDISCVKHIIYVDnkainkaeyPEGFEIHSMQSVEELGSNPENLgiPPSRPTPSDMAIVMYTSGSTGRPK 286
Cdd:cd05959 112 AP-VLAAALtKSEHTLVVLIVSG---------GAGPEAGALLLAELVAAEAEQL--KPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 287 GVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsdqsskikkgSKGDCTVL 366
Cdd:cd05959 180 GVVHLHADIYWTAELYARNVLGIREDDVC-----------FSAAKLFFAYGLGNSLTFPL------------SVGATTVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 367 KPTLMAAvpeimDRIYKnvmskvqEMNYIQKTLFkigydykleqikkgYDAP--LCNLLLFKKVKALLGGNVRMMLSGGA 444
Cdd:cd05959 237 MPERPTP-----AAVFK-------RIRRYRPTVF--------------FGVPtlYAAMLAAPNLPSRDLSSLRLCVSAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 445 PLSPQTHRFMNVCFCCPIGQGYGLTE------SCGAGTVtevtdyTTGRVGAPLICCEIKLKDwQEGGYTINDKPnprGE 518
Cdd:cd05959 291 ALPAEVGERWKARFGLDILDGIGSTEmlhiflSNRPGRV------RYGTTGKPVPGYEVELRD-EDGGDVADGEP---GE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 519 IVIGGQNISMGYFKNEEKTAEDYSvdenGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 598
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTFQ----GE-WTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEVESALVQHPAV 434
|
490 500
....*....|....*....|....*
gi 530422004 599 DNICAFAKSDQSYVI---SFVVPNQ 620
Cdd:cd05959 435 LEAAVVGVEDEDGLTkpkAFVVLRP 459
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
262-698 |
2.56e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 95.33 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP----KDTYIGYLPLAHVLELTAEISCFTY- 336
Cdd:PRK08751 200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTANGLVFMKi 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 337 -GCRIGYSSPltlSDQSSKIKKgskgdctvLKPTLMAAVPEImdriyknvmskvqemnyiqKTLFKigydykleqikKGY 415
Cdd:PRK08751 280 gGCNHLISNP---RDMPGFVKE--------LKKTRFTAFTGV-------------------NTLFN-----------GLL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 416 DAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHrfmnvcfcCPIGQGYGLTESCGAGTVTEVT--DYTtGRVGAPLI 493
Cdd:PRK08751 319 NTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTG--------LTLVEAYGLTETSPAACINPLTlkEYN-GSIGLPIP 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 494 CCEIKLKDWQEGGYTINDKpnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PRK08751 390 STDACIKDDAGTVLAIGEI----GELCIKGPQVMKGYWKRPEETAK--VMDADG--WLHTGDIARMDEQGFVYIVDRKKD 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 574 LVkLQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKrltllaqqKGVEGTWVDICNNPAMEAEILKEi 653
Cdd:PRK08751 462 MI-LVSGFNVYPNEIEDVIAMMPGVLEVAAVG-----------VPDEK--------SGEIVKVVIVKKDPALTAEDVKA- 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 530422004 654 REAANamkLERFEIPIKVRLSPEpwTPEtglvTDAFKLKRKELRN 698
Cdd:PRK08751 521 HARAN---LTGYKQPRIIEFRKE--LPK----TNVGKILRRELRD 556
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
178-592 |
3.12e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 96.15 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 178 VTLYATLGKEAVVHGLNESEASYLITSVELLES-KLKTALLDISCVKHIIYVDN--KAINKAEypegfEIHSMQSVEELg 254
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKFLEKlKNKGFDLELPENVKVIYLEDlkAKISKVD-----KLTALLAARLL- 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 255 snP----ENLGIPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTAE 330
Cdd:PRK08633 767 --ParllKRLYGPT--FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSLPFFHSFGLTVT 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 331 --------ISCftygcrIGYSSPLtlsdQSSKIKKgskgdcTVLK--PTLMAAVPEIMdRIYknvmskvqemnyiqktlf 400
Cdd:PRK08633 842 lwlpllegIKV------VYHPDPT----DALGIAK------LVAKhrATILLGTPTFL-RLY------------------ 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 401 kigydykleqikkgydaplcnlLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV--- 477
Cdd:PRK08633 887 ----------------------LRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVnlp 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 478 -TEVTDYTT------GRVGAPLICCEIKLKDwQEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEdYSVDENGQRW 550
Cdd:PRK08633 945 dVLAADFKRqtgskeGSVGMPLPGVAVRIVD-PETFEEL--PPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKDIDGIGW 1020
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 530422004 551 FCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAAL 592
Cdd:PRK08633 1021 YVTGDKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
262-617 |
3.71e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 94.66 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCE-RIPGLG--PKDTYIGYLPLAHVLELTAEISCftyGC 338
Cdd:PLN02246 171 LPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLYfhSDDVILCVLPMFHIYSLNSVLLC---GL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 339 RIGysspltlsdqsSKIKKGSKGDCTVL-------KPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigyDYKLEQI 411
Cdd:PLN02246 248 RVG-----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKSPVVE----------------KYDLSSI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 412 kkgydaplcnlllfkkvkallggnvRMMLSGGAPLSPQTH-----RFMNVCfccpIGQGYGLTEscgAGTV--------T 478
Cdd:PLN02246 301 -------------------------RMVLSGAAPLGKELEdafraKLPNAV----LGQGYGMTE---AGPVlamclafaK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 479 EVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGE 558
Cdd:PLN02246 349 EPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDPEATAN--TIDKDG--WLHTGDIGY 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530422004 559 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVV 617
Cdd:PLN02246 422 IDDDDELFIVDRLKELIKYK-GFQVAPAELEALLISHPSIADAAVVPMKDEVageVPVAFVV 482
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
128-656 |
4.58e-20 |
|
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: 94.23 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGlKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYA-TLGKEA--VVHGLNESEASYLITS 204
Cdd:cd05931 27 YAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpTPGRHAerLAAILADAGPRVVLTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 205 VELLEsklktALLDIscvkhiiyvdnkainkAEYPEGFEIHSMQSVEELGSNPENLGIPPSrPTPSDMAIVMYTSGSTGR 284
Cdd:cd05931 106 AAALA-----AVRAF----------------AASRPAAGTPRLLVVDLLPDTSAADWPPPS-PDPDDIAYLQYTSGSTGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 285 PKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIGYSSPLT-LSDQSSKIKKGS 359
Cdd:cd05931 164 PKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYHdmglIGGLLTPLYS---GGPSVLMSPAAfLRRPLRWLRLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 360 KGDCTvlkptlMAAVPeimdriyknvmskvqemNYiqktlfkiGYDYkleQIKKGYDAPLCNLLLfkkvkallgGNVRMM 439
Cdd:cd05931 240 RYRAT------ISAAP-----------------NF--------AYDL---CVRRVRDEDLEGLDL---------SSWRVA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 440 LSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTESC--------GAGTVTEVTDYTTG--------------- 486
Cdd:cd05931 277 LNGAEPVRPATlRRFAEAfapfgfrpeAFRP----SYGLAEATlfvsggppGTGPVVLRVDRDALagravavaaddpaar 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 487 ---RVGAPLICCEIKLKDwQEGGytindKPNPR---GEIVIGGQNISMGYFKNEEKTAE--DYSVDENGQRWFCTGDIGE 558
Cdd:cd05931 353 elvSCGRPLPDQEVRIVD-PETG-----RELPDgevGEIWVRGPSVASGYWGRPEATAEtfGALAATDEGGWLRTGDLGF 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 559 FHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPlidnicafAKSDQSYVISFVVPNQKRLTLLAQQKgVEGTWVd 638
Cdd:cd05931 427 LH-DGELYITGRLKDLI-IVRGRNHYPQDIEATAEEAH--------PALRPGCVAAFSVPDDGEERLVVVAE-VERGAD- 494
|
570
....*....|....*...
gi 530422004 639 icnnPAMEAEILKEIREA 656
Cdd:cd05931 495 ----PADLAAIAAAIRAA 508
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
269-621 |
1.29e-19 |
|
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: 92.15 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKdtyigylPLAHVleltaEISCFTYGCRIG-YSSPLT 347
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAHAWRREYELDSF-------PVRLL-----QMASFSFDVFAGdFARSLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LSDQSSKIKKGSKGDCTVL-------KPTLMAAVPE----IMDRIYKNvmskvqEMNYIQKTLFKIGYDykleqikkgyd 416
Cdd:cd17650 159 NGGTLVICPDEVKLDPAALydlilksRITLMESTPAlirpVMAYVYRN------GLDLSAMRLLIVGSD----------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 417 apLCNLLLFKKVKALLGGNVRMMLSggaplspqthrfmnvcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAP 491
Cdd:cd17650 222 --GCKAQDFKTLAARFGQGMRIINS------------------------YGVTEATIDSTYYEEGRDPLGDsanvpIGRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 492 LICCEIklkdwqeggYTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGC 564
Cdd:cd17650 276 LPNTAM---------YVLDERLQPQpvgvaGELYIGGAGVARGYLNRPELTAERFVENpfAPGERMYRTGDLARWRADGN 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 565 LQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 621
Cdd:cd17650 347 VELLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVVAVREDkggEARLCAYVVAAAT 405
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-697 |
2.42e-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: 90.03 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYSSP 345
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERL-GLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 346 LTlsDQSSKIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIQKTLFKIGydykleqikkgydaplcnll 423
Cdd:cd05917 78 SF--DPLAVLEAIEKEKCTALHgvPTMFIA-----------------ELEHPDFDKFDLS-------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 424 lfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR---VGAPLICCEIKL 499
Cdd:cd05917 119 -----------SLRTGIMAGAPCPPELmKRVIEVMNMKDVTIAYGMTETSPVSTQTRTDDSIEKRvntVGRIMPHTEAKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 500 KDwQEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDysvdENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQA 579
Cdd:cd05917 188 VD-PEGGIVP--PVGVPGELCIRGYSVMKGYWNDPEKTAEA----IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 580 GEYVSLGKVEAALKNCPLIDNICAFAKSDQSYvisfvvpnqkrltllaqqkGVE-GTWVDICNNPAMEAEilkEIREAAN 658
Cdd:cd05917 260 GENIYPREIEEFLHTHPKVSDVQVVGVPDERY-------------------GEEvCAWIRLKEGAELTEE---DIKAYCK 317
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 530422004 659 AmKLERFEIPIKVRLSPE-PwtpetglVTDAFKLKRKELR 697
Cdd:cd05917 318 G-KIAHYKVPRYVFFVDEfP-------LTVSGKIQKFKLR 349
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
101-605 |
2.50e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 92.13 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 101 ILSEENEMQPNgkvfKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAE---------WMIAAQTcf 171
Cdd:PRK06155 26 MLARQAERYPD----RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEfldvflgcaWLGAIAV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 172 kynfPLVTlyATLGKEaVVHGLNESEASYLITSVELLESkLKTALLDISCVKHIIYVDnkAINKAEYPEGFEIHSMQsve 251
Cdd:PRK06155 100 ----PINT--ALRGPQ-LEHILRNSGARLLVVEAALLAA-LEAADPGDLPLPAVWLLD--APASVSVPAGWSTAPLP--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 252 elgsnPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAG-MTGqceRIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK06155 167 -----PLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyWWGrNSA---EDLEIGADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 330 EISCFTYGCRIgysspltlsdqsskikkgskgdctVLKPTLMAAvpEIMDRIYKNvmskvqemnyiQKTLFkigydYKLe 409
Cdd:PRK06155 239 FFQALLAGATY------------------------VLEPRFSAS--GFWPAVRRH-----------GATVT-----YLL- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 410 qikkGYDAPLcnLLLFKKVKALLGGNVRMMLSGGAPlsPQTHRFMNVCFCCPIGQGYGLTES---CGaGTVTEVTDYTTG 486
Cdd:PRK06155 276 ----GAMVSI--LLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETnfvIA-VTHGSQRPGSMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 487 RVgAPLIccEIKLKDwqEGGYTIndKPNPRGEIVIGGQN---ISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDG 563
Cdd:PRK06155 347 RL-APGF--EARVVD--EHDQEL--PDGEPGELLLRADEpfaFATGYFGMPEKTVEAWR-----NLWFHTGDRVVRDADG 414
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 530422004 564 CLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 605
Cdd:PRK06155 415 WFRFVDRIKDAIRRR-GENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
271-620 |
3.69e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.83 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTG----QCERIPGLGPKDTYIGYLPLAHVLELtaeiSCFTYGcrigysspl 346
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELfvrfEASQYEYPGSDNVYLAALPMFHIYGL----SLFVVG--------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 347 TLSDQSSKIkkgskgdctvlkptlmaavpeIMDRIYKNVMSKVQEMNYIqkTLFKIgydykleqikkgydAPLCNLLLFK 426
Cdd:PLN02574 266 LLSLGSTIV---------------------VMRRFDASDMVKVIDRFKV--THFPV--------------VPPILMALTK 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 427 KVKALLGG---NVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGT----VTEVTDYTTGRVGAPLIccEIK 498
Cdd:PLN02574 309 KAKGVCGEvlkSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIQGYGMTESTAVGTrgfnTEKLSKYSSVGLLAPNM--QAK 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 499 LKDWQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTaeDYSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQ 578
Cdd:PLN02574 387 VVDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNPKAT--QSTIDKDG--WLRTGDIAYFDEDGYLYIVDRLKEIIKYK 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530422004 579 aGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQ 620
Cdd:PLN02574 460 -GFQIAPADLEAVLISHPEIIDAAVTAVPDKecgEIPVAFVVRRQ 503
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
268-700 |
4.88e-19 |
|
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: 90.68 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLA---HVLE-LTAEISCftyGCRIGYS 343
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAL-GLTSESRVLQFASYTfdvSILEiFTTLAAG---GCLCIPS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 344 SPLTLSDQSSKIKKgSKGDCTVLKPTLMA-----AVPEImdriyknvmskvqemnyiqKTLFKIGydyklEQIKKgydap 418
Cdd:cd05918 180 EEDRLNDLAGFINR-LRVTWAFLTPSVARlldpeDVPSL-------------------RTLVLGG-----EALTQ----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 419 lcnlllfkKVKALLGGNVRMMlsggaplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVTDYTTGR-VGAPL--ICC 495
Cdd:cd05918 230 --------SDVDTWADRVRLI------------------------NAYGPAECTIAATVSPVVPSTDPRnIGRPLgaTCW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 496 EIKLKDwqeggytiNDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDY---------SVDENGQRWFCTGDIGEFHPDG 563
Cdd:cd05918 278 VVDPDN--------HDRLVPIgavGELLIEGPILARGYLNDPEKTAAAFiedpawlkqEGSGRGRRLYRTGDLVRYNPDG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 564 CLQIIDRKKDLVKLQaGEYVSLGKVEAALKNC-PLIDNICAFA-----KSDQSYVISFVVPNQkrltllAQQKGVEGTWV 637
Cdd:cd05918 350 SLEYVGRKDTQVKIR-GQRVELGEIEHHLRQSlPGAKEVVVEVvkpkdGSSSPQLVAFVVLDG------SSSGSGDGDSL 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422004 638 DICNNPAMEAEIlKEIREAANAmKLERFEIP-IKVRLSPEPWTPeTGlvtdafKLKRKELRNHY 700
Cdd:cd05918 423 FLEPSDEFRALV-AELRSKLRQ-RLPSYMVPsVFLPLSHLPLTA-SG------KIDRRALRELA 477
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
122-621 |
5.58e-19 |
|
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: 90.61 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 122 NYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL 201
Cdd:cd17656 11 NQKL-TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ITSVELlESKLKtalldiscvkhiiyvDNKAINKAEYPegfeIHSMQSVEELGSNPENlgippsrptpSDMAIVMYTSGS 281
Cdd:cd17656 90 LTQRHL-KSKLS---------------FNKSTILLEDP----SISQEDTSNIDYINNS----------DDLLYIIYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 282 TGRPKGVMMHHSNLIAGMtgQCERipglgpkdTYIGYLPLAHVLELTAeiscftygcrigYSSPLTLSDQSSKIKKGskG 361
Cdd:cd17656 140 TGKPKGVQLEHKNMVNLL--HFER--------EKTNINFSDKVLQFAT------------CSFDVCYQEIFSTLLSG--G 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 362 DCTVLKPTLMAAVPEIMDRIYKNvmskvqemnYIQKTLFKIGYdykLEQI--KKGYDAPLcnlllFKKVKALLGGNVRMM 439
Cdd:cd17656 196 TLYIIREETKRDVEQLFDLVKRH---------NIEVVFLPVAF---LKFIfsEREFINRF-----PTCVKHIITAGEQLV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 440 LSggaplspQTHRFMNVCFCCPIGQGYGLTEScgagtvTEVTDYTTGR---------VGAPLICCEIKLKDWQEggytin 510
Cdd:cd17656 259 IT-------NEFKEMLHEHNVHLHNHYGPSET------HVVTTYTINPeaeipelppIGKPISNTWIYILDQEQ------ 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 511 dKPNPRG---EIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 585
Cdd:cd17656 320 -QLQPQGivgELYISGASVARGYLNRQELTAEKFFPDpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR-GYRIEL 397
|
490 500 510
....*....|....*....|....*....|....*....
gi 530422004 586 GKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 621
Cdd:cd17656 398 GEIEAQLLNHPGVSEAVVLDKADdkgEKYLCAYFVMEQE 436
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-608 |
7.31e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 90.19 E-value: 7.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 133 RRVNNFGSGLTALGLKPKNTIAI-------FCETRAEWMIAAQTCFKYnfpLVTLYATLgKEAVVHGLNESEASYLITSV 205
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLilpnrftYIELSFAVAYAGGRLGLV---FVPLNPTL-KESVLRYLVADAGGRIVLAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLESKLKTALldISCVKHIIYVDNKAINKAEYPegfeihsmqsveelgsnpenlgIPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:cd05922 77 AGAADRLRDAL--PASPDPGTVLDADGIRAARAS----------------------APAHEVSHEDLALLLYTSGSTGSP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI----GYSSPLTLSDqsskikkgskg 361
Cdd:cd05922 133 KLVRLSHQNLLANARSIAEYL-GITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDDAFWE----------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 362 DCTVLKPTLMAAVPeimdriyknvmskvqemnYIQKTLFKIGYDykleqikkgyDAPLCNLllfkkvkallggnvRMMLS 441
Cdd:cd05922 201 DLREHGATGLAGVP------------------STYAMLTRLGFD----------PAKLPSL--------------RYLTQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 442 GGAPLSPQT-HRFmnvcfcCPIGQG------YGLTEsCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDwQEGGYTind 511
Cdd:cd05922 239 AGGRLPQETiARL------RELLPGaqvyvmYGQTE-ATRRMTYlppERILEKPGSIGLAIPGGEFEILD-DDGTPT--- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 512 KPNPRGEIVIGGQNISMGYFKNEektAEDYSVDENGQRWFcTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAA 591
Cdd:cd05922 308 PPGEPGEIVHRGPNVMKGYWNDP---PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIEAA 382
|
490
....*....|....*..
gi 530422004 592 LKNCPLIDNICAFAKSD 608
Cdd:cd05922 383 ARSIGLIIEAAAVGLPD 399
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
232-629 |
1.00e-18 |
|
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: 90.03 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 232 AINKAEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGP 311
Cdd:cd05906 131 EFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 312 KDTYIGYLPLAHVLELT-AEISCFTYGCR-IGYSSPLTLSDqsskikkgskgdctvlkPTLMaavpeimdriyknvmskv 389
Cdd:cd05906 208 QDVFLNWVPLDHVGGLVeLHLRAVYLGCQqVHVPTEEILAD-----------------PLRW------------------ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 390 qeMNYIQKtlFKIGYDYkleqikkgydAP--LCNLLL-----FKKVKALLgGNVRMMLSGGAPLSPQTHRFM-------- 454
Cdd:cd05906 253 --LDLIDR--YRVTITW----------APnfAFALLNdlleeIEDGTWDL-SSLRYLVNAGEAVVAKTIRRLlrllepyg 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 455 ---NVcfccpIGQGYGLTESCgAGTVTEVTDYTTGR--------VGAPLICCEIKLKDwqeggytINDKPNPRGEI---V 520
Cdd:cd05906 318 lppDA-----IRPAFGMTETC-SGVIYSRSFPTYDHsqalefvsLGRPIPGVSMRIVD-------DEGQLLPEGEVgrlQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 521 IGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVKLQAGEYvSLGKVEAALKNCPLIDN 600
Cdd:cd05906 385 VRGPVVTKGYYNNPEANAE--AFTEDG--WFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNY-YSHEIEAAVEEVPGVEP 458
|
410 420 430
....*....|....*....|....*....|....*.
gi 530422004 601 --ICAFAKSDQS-----YVIsFVVPNQKRLTLLAQQ 629
Cdd:cd05906 459 sfTAAFAVRDPGaeteeLAI-FFVPEYDLQDALSET 493
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
245-575 |
1.17e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 89.55 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 245 HSMQSVEELGSNPEN------LGIPPSRPT----PSDMAIVMYTSGSTGRPKGVMMHHSNLIA-GMTgqCERIPGLGPKD 313
Cdd:PRK07514 121 AGAPHVETLDADGTGslleaaAAAPDDFETvprgADDLAAILYTSGTTGRSKGAMLSHGNLLSnALT--LVDYWRFTPDD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 314 TYIGYLPLAHVLELTAEISCftygcrigyssplTLSDQSSKIkkgskgdctvLKPTL-MAAVPEIMDRiyKNVMSKVqem 392
Cdd:PRK07514 199 VLIHALPIFHTHGLFVATNV-------------ALLAGASMI----------FLPKFdPDAVLALMPR--ATVMMGV--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 393 nyiqKTLfkigYDYKLEQikKGYDAPLCnlllfkkvkallgGNVRMMLSGGAPLSPQTHRfmnvCFCCPIGQG----YGL 468
Cdd:PRK07514 251 ----PTF----YTRLLQE--PRLTREAA-------------AHMRLFISGSAPLLAETHR----EFQERTGHAilerYGM 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 469 TESC--------G---AGTVtevtdyttgrvGAPLICCEIKLKDWQEGgytindKPNPRGE---IVIGGQNISMGYFKNE 534
Cdd:PRK07514 304 TETNmntsnpydGerrAGTV-----------GFPLPGVSLRVTDPETG------AELPPGEigmIEVKGPNVFKGYWRMP 366
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 530422004 535 EKTAEDYSVDenGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK07514 367 EKTAEEFRAD--G--FFITGDLGKIDERGYVHIVGRGKDLI 403
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
245-598 |
1.19e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 89.56 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 245 HSMQSVEELGSNpeNLGIPPSRPT-PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH 323
Cdd:PRK06145 125 AAQADSRRLAQG--GLEIPPQAAVaPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIAL-GLTASERLLVVGPLYH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 324 V--LELTAeISCFTYGCRIGYSSPLTLSDQSSKIKKgSKGDCTVLKPTLMAAVPEIMDRiyknvmskvqemnyiqktlfk 401
Cdd:PRK06145 202 VgaFDLPG-IAVLWVGGTLRIHREFDPEAVLAAIER-HRLTCAWMAPVMLSRVLTVPDR--------------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 402 igYDYKLeqikkgydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQTHR-----FMNVCFCcpigQGYGLTESCGAGT 476
Cdd:PRK06145 259 --DRFDL-------------------------DSLAWCIGGGEKTPESRIRdftrvFTRARYI----DAYGLTETCSGDT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 477 VTEVTDY--TTGRVGAPLICCEIKLKDwQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqrWFCTG 554
Cdd:PRK06145 308 LMEAGREieKIGSTGRALAHVEIRIAD-GAGRWL---PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----WFRSG 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530422004 555 DIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLI 598
Cdd:PRK06145 379 DVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEV 421
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
124-609 |
1.19e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 90.04 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 124 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEW------MIAAQTCFKYNFPlVTLYATLGKEAvvhglnESE 197
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYgivalgIMAAGGVFSGANP-TALESEIKKQA------EAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 198 ASYLITSVELLESKLKTALLDIscvkhIIYVDNKAINKAEYPEgfeihSMQSVEELGSNPENLGIppsrpTPSDMAIVMY 277
Cdd:PLN02330 127 GAKLIVTNDTNYGKVKGLGLPV-----IVLGEEKIEGAVNWKE-----LLEAADRAGDTSDNEEI-----LQTDLCALPF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 278 TSGSTGRPKGVMMHHSNLIAGMtgqCERIPGLGP----KDTYIGYLPLAHVLELTAeISCFTYgcrigysspltlsDQSS 353
Cdd:PLN02330 192 SSGTTGISKGVMLTHRNLVANL---CSSLFSVGPemigQVVTLGLIPFFHIYGITG-ICCATL-------------RNKG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 354 KIKKGSKGDCTVLKPTLMAA-------VPEIMDRIYKNVMskVQEmnyiqktlfkigydYKLEQIKkgydaplcnlllfk 426
Cdd:PLN02330 255 KVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKNPI--VEE--------------FDLSKLK-------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 427 kvkallggnVRMMLSGGAPLSPQ-----THRFMNVcfccPIGQGYGLTE-SCGagTVTEvTDYTTGR-------VGAPLI 493
Cdd:PLN02330 305 ---------LQAIMTAAAPLAPElltafEAKFPGV----QVQEAYGLTEhSCI--TLTH-GDPEKGHgiakknsVGFILP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 494 CCEIKLKDWQEGGYTINDKPnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PLN02330 369 NLEVKFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYNNKEETDR--TIDEDG--WLHTGDIGYIDDDGDIFIVDRIKE 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 530422004 574 LVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:PLN02330 442 LIKYK-GFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
271-596 |
2.12e-18 |
|
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: 87.17 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCRIGYSSPLTlsd 350
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFH-----------TFGYKAGIVACLL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 351 qsskikKGSkgdcTVLkPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGY--DYKLEQIKKGYD-APLCNLLLFKK 427
Cdd:cd17638 66 ------TGA----TVV-PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGrkKFDLSSLRAAVTgAATVPVELVRR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 428 VKALLGgnvrmmlsggaplspqthrFMNVCfccpigQGYGLTEsCGAGTVTEVTDYTT---GRVGAPLICCEIKLKDwqe 504
Cdd:cd17638 135 MRSELG-------------------FETVL------TAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 505 ggytindkpnpRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVS 584
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAE--AIDADG--WLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVY 249
|
330
....*....|..
gi 530422004 585 LGKVEAALKNCP 596
Cdd:cd17638 250 PAEVEGALAEHP 261
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
267-643 |
3.56e-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: 87.75 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-------AGMTgqceripgLGPKDTyigylpLAHVLELTAEISCFTYGCR 339
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyvsqppARLD--------VGPGSR------VAQVLSIAFDACIGEIFST 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 340 IGYSSPLTLSDQSSKIKKGSKG-DCTVLKPTLMAAVPeimdriyknvmskvqemnyiqktlfkigydykleqiKKGYDap 418
Cdd:cd17653 168 LCNGGTLVLADPSDPFAHVARTvDALMSTPSILSTLS------------------------------------PQDFP-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 419 lcnlllfkkvkallggNVRMMLSGGAPLSP-------QTHRFMNvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAP 491
Cdd:cd17653 210 ----------------NLKTIFLGGEAVPPslldrwsPGRRLYN---------AYGPTECTISSTMTELLPGQPVTIGKP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 492 LICCEIKLKDwqeggytINDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQ 566
Cdd:cd17653 265 IPNSTCYILD-------ADLQPVPegvVGEICISGVQVARGYLGNPALTASKFVPDpfWPGSRMYRTGDYGRWTEDGGLE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 567 IIDRKKDLVKLQaGEYVSLGKVEA-ALKNCPLIDNICAFAKSDQsyVISFVVPN-------QKRLTLLAQQKGVEGTWVD 638
Cdd:cd17653 338 FLGREDNQVKVR-GFRINLEEIEEvVLQSQPEVTQAAAIVVNGR--LVAFVTPEtvdvdglRSELAKHLPSYAVPDRIIA 414
|
....*
gi 530422004 639 ICNNP 643
Cdd:cd17653 415 LDSFP 419
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
128-593 |
4.14e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 88.02 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK---------YNF---PLVTLYATLGKEAVVHglne 195
Cdd:PRK07798 31 YAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKaravpvnvnYRYvedELRYLLDDSDAVALVY---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 196 sEASYLITSVELLESKLKtalldiscVKHIIYVDNKAINkaEYPEGfeIHSMQSVEELGSnPENLGIPPSrptPSDMaIV 275
Cdd:PRK07798 107 -EREFAPRVAEVLPRLPK--------LRTLVVVEDGSGN--DLLPG--AVDYEDALAAGS-PERDFGERS---PDDL-YL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 276 MYTSGSTGRPKGVMMHHSNLiagmtgqceRIPGLGPKDTYIGylPLAHVLELTAEISCFTYGCRIGYSSPL--------T 347
Cdd:PRK07798 169 LYTGGTTGMPKGVMWRQEDI---------FRVLLGGRDFATG--EPIEDEEELAKRAAAGPGMRRFPAPPLmhgagqwaA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LSDQSSkikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmsKVQEMnyiqktlFKIGydykleqikkgyDA---PLcnlll 424
Cdd:PRK07798 238 FAALFS-------GQTVVLLPDVRFDADEVWRTIERE---KVNVI-------TIVG------------DAmarPL----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 fkkVKALLGGN------VRMMLSGGAPLSPQTHR-----FMNVCfccpIGQGYGLTES--CGAGTVTEVTDYTTG-RVGA 490
Cdd:PRK07798 284 ---LDALEARGpydlssLFAIASGGALFSPSVKEallelLPNVV----LTDSIGSSETgfGGSGTVAKGAVHTGGpRFTI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 491 plicceiklkdwqeGGYTI----NDKPNPRGEIVIG----GQNISMGYFKNEEKTAEDYSVdENGQRWFCTGDIGEFHPD 562
Cdd:PRK07798 357 --------------GPRTVvldeDGNPVEPGSGEIGwiarRGHIPLGYYKDPEKTAETFPT-IDGVRYAIPGDRARVEAD 421
|
490 500 510
....*....|....*....|....*....|.
gi 530422004 563 GCLQIIDRkKDLVKLQAGEYVSLGKVEAALK 593
Cdd:PRK07798 422 GTITLLGR-GSVCINTGGEKVFPEEVEEALK 451
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
268-620 |
7.65e-18 |
|
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: 86.98 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIgylpLAH-------VLELtaeISCFTYGCRI 340
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDDVWT----LFHsyafdfsVWEI---WGALLHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 341 GYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAavpeimdriYKNVMSKVQEMNyiqktlfkigydykleqikkgyDAPLc 420
Cdd:cd17643 163 VVVPYEVARSPEDFARLLRDEGVTVLNQTPSA---------FYQLVEAADRDG----------------------RDPL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 421 nlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQ---GYGLTESCGAGTVTEVTDYTTGRVGAPLICCEI 497
Cdd:cd17643 211 --------------ALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETTVHVTFRPLDAADLPAAAASPIGRPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 498 klkdwqeGGYTI-----NDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVDEN---GQRWFCTGDIGEFHPDGCLQ 566
Cdd:cd17643 277 -------PGLRVyvldaDGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpGSRMYRTGDLARRLPDGELE 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 530422004 567 IIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 620
Cdd:cd17643 350 YLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDepgDTRLVAYVVADD 405
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
260-624 |
8.74e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 87.38 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 260 LGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCE-------RIPGLGPKDTYIGYLPLAHVLELTAeis 332
Cdd:PRK07059 194 QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-QMEawlqpafEKKPRPDQLNFVCALPLYHIFALTV--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 333 CFTYGCRIGYSSPLTLS--DQSSKIKKGSKgdctvLKPTLMAAVpeimdriyknvmskvqemnyiqKTLFkigydykleq 410
Cdd:PRK07059 270 CGLLGMRTGGRNILIPNprDIPGFIKELKK-----YQVHIFPAV----------------------NTLY---------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 411 ikkgydaplcNLLL---------FKKVKALLGGnvrmmlsGGAPLSPQTHRFMNVCfCCPIGQGYGLTESCGAGTV--TE 479
Cdd:PRK07059 313 ----------NALLnnpdfdkldFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCnpVD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 480 VTDYTtGRVGAPLICCEIKLKDwQEGgytiNDKPNPR-GEIVIGGQNISMGYFKNEEKTAEDYSVDEngqrWFCTGDIGE 558
Cdd:PRK07059 375 ATEFS-GTIGLPLPSTEVSIRD-DDG----NDLPLGEpGEICIRGPQVMAGYWNRPDETAKVMTADG----FFRTGDVGV 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530422004 559 FHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKRLT 624
Cdd:PRK07059 445 MDERGYTKIVDRKKDMI-LVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEhsgEAVKLFVVKKDPALT 512
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-618 |
9.80e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 9.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-- 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ellESKLKTALLDISCVkhiIYVDNKAINKAEYPegfeihsmqsveelgsnpenlgiPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 3161 ---QSHLRLPLAQGVQV---LDLDRGDENYAEAN-----------------------PAIRTMPENLAYVIYTSGSTGKP 3211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLI--AGMTGQCEripGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQsskikkgskgdc 363
Cdd:PRK12316 3212 KGVGIRHSALSnhLCWMQQAY---GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP------------ 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 364 tvlkptlmAAVPEIMDRIYKNVMSKVQEMnyIQKtlfkigydykleqikkgydaplcnllLFKKVKALLGGNVRMMLSGG 443
Cdd:PRK12316 3277 --------ALLVELINSEGVDVLHAYPSM--LQA--------------------------FLEEEDAHRCTSLKRIVCGG 3320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 444 APLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwqeggytINDKPNPRG---E 518
Cdd:PRK12316 3321 EALPADLQQQVFAGL--PLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-------GSLEPVPVGalgE 3391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 519 IVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCP 596
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLTAERFVPDpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHP 3470
|
490 500
....*....|....*....|..
gi 530422004 597 LIDNICAFAKSDQSyVISFVVP 618
Cdd:PRK12316 3471 WVREAVVLAVDGRQ-LVAYVVP 3491
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
270-697 |
1.12e-17 |
|
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: 86.24 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLS 349
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPT-AAYWLGLRPDDIH-----------WNIADPGWAKGAWSSFFGPWLLG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 350 dqsskikkgskgdCTVLKPTLMAAVPEimdRIYKnVMSKvqemnyiqktlfkigydyklEQIKKGYDAPLCNLLLFKKvk 429
Cdd:cd05972 149 -------------ATVFVYEGPRFDAE---RILE-LLER--------------------YGVTSFCGPPTAYRMLIKQ-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 430 ALLGGN---VRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGG 506
Cdd:cd05972 190 DLSSYKfshLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 507 YTindKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYSVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVS 584
Cdd:cd05972 269 EL---PPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD-----YYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 585 LGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVpnqkrltllaQQKGVEGTwvdicnnPAMEAEILKEIREaanamK 661
Cdd:cd05972 340 PFEVESALLEHPAVAEAAVVGSPDPVRgevVKAFVV----------LTSGYEPS-------EELAEELQGHVKK-----V 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 530422004 662 LERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELR 697
Cdd:cd05972 398 LAPYKYPREIEFVEElPKTI-SG------KIRRVELR 427
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
128-575 |
1.44e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 86.93 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAifcetraewmiaaqtcfkYNFPLV--TLYATLGKEA---------------VV 190
Cdd:PRK07529 61 YAELLADVTRTANLLHSLGVGPGDVVA------------------FLLPNLpeTHFALWGGEAagianpinpllepeqIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 191 HGLNESEASYLITSVELLES----KLKTALLDISCVKHIIYVDnkaINKAEYPEGFEIHSMQSV----------EELGSN 256
Cdd:PRK07529 123 ELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVD---LARYLPGPKRLAVPLIRRkaharildfdAELARQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 257 PENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFT 335
Cdd:PRK07529 200 PGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA-NAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGlAPLA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 336 YGCRIGYSSPLtlsdqsskikkGSKGdctvlkPTLMAAVPEIMDRIYKNVMSKVqemnyiqKTLFkigydykleqikkgy 415
Cdd:PRK07529 279 RGAHVVLATPQ-----------GYRG------PGVIANFWKIVERYRINFLSGV-------PTVY--------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 416 daplcNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHR-FMNVCfCCPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLI 493
Cdd:PRK07529 320 -----AALLQVPVDGHDISSLRYALCGAAPLPVEVFRrFEAAT-GVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 494 CCEIK-LKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFkNEEKTAEDYSvdenGQRWFCTGDIGEFHPDGCLQIIDRKK 572
Cdd:PRK07529 394 YQRVRvVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL----EDGWLNTGDLGRIDADGYFWLTGRAK 468
|
...
gi 530422004 573 DLV 575
Cdd:PRK07529 469 DLI 471
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-618 |
1.57e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.71 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLEsklktaLLDISCVKHIIYVDNKAINKAEYPEGfeihsmqsveelgsNPEnlgippSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 617 HLGR------KLPLAAGVQVLDLDRPAAWLEGYSEE--------------NPG------TELNPENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkgskgdctv 365
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRD--------------- 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 lkptlMAAVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykleqikkgydapLCNLLLFKKVKALLggNVRMMLSGGAP 445
Cdd:PRK12316 735 -----PAKLVELINREGVDTLHFVPSM--------------------------LQAFLQDEDVASCT--SLRRIVCSGEA 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 446 LS-----------PQTHRFmNVcfccpigqgYGLTESCGAGT----VTEVTDytTGRVGAPLIcceiklkdwQEGGYTIN 510
Cdd:PRK12316 782 LPadaqeqvfaklPQAGLY-NL---------YGPTEAAIDVThwtcVEEGGD--SVPIGRPIA---------NLACYILD 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 511 DKPNP-----RGEIVIGGQNISMGYFKNEEKTAEDYSVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYV 583
Cdd:PRK12316 841 ANLEPvpvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRI 919
|
490 500 510
....*....|....*....|....*....|....*
gi 530422004 584 SLGKVEAALKNCPLIDNICAFAKSDQSYViSFVVP 618
Cdd:PRK12316 920 ELGEIEARLLEHPWVREAAVLAVDGKQLV-GYVVL 953
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
77-575 |
1.74e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.40 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 77 DTLDKLFDHAVSKFGKKDSLGTREilseenemqpngkvfkklilGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIF 156
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRD--------------------QGLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 157 CETRAEWmiaaqtcfkynfpLVTLYAT--LGkeAVV-------------HGLNESEASYLITS--------VELLES--- 210
Cdd:PRK08315 75 APNVPEW-------------VLTQFATakIG--AILvtinpayrlseleYALNQSGCKALIAAdgfkdsdyVAMLYElap 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 211 --------KLKTALLdiSCVKHIIYVDnkainkAEYPEGFeiHSMQSVEELGSNPENLGIPPSRPT--PSDmAIVM-YTS 279
Cdd:PRK08315 140 elatcepgQLQSARL--PELRRVIFLG------DEKHPGM--LNFDELLALGRAVDDAELAARQATldPDD-PINIqYTS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 280 GSTGRPKGVMMHHSNLI--AGMTGQCERipgLGPKDTYIGYLPLAH----VLeltAEISCFTYGCRIGYssPLTLSDQSS 353
Cdd:PRK08315 209 GTTGFPKGATLTHRNILnnGYFIGEAMK---LTEEDRLCIPVPLYHcfgmVL---GNLACVTHGATMVY--PGEGFDPLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 354 KIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIqktLFKigyDYKLEQIKKGYDA-PLCNLLLFKKVKA 430
Cdd:PRK08315 281 TLAAVEEERCTALYgvPTMFIA-----------------ELDHP---DFA---RFDLSSLRTGIMAgSPCPIEVMKRVID 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 431 llggnvRMMLSGgaplspqthrfmnVCFCcpigqgYGLTESCGAGTVTEVTD-----YTTgrVGAPLICCEIKLKDwQEG 505
Cdd:PRK08315 338 ------KMHMSE-------------VTIA------YGMTETSPVSTQTRTDDplekrVTT--VGRALPHLEVKIVD-PET 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 506 GYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK08315 390 GETV--PRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDADG--WMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
263-618 |
1.92e-17 |
|
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: 85.79 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLA---HVLELTAEISCftyGCR 339
Cdd:cd17646 131 PLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYP-LGPGDRVLQKTPLSfdvSVWELFWPLVA---GAR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 340 IGYSSPLTLSDqsskikkgskgdctvlkptlMAAVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykLEQIKKGYDAPL 419
Cdd:cd17646 207 LVVARPGGHRD--------------------PAYLAALIREHGVTTCHFVPSM---------------LRVFLAEPAAGS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 420 CnlllfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTEscgagTVTEVTDYT-TGRVGAPLIccEI 497
Cdd:cd17646 252 C-------------ASLRRVFCSGEALPPELaARFLAL-PGAELHNLYGPTE-----AAIDVTHWPvRGPAETPSV--PI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 498 KLKDWQEGGYTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDR 570
Cdd:cd17646 311 GRPVPNTRLYVLDDALRPVpvgvpGELYLGGVQLARGYLGRPALTAERFVPDpfGPGSRMYRTGDLARWRPDGALEFLGR 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 530422004 571 KKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd17646 391 SDDQVKIR-GFRVEPGEIEAALAAHPAVTHAVVVARAAPAgaaRLVGYVVP 440
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
271-618 |
2.22e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 86.09 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI-----GYSS 344
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYHGHGLIAALlATLASGGAVllparGRFS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 345 PLTLSDqsskikkgskgDCTVLKPTLMAAVPeimdriyknvmskvqemnyiqkTLFKIGYDYKLEQIKKGYDAPLcnlll 424
Cdd:PRK05852 256 AHTFWD-----------DIKAVGATWYTAVP----------------------TIHQILLERAATEPSGRKPAAL----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 fkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY--------TTGRVG---APLI 493
Cdd:PRK05852 298 ------------RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIgqtenpvvSTGLVGrstGAQI 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 494 ccEIKLKDWQEGGytindkPNPRGEIVIGGQNISMGYFKNEEKTAEDYSvdeNGqrWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PRK05852 366 --RIVGSDGLPLP------AGAVGEVWLRGTTVVRGYLGDPTITAANFT---DG--WLRTGDLGSLSAAGDLSIRGRIKE 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 530422004 574 LVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 618
Cdd:PRK05852 433 LIN-RGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
263-624 |
3.88e-17 |
|
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: 85.09 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPL---AHVLELtaeiscFTYGCr 339
Cdd:cd17651 129 PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS-LGPGARTLQFAGLgfdVSVQEI------FSTLC- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 340 igysspltlsdqsskikkgsKGDCTVLKP--------TLMAAVPEimdriyknvmskvqemnyiqktlfkigydYKLEQI 411
Cdd:cd17651 201 --------------------AGATLVLPPeevrtdppALAAWLDE-----------------------------QRISRV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 412 kkgyDAP---LCNLLLFKKVKALLGGNVRMMLSGGAPLS--------PQTHRFMNVCFccpigqGYGLTESCGAgTVTEV 480
Cdd:cd17651 232 ----FLPtvaLRALAEHGRPLGVRLAALRYLLTGGEQLVltedlrefCAGLPGLRLHN------HYGPTETHVV-TALSL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 481 TDYTTGR-----VGAPLICCEIKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVDE--NGQRW 550
Cdd:cd17651 301 PGDPAAWpapppIGRPIDNTRVYVLD-------AALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPfvPGARM 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422004 551 FCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQsyvisfvvPNQKRLT 624
Cdd:cd17651 374 YRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALARHPGVREAVVLAREDR--------PGEKRLV 438
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
118-700 |
3.91e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 84.98 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 118 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESE 197
Cdd:PRK08316 30 LVFGDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 198 ASYLITSVELLEskLKTALLDISCVKHIIYVDnkAINKAEYPEGFeiHSMQSVEELGSNPEnlgiPPSRPTPSDMAIVMY 277
Cdd:PRK08316 109 ARAFLVDPALAP--TAEAALALLPVDTLILSL--VLGGREAPGGW--LDFADWAEAGSVAE----PDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 278 TSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvlelTAEISCFTygcrigysSPLTLSDQSSKIkk 357
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVS-CIVAGDMSADDIPLHALPLYH----CAQLDVFL--------GPYLYVGATNVI-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 358 gskgdctVLKPTLmaavPEIMDRIYKnvmskvqemnYIQKTLFK-----IG------YD-YKLEQIKKGYdaplcnlllf 425
Cdd:PRK08316 244 -------LDAPDP----ELILRTIEA----------ERITSFFApptvwISllrhpdFDtRDLSSLRKGY---------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 426 kkvkallggnvrmmlsGGAPLSPQT------HRFMNVCF--CcpigqgYGLTESCGAGTV--TEVTDYTTGRVGAPLICC 495
Cdd:PRK08316 293 ----------------YGASIMPVEvlkelrERLPGLRFynC------YGQTEIAPLATVlgPEEHLRRPGSAGRPVLNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 496 EIKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKK 572
Cdd:PRK08316 351 ETRVVD-------DDGNDVAPgevGEIVHRSPQLMLGYWDDPEKTAEAF---RGG--WFHSGDLGVMDEEGYITVVDRKK 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 573 DLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqqkgVEGTWVDicnnpamEAEI 649
Cdd:PRK08316 419 DMIK-TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWieaVTAVVVP-------------KAGATVT-------EDEL 477
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 530422004 650 LKEIREaanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHY 700
Cdd:PRK08316 478 IAHCRA-----RLAGFKVPKRVIFVDElPRNP-SG------KILKRELRERY 517
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
126-620 |
5.01e-17 |
|
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: 84.51 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLESkLKTALLDISCVKHIIyvdnkAINKAEYPEgfeihsMQSVEELGSNPEnlGIPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:TIGR02262 111 ALLPV-IKAALGKSPHLEHRV-----VVGRPEAGE------VQLAELLATESE--QFKPAATQADDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLsdqsskikkgskGDCTV 365
Cdd:TIGR02262 177 KGVVHTHSNPYWTAELYARNTLGIREDDVC-----------FSAAKLFFAYGLGNALTFPMSV------------GATTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 lkptLMAAVPeIMDRIYKnvmskvqEMNYIQKTLFkigydykleqikkgYDAP--LCNLLLFKKVKALLGGNVRMMLSGG 443
Cdd:TIGR02262 234 ----LMGERP-TPDAVFD-------RLRRHQPTIF--------------YGVPtlYAAMLADPNLPSEDQVRLRLCTSAG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 444 APLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGGYTINDKPnprGEIVIGG 523
Cdd:TIGR02262 288 EALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG-DGGQDVADGEP---GELLISG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 524 QNISMGYFKNEEKTAEDYSVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICA 603
Cdd:TIGR02262 364 PSSATMYWNNRAKSRDTFQGE-----WTRSGDKYVRNDDGSYTYAGRTDDMLKV-SGIYVSPFEIESALIQHPAVLEAAV 437
|
490 500
....*....|....*....|
gi 530422004 604 FAKSDQSYVI---SFVVPNQ 620
Cdd:TIGR02262 438 VGVADEDGLIkpkAFVVLRP 457
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
134-697 |
5.96e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.85 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 134 RVNNFGSGLTALGLKPKNTIAIFC---ETRAEWMIAaqtcfkynfplVTLYAtlgkeAVVHGLNE----SEASYLITSVE 206
Cdd:PLN02860 41 GVLSLAAGLLRLGLRNGDVVAIAAlnsDLYLEWLLA-----------VACAG-----GIVAPLNYrwsfEEAKSAMLLVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 207 llesklKTAL-LDISCVKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGS--NPENL---GIPPSRPT----PSDMAIVM 276
Cdd:PLN02860 105 ------PVMLvTDETCSSWYEELQNDRLPSLMWQVFLESPSSSVFIFLNSflTTEMLkqrALGTTELDyawaPDDAVLIC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 277 YTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVleltaeiscftyGcriGYSSPLTLSdqsskik 356
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALIVQSLAKIA-IVGYGEDDVYLHTAPLCHI------------G---GLSSALAML------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 357 kgSKGDCTVLKPTLMA-AVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykleqikkgydapLCNLLLFKKVKALLGGN 435
Cdd:PLN02860 236 --MVGACHVLLPKFDAkAALQAIKQHNVTSMITVPAM--------------------------MADLISLTRKSMTWKVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 436 --VRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPL-ICCEIKLKDWQEGGYTIND 511
Cdd:PLN02860 288 psVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLqTVNQTKSSSVHQPQGVCVG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 512 KPNPRGEIVIG-------------GQNISMGYFKNEEKTAEDYSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQ 578
Cdd:PLN02860 368 KPAPHVELKIGldessrvgriltrGPHVMLGYWGQNSETASVLSNDG----WLDTGDIGWIDKAGNLWLIGRSNDRIK-T 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 579 AGEYVSLGKVEAALKNCPLIdnicafaksdqSYVISFVVPNQkRLT--LLAQQKGVEG-TWVDIcNNPAMEAEIL---KE 652
Cdd:PLN02860 443 GGENVYPEEVEAVLSQHPGV-----------ASVVVVGVPDS-RLTemVVACVRLRDGwIWSDN-EKENAKKNLTlssET 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 530422004 653 IREAANAMKLERFEIP--IKVRLSPEPWTpETGlvtdafKLKRKELR 697
Cdd:PLN02860 510 LRHHCREKNLSRFKIPklFVQWRKPFPLT-TTG------KIRRDEVR 549
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
268-624 |
6.76e-17 |
|
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: 83.99 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPlAHVLELTAEiscftygcrigyssPLT 347
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFS-NYVFDFFVE--------------QMT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LSDQSskikkgskGDCTVLKPTLMAAVPeimDRIYKnvmskvqemnYIQKTlfKIGYDYKLEQIKKGYDAPLCNLLlfkk 427
Cdd:cd17648 157 LALLN--------GQKLVVPPDEMRFDP---DRFYA----------YINRE--KVTYLSGTPSVLQQYDLARLPHL---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 428 vkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgagTVTE-VTDYTTGRVGAPLICCEIKLKDWqegg 506
Cdd:cd17648 210 ---------KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET----TVTNhKRFFPGDQRFDKSLGRPVRNTKC---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 507 YTIND--KPNP---RGEIVIGGQNISMGYFKNEEKTAEDY----------SVDENGQRWFCTGDIGEFHPDGCLQIIDRK 571
Cdd:cd17648 273 YVLNDamKRVPvgaVGELYLGGDGVARGYLNRPELTAERFlpnpfqteqeRARGRNARLYKTGDLVRWLPSGELEYLGRN 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530422004 572 KDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD--------QSYVISFVVPNQKRLT 624
Cdd:cd17648 353 DFQVKIR-GQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriQKYLVGYYLPEPGHVP 412
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
128-618 |
1.01e-16 |
|
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: 83.14 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAqtcfkynfplvtLYATLGkeavvhglneSEASYLItsvel 207
Cdd:cd12115 27 YAELNRRANRLAARLRAAGVGPESRVGVCLERTPD-LVVA------------LLAVLK----------AGAAYVP----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 lesklktalLDiscvkhiiyvdnkainkAEYPEgfeihsmqsvEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKG 287
Cdd:cd12115 79 ---------LD-----------------PAYPP----------ERLRFILEDAQARLVLTDPDDLAYVIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VMMHHSNLIAGMTGQCERIPglgpKDTyigylpLAHVLELTA---EISCF------TYGCRIGY-SSPLTLSDQSSKikk 357
Cdd:cd12115 123 VAIEHRNAAAFLQWAAAAFS----AEE------LAGVLASTSicfDLSVFelfgplATGGKVVLaDNVLALPDLPAA--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 358 gskgdCTVlkpTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQikkgyDAplcnlllfkkvkalLGGNVR 437
Cdd:cd12115 190 -----AEV---TLINTVPSAAAEL--------------------------LRH-----DA--------------LPASVR 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 438 MMLSGGAPLS----------PQTHRFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGRV--GAPLicceiklkdwqeG 505
Cdd:cd12115 217 VVNLAGEPLPrdlvqrlyarLQVERVVNL---------YGPSEDTTYSTVAPVPPGASGEVsiGRPL------------A 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 506 G---YTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:cd12115 276 NtqaYVLDRALQPVplgvpGELYIGGAGVARGYLGRPGLTAERFLPDpfGPGARLYRTGDLVRWRPDGLLEFLGRADNQV 355
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 530422004 576 KLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd12115 356 KVR-GFRIELGEIEAALRSIPGVREAVVVAIGDAAgerRLVAYIVA 400
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
262-598 |
1.16e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 83.32 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPPSRPTpsdmaIVMYTSGSTGRPKGVMMHHSNLIA-----GMTGQceripgLGPKDTYIGYLPLAHVLELTAEI-SCFT 335
Cdd:PRK09088 132 IPPERVS-----LILFTSGTSGQPKGVMLSERNLQQtahnfGVLGR------VDAHSSFLCDAPMFHIIGLITSVrPVLA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 336 YGCRI----GYSSPLTLsdqsskikkGSKGDCTvLKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykleQI 411
Cdd:PRK09088 201 VGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAF----------------------------RA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 412 KKGYDAplcnlllfkkvKALlgGNVRMMLSGGAPlSPQTHRFMNVCFCCPIGQGYGLTEscgAGTV------TEVTDYTT 485
Cdd:PRK09088 243 QPGFDA-----------AAL--RHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSE---AGTVfgmsvdCDVIRAKA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 486 GRVGAPLICCEIKLKDWQEggytiND-KPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGC 564
Cdd:PRK09088 306 GAAGIPTPTVQTRVVDDQG-----NDcPAGVPGELLLRGPNLSPGYWRRPQATAR--AFTGDG--WFRTGDIARRDADGF 376
|
330 340 350
....*....|....*....|....*....|....
gi 530422004 565 LQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLI 598
Cdd:PRK09088 377 FWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
249-711 |
1.41e-16 |
|
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: 83.64 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 249 SVEELGSNPENLGIPPSRP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKD-TYIGYLPLAHvl 325
Cdd:cd05921 142 SFAELAATPPTAAVDAAFAavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNH-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 326 eltaeiscfTYGCRIGYSspLTLSDQSS-KIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyiqkt 398
Cdd:cd05921 220 ---------TFGGNHNFN--LVLYNGGTlYIDDG--------KPmpggfeETLRNLREISPTVYFNV------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 399 lfKIGYDYKLEQIKKgyDAPLCNLLlFKkvkallggNVRMMLSGGAPLSPQT-------------HRFmnvcfccPIGQG 465
Cdd:cd05921 268 --PAGWEMLVAALEK--DEALRRRF-FK--------RLKLMFYAGAGLSQDVwdrlqalavatvgERI-------PMMAG 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 466 YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLkdwqeggYTINDKPnprgEIVIGGQNISMGYFKNEEKTAEdySVDE 545
Cdd:cd05921 328 LGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKY----EVRVKGPNVTPGYWRQPELTAQ--AFDE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 546 NGqrWFCTGDIGEF----HPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNC--PLIDNIcAFAKSDQSYVISFVVPN 619
Cdd:cd05921 395 EG--FYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRARAVAAcaPLVHDA-VVAGEDRAEVGALVFPD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 620 QKRLTLLAQqkgvegtwvdicNNPAMEAEILK--EIREAANAMkLERFE--------IPIKVRLSPEPWTPETGLVTDAF 689
Cdd:cd05921 472 LLACRRLVG------------LQEASDAEVLRhaKVRAAFRDR-LAALNgeatgsssRIARALLLDEPPSIDKGEITDKG 538
|
490 500
....*....|....*....|..
gi 530422004 690 KLKRKELRNHYLKDIERMYGGK 711
Cdd:cd05921 539 YINQRAVLERRAALVERLYADT 560
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-620 |
1.85e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.44 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLesklktALLDISCVKHIIYVDNKAINKAEYPEGFeihsmqsveelgsnpenlgiPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12467 618 HLL------AQLPVPAGLRSLCLDEPADLLCGYSGHN--------------------PEVALDPDNLAYVIYTSGSTGQP 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTV 365
Cdd:PRK12467 672 KGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTV 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LKptlmaAVPeimdriyknvmskvqemNYIQKTLfkigydykleqikkgyDAPLCNLLLfkKVKALLGGNVRMMLSGGAP 445
Cdd:PRK12467 751 LK-----IVP-----------------SHLQALL----------------QASRVALPR--PQRALVCGGEALQVDLLAR 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 446 ---LSPQThRFMNVcfccpigqgYGLTESCGAGTVTEVT----DYTTGRVGAPLICCEIKLKDWQeggytINDKPNP-RG 517
Cdd:PRK12467 791 vraLGPGA-RLINH---------YGPTETTVGVSTYELSdeerDFGNVPIGQPLANLGLYILDHY-----LNPVPVGvVG 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 518 EIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKN 594
Cdd:PRK12467 856 ELYIGGAGLARGYHRRPALTAERFVPDpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR-GFRIELGEIEARLLA 934
|
490 500
....*....|....*....|....*...
gi 530422004 595 CPLIDN--ICAFAKSDQSYVISFVVPNQ 620
Cdd:PRK12467 935 QPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
271-592 |
2.32e-16 |
|
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: 82.12 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsd 350
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRV-----------FSSAKMFFGYGLGNSLWFPL---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 351 qsskikkgSKGDCTVLKPTlmAAVPEimdriykNVMSKVQEMnyiQKTLFkigydykleqikkgYDAP--LCNLLLFKKV 428
Cdd:cd05919 157 --------AVGASAVLNPG--WPTAE-------RVLATLARF---RPTVL--------------YGVPtfYANLLDSCAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 429 KALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYT 508
Cdd:cd05919 203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD--EEGHT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 509 IndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKV 588
Cdd:cd05919 281 I--PPGEEGDLLVRGPSAAVGYWNNPEKSRATF----NGG-WYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEV 352
|
....
gi 530422004 589 EAAL 592
Cdd:cd05919 353 ESLI 356
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
266-624 |
3.10e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 82.41 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 266 RP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERI--PGLGP-KDTYIGYLPLAHVLELTaeISCFTYgcri 340
Cdd:PRK08974 200 KPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QAKAAygPLLHPgKELVVTALPLYHIFALT--VNCLLF---- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 341 gysspltlsdqsskIKKGSKGdctvLKPTLMAAVPEIMDRIYKNVMSKVQEMNyiqkTLFkigydykleqikkgydaplc 420
Cdd:PRK08974 273 --------------IELGGQN----LLITNPRDIPGFVKELKKYPFTAITGVN----TLF-------------------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 421 NLLL----FKKVKAllgGNVRMMLSGGAPL-SPQTHRFMNVCfCCPIGQGYGLTEsCG---AGTVTEVTDYTtGRVGAPL 492
Cdd:PRK08974 311 NALLnneeFQELDF---SSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTE-CSplvSVNPYDLDYYS-GSIGLPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 493 ICCEIKLKDwQEGgytiNDKPN-PRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRK 571
Cdd:PRK08974 385 PSTEIKLVD-DDG----NEVPPgEPGELWVKGPQVMLGYWQRPEATDE---VIKDG--WLATGDIAVMDEEGFLRIVDRK 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 572 KDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKRLT 624
Cdd:PRK08974 455 KDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLT 509
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
268-710 |
5.67e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 81.85 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPGLGPKdTYIGYLPLAHVLeltaeiscftygcriGYSSP 345
Cdd:PRK08180 207 GPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqMLAQTFPFLAEEPP-VLVDWLPWNHTF---------------GGNHN 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 346 LTLsdqsskikkgskgdctVL-----------KPTlmaavPEIMDRIYKNvmskvqeMNYIQKTLF---KIGYDYKLEQI 411
Cdd:PRK08180 271 LGI----------------VLynggtlyiddgKPT-----PGGFDETLRN-------LREISPTVYfnvPKGWEMLVPAL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 412 KKgyDAPLCNLLLfkkvkallgGNVRMMLSGGAPLSPQT----HRF-MNVC-----FCCpigqGYGLTESCGAGTVTEVT 481
Cdd:PRK08180 323 ER--DAALRRRFF---------SRLKLLFYAGAALSQDVwdrlDRVaEATCgerirMMT----GLGMTETAPSATFTTGP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 482 DYTTGRVGAPLICCEIKLKDwqEGGytindkpnpRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFH- 560
Cdd:PRK08180 388 LSRAGNIGLPAPGCEVKLVP--VGG---------KLEVRVKGPNVTPGYWRAPELTAE--AFDEEG--YYRSGDAVRFVd 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 561 PDgclqiiDRKKDLV---------KLQAGEYVSLG----KVEAALKncPLIDNICaFAKSDQSYVISFVVPNQKRLTLLA 627
Cdd:PRK08180 453 PA------DPERGLMfdgriaedfKLSSGTWVSVGplraRAVSAGA--PLVQDVV-ITGHDRDEIGLLVFPNLDACRRLA 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 628 QQkGVEGTWVDICNNPAMEA---EILKEIREAA--NAMKLERfeipikVRLSPEPWTPETGLVTDAFKLKRKELRNHYLK 702
Cdd:PRK08180 524 GL-LADASLAEVLAHPAVRAafrERLARLNAQAtgSSTRVAR------ALLLDEPPSLDAGEITDKGYINQRAVLARRAA 596
|
....*...
gi 530422004 703 DIERMYGG 710
Cdd:PRK08180 597 LVEALYAD 604
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
126-618 |
5.89e-16 |
|
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: 80.94 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsNPENLgippsrptpsdmAIVMYTSGSTGRP 285
Cdd:cd17644 104 --------------------------------------------------QPENL------------AYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDtyigylplaHVLELtaeiSCFTYGCRIGYSSPLTLSdqsskikkgskGDCTV 365
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEY-GITSSD---------RVLQF----ASIAFDVAAEEIYVTLLS-----------GATLV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LKPTLMAAVPEIMdriyknvmskvqeMNYIQK---TLFKIGYDYKLEQIKKGydaplcnlllfKKVKALLGGNVRMMLSG 442
Cdd:cd17644 177 LRPEEMRSSLEDF-------------VQYIQQwqlTVLSLPPAYWHLLVLEL-----------LLSTIDLPSSLRLVIVG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 443 GAPLSPQTH-----------RFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIKLKDWqegg 506
Cdd:cd17644 233 GEAVQPELVrqwqknvgnfiQLINV---------YGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILDE---- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 507 ytiNDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYSVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQa 579
Cdd:cd17644 300 ---NLQPVPvgvPGELHIGGVGLARGYLNRPELTAEKFISHpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIR- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 530422004 580 GEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd17644 376 GFRIELGEIEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVP 417
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
250-596 |
5.92e-16 |
|
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: 81.09 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 250 VEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERipGLGPKDTYIGYLPL---AHVLE 326
Cdd:cd12117 116 VIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV--TLGPDDRVLQTSPLafdASTFE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 327 LtaeiscftYGCRIgysspltlsdqsskikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSkvqemnyiqkTLFKIgydy 406
Cdd:cd12117 194 I--------WGALL------------------NGARLVLAPKGTLLDPDALGALIAEEGVT----------VLWLT---- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 407 kleqikkgydAPLCNLLLFKKVKALLGgnVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DY 483
Cdd:cd12117 234 ----------AALFNQLADEDPECFAG--LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTelDE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 484 TTGRV--GAPLICCEIKLKDwqEGGytindKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDI 556
Cdd:cd12117 302 VAGSIpiGRPIANTRVYVLD--EDG-----RPVPPgvpGELYVGGDGLALGYLNRPALTAERFVADpfGPGERLYRTGDL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530422004 557 GEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCP 596
Cdd:cd12117 375 ARWLPDGRLEFLGRIDDQVKIR-GFRIELGEIEAALRAHP 413
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
124-575 |
1.02e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 80.85 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 124 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL-- 201
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlc 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ----------ITSVELLESKLKTALLD-ISCVKHIIY--VDNKAINK-AEYPEGFEIHSMQSVE-------ELGSNPENl 260
Cdd:PRK06710 128 ldlvfprvtnVQSATKIEHVIVTRIADfLPFPKNLLYpfVQKKQSNLvVKVSESETIHLWNSVEkevntgvEVPCDPEN- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 261 gippsrptpsDMAIVMYTSGSTGRPKGVMMHHSNLIAG-MTGQCERIPGLGPKDTYIGYLPLAHVLELTAEIS-CFTYGC 338
Cdd:PRK06710 207 ----------DLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNlSIMQGY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 339 RIGYSSPLTLSDQSSKIKKGskgdctvlKPTLMAAVPEImdriyknvmskvqemnYIQktlfkigydykleqikkgydap 418
Cdd:PRK06710 277 KMVLIPKFDMKMVFEAIKKH--------KVTLFPGAPTI----------------YIA---------------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 419 LCNLLLFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT----DYTTGRVGAPLIC 494
Cdd:PRK06710 311 LLNSPLLKEYDI---SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES---SPVTHSNflweKRVPGSIGVPWPD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 495 CEIKLKDWQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAedySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDL 574
Cdd:PRK06710 385 TEAMIMSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETA---AVLQDG--WLHTGDVGYMDEDGFFYVKDRKKDM 456
|
.
gi 530422004 575 V 575
Cdd:PRK06710 457 I 457
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
268-697 |
1.20e-15 |
|
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: 80.10 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCE---RIPGLGPKDTYIGYLPL---AHVLELTAEISCftygcrig 341
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQataERYGLTPGDRELQFASFnfdGAHEQLLPPLIC-------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 342 ysspltlsdqsskikkgskGDCTVLKP-TLMAAVPEIMDRIYKNVMSKVQemnyiqktlFKIGYDYKLeqikkgydaplc 420
Cdd:cd17649 160 -------------------GACVVLRPdELWASADELAEMVRELGVTVLD---------LPPAYLQQL------------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 421 nLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLicc 495
Cdd:cd17649 200 -AEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLF-NAYGPTEATVTPLVWKCEAGAARAgasmpIGRPL--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 496 eiklkdwqeGGYT--INDK------PNPRGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGC 564
Cdd:cd17649 275 ---------GGRSayILDAdlnpvpVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgAPGSRLYRTGDLARWRDDGV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 565 LQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS--YVISFVVPNQkrltllaqqkgvegtwvdicnn 642
Cdd:cd17649 346 IEYLGRVDHQVKIR-GFRIELGEIEAALLEHPGVREAAVVALDGAGgkQLVAYVVLRA---------------------- 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 643 PAMEAEILKEIReAANAMKLERFEIPIK-VRLSPEPWTPETglvtdafKLKRKELR 697
Cdd:cd17649 403 AAAQPELRAQLR-TALRASLPDYMVPAHlVFLARLPLTPNG-------KLDRKALP 450
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
269-575 |
1.73e-15 |
|
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: 79.84 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcriGYSSPLTl 348
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE-WKTKDRILSWMPLTHDMGLIA-----------FHLAPLI- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 349 sdqsskikkgsKGDCTVLKPTLMAAVPEImdriykNVMSKVQEMNYIQKTLFKIGYDYKLEQIK--KGYDAPLcnlllfk 426
Cdd:cd05908 172 -----------AGMNQYLMPTRLFIRRPI------LWLKKASEHKATIVSSPNFGYKYFLKTLKpeKANDWDL------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 427 kvkallgGNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQG-----YGLTE-SCGA---------------------GTVT 478
Cdd:cd05908 228 -------SSIRMILNGAEPIDYElCHEFLDHMSKYGLKRNailpvYGLAEaSVGAslpkaqspfktitlgrrhvthGEPE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 479 EVTD------YTTGRVGAPLICCEIKLKDWQ----EGGYTindkpnprGEIVIGGQNISMGYFKNEEKTAEDYSVDEngq 548
Cdd:cd05908 301 PEVDkkdsecLTFVEVGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEATAKVFTDDG--- 369
|
330 340
....*....|....*....|....*..
gi 530422004 549 rWFCTGDIGeFHPDGCLQIIDRKKDLV 575
Cdd:cd05908 370 -WLKTGDLG-FIRNGRLVITGREKDII 394
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
277-697 |
4.15e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 78.73 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 277 YTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHvleltAEISCFTYGCRIGYSSPLTLSDQSSKIK 356
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYL-MALSNALIWGMNEGAVYLWTLPMFH-----CNGWCFTWTLAALCGTNICLRQVTAKAI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 357 KGSKGDCTVlkpTLMAAVPEIMDRIyknVMSKVQEmnyiqkTLFkigydykleqikkgydaPLCNLllfkkvkallggnV 436
Cdd:PLN02479 276 YSAIANYGV---THFCAAPVVLNTI---VNAPKSE------TIL-----------------PLPRV-------------V 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 437 RMMLSGGAP-------LSPQTHRfmnvcfccpIGQGYGLTESCGAGTV-----------TEVTDYTTGRVGAPLICCE-I 497
Cdd:PLN02479 314 HVMTAGAAPppsvlfaMSEKGFR---------VTHTYGLSETYGPSTVcawkpewdslpPEEQARLNARQGVRYIGLEgL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 498 KLKDWQEGgytindKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKK 572
Cdd:PLN02479 385 DVVDTKTM------KPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF---ANG--WFHSGDLGVKHPDGYIEIKDRSK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 573 DLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS---FVVPNQKrltllaqqkgvegtwVDICNNPAMEAEI 649
Cdd:PLN02479 454 DII-ISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESpcaFVTLKPG---------------VDKSDEAALAEDI 517
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 530422004 650 LKEIREaanamKLERFEIPIKVRLSPEPWTPeTGlvtdafKLKRKELR 697
Cdd:PLN02479 518 MKFCRE-----RLPAYWVPKSVVFGPLPKTA-TG------KIQKHVLR 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-619 |
4.44e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.82 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLESklktalLDISCVKHIIYVDNKAINKAEYPEgfeihsmqsveelgSNPENlgippsRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12467 1680 HLQAR------LPLPDGLRSLVLDQEDDWLEGYSD--------------SNPAV------NLAPQNLAYVIYTSGSTGRP 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaEISCFtygcriGYSSPLTlsdqsskikkgsKGDCTV 365
Cdd:PRK12467 1734 KGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAF------DVSVW------ELFWPLI------------NGARLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LKPTLMAAVPE-IMDRIYKN-VMSKVQEMNYIQktlfkigydyKLEQIKKGYDAPLcnlllfkkvkallggNVRMMLSGG 443
Cdd:PRK12467 1789 IAPPGAHRDPEqLIQLIERQqVTTLHFVPSMLQ----------QLLQMDEQVEHPL---------------SLRRVVCGG 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 444 APLSPQTHR-FMNVCFCCPIGQGYGLTEscgagTVTEVTDYT------TGRVGAPLiccEIKLKDWqeGGYTINDKPNPR 516
Cdd:PRK12467 1844 EALEVEALRpWLERLPDTGLFNLYGPTE-----TAVDVTHWTcrrkdlEGRDSVPI---GQPIANL--STYILDASLNPV 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 517 -----GEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 588
Cdd:PRK12467 1914 pigvaGELYLGGVGLARGYLNRPALTAERFVADpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEI 1992
|
490 500 510
....*....|....*....|....*....|...
gi 530422004 589 EAALKNCPLIDNICAFAK--SDQSYVISFVVPN 619
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQdgANGKQLVAYVVPT 2025
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
263-592 |
2.63e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.80 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltaeiscftYGCRIGY 342
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW-QWTADDVLVHGLPLFHV-----------HGLVLGV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 343 SSPLTLSDQSSKIKKGSK---GDCTVLKPTLMAAVPEIMDRIYKNVmskvqemnyiqktlfkigydykleqikkgyDAPl 419
Cdd:PRK07787 189 LGPLRIGNRFVHTGRPTPeayAQALSEGGTLYFGVPTVWSRIAADP------------------------------EAA- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 420 cnlllfkkvKALlgGNVRMMLSGGAPLS-PQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIK 498
Cdd:PRK07787 238 ---------RAL--RGARLLVSGSAALPvPVFDRLAALTGHRPV-ERYGMTETLITLSTRADGERRPGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 499 LKDwqEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKK-DLVKl 577
Cdd:PRK07787 306 LVD--EDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAA--AFTADG--WFRTGDVAVVDPDGMHRIVGREStDLIK- 378
|
330
....*....|....*.
gi 530422004 578 qAGEY-VSLGKVEAAL 592
Cdd:PRK07787 379 -SGGYrIGAGEIETAL 393
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
269-610 |
2.75e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 76.67 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTaeISCFT---YGCRIG-YSS 344
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFGLT--VGLFTpllTGAEVFlYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 345 PL-------TLSDQsskikkgskgDCTVL--KPTLMAavpeimdriyknvmskvqemNYIQktlFKIGYDYkleqikkgy 415
Cdd:PRK08043 441 PLhyrivpeLVYDR----------NCTVLfgTSTFLG--------------------NYAR---FANPYDF--------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 416 daplcnlllfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-----------SCGAGTVTEVTDYT 484
Cdd:PRK08043 479 ------------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEcapvvsinvpmAAKPGTVGRILPGM 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 485 TGRVgaplicceIKLKDWQEGgytindkpnprGEIVIGGQNISMGYFKNEE------KTAEdysvDENGQR---WFCTGD 555
Cdd:PRK08043 541 DARL--------LSVPGIEQG-----------GRLQLKGPNIMNGYLRVEKpgvlevPTAE----NARGEMergWYDTGD 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 556 IGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEA-ALKNCPLIDNiCAFAKSDQS 610
Cdd:PRK08043 598 IVRFDEQGFVQIQGRAKRFAKI-AGEMVSLEMVEQlALGVSPDKQH-ATAIKSDAS 651
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-630 |
2.91e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLEsklktallDISCvkhiiyvdnkainkaeyPEGFEIHSMQSVEELGSNPEnlGIPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 2109 HLLE--------RLPL-----------------PAGVARLPLDRDAEWADYPD--TAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTlsdqsskikkgsKGDCTV 365
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS--FDGAHE-QWFH---------PLL------------NGARVL 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LKPTLMAAVPEIMDRIYKNVMSKVqemnyiqktlfkigydykleqikkgyDAPLCNLLLFKKVKALLGG--NVRMMLSGG 443
Cdd:PRK12316 2217 IRDDELWDPEQLYDEMERHGVTIL--------------------------DFPPVYLQQLAEHAERDGRppAVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 444 ----APLSPQTHRFMNVCFccpIGQGYGLTEscgagTVTEVTDYTTGRV---GAPLICCEIKLKDwqEGGYTINDKPNP- 515
Cdd:PRK12316 2271 eavpAASLRLAWEALRPVY---LFNGYGPTE-----AVVTPLLWKCRPQdpcGAAYVPIGRALGN--RRAYILDADLNLl 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 516 ----RGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 588
Cdd:PRK12316 2341 apgmAGELYLGGEGLARGYLNRPGLTAERFVPDpfsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR-GFRIELGEI 2419
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 530422004 589 EAALKNCPLIDNICAFAKSDQS--YVISFVVPNQKRLTLLAQQK 630
Cdd:PRK12316 2420 EARLQAHPAVREAVVVAQDGASgkQLVAYVVPDDAAEDLLAELR 2463
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
130-697 |
3.16e-14 |
|
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: 75.55 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 130 EVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVelle 209
Cdd:cd05971 11 ELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 210 sklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptPSDMAIVMYTSGSTGRPKGVM 289
Cdd:cd05971 87 -----------------------------------------------------------SDDPALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 290 MHHSNLIaGMTGQCERIPGLGPKDTYIGYLPlahvleltAEISCftygcrIGysspltlsdqsskikkgskGDCTVLKPT 369
Cdd:cd05971 108 HAHRVLL-GHLPGVQFPFNLFPRDGDLYWTP--------ADWAW------IG-------------------GLLDVLLPS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 370 LMAAVPEIMDRIYKnvmskvqemnYIQKTLFKIGYDYKLEQIKkgydAPLCNLLLFKKVKALL---GGNVRMMLSGGAPL 446
Cdd:cd05971 154 LYFGVPVLAHRMTK----------FDPKAALDLMSRYGVTTAF----LPPTALKMMRQQGEQLkhaQVKLRAIATGGESL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 447 SPQTHRFMNVCFCCPIGQGYGLTEsCGA--GTVTEVTDYTTGRVGAPLICCEIKLkdwqeggytINDK-----PNPRGEI 519
Cdd:cd05971 220 GEELLGWAREQFGVEVNEFYGQTE-CNLviGNCSALFPIKPGSMGKPIPGHRVAI---------VDDNgtplpPGEVGEI 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 520 VIGGQNISM--GYFKNEEKTAEDYSVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPL 597
Cdd:cd05971 290 AVELPDPVAflGYWNNPSATEKKMAGD-----WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPA 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 598 IDNICAFAKSDQ---SYVISFVVPNQkrltllaqqkGVEGTwvdicnnpameAEILKEIREAANAmKLERFEIPIKVRLS 674
Cdd:cd05971 364 VLMAAVVGIPDPirgEIVKAFVVLNP----------GETPS-----------DALAREIQELVKT-RLAAHEYPREIEFV 421
|
570 580
....*....|....*....|...
gi 530422004 675 PEPWTPETGlvtdafKLKRKELR 697
Cdd:cd05971 422 NELPRTATG------KIRRRELR 438
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
126-618 |
3.72e-14 |
|
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: 75.37 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrpTPSDMAIVMYTSGSTGRP 285
Cdd:cd17652 91 --------------------------------------------------------------TPDNLAYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAeisCFTYGCR--IGYSSPLTLSDQSSKIKKGSK 360
Cdd:cd17652 109 KGVVVTHRGLANLAAAQIAAF-DVGPGSRVLQFASPsfdASVWELLM---ALLAGATlvLAPAEELLPGEPLADLLREHR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 361 GDCTVLKPTLMAAVPEimdriyknvmskvqemnyiqktlfkigydykleqikkgydaplcnlllfkkvKALLGGnvRMML 440
Cdd:cd17652 185 ITHVTLPPAALAALPP----------------------------------------------------DDLPDL--RTLV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 441 SGGAPLSPQ-------THRFMNvcfccpigqGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIK-LKDWQEggytind 511
Cdd:cd17652 211 VAGEACPAElvdrwapGRRMIN---------AYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYvLDARLR------- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 512 kPNP---RGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 585
Cdd:cd17652 275 -PVPpgvPGELYIAGAGLARGYLNRPGLTAERFVADpfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIR-GFRIEL 352
|
490 500 510
....*....|....*....|....*....|....*.
gi 530422004 586 GKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP 618
Cdd:cd17652 353 GEVEAALTEHPGVAEAVVVVRDDRPGDkrlVAYVVP 388
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
128-608 |
3.95e-14 |
|
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: 75.23 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 207
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 LEsklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsRPTPSDMAIVMYTSGSTGRPKG 287
Cdd:cd05969 83 YE--------------------------------------------------------RTDPEDPTLLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VMMHHSNLIA-GMTGQceRIPGLGPKDTYIgylplahvleLTAEISCFTyGCRIGYSSPLTLSdqsskikkgskgdCTVL 366
Cdd:cd05969 107 VLHVHDAMIFyYFTGK--YVLDLHPDDIYW----------CTADPGWVT-GTVYGIWAPWLNG-------------VTNV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 367 kptlmaavpeimdriyknvmskVQEMNYIQKTLFKIGYDYKleqIKKGYDAPLCNLLLFKKVKALLG----GNVRMMLSG 442
Cdd:cd05969 161 ----------------------VYEGRFDAESWYGIIERVK---VTVWYTAPTAIRMLMKEGDELARkydlSSLRFIHSV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 443 GAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIKLKDwQEGGYTindKPNPRGEIVI 521
Cdd:cd05969 216 GEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVD-ENGNEL---PPGTKGILAL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 522 GGQNISM--GYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLID 599
Cdd:cd05969 292 KPGWPSMfrGIWNDEERYKNSF---IDG--WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAVA 365
|
....*....
gi 530422004 600 NICAFAKSD 608
Cdd:cd05969 366 EAGVIGKPD 374
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
269-618 |
5.82e-14 |
|
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: 74.51 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIagmtGQCEripglgpkdtyigylplahvleltAEISCFTygcrigysspLTL 348
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCE------------------------WHRPYFG----------VTP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 349 SDQSSKIKkGSKGDCTVLK--PTLMA-AVPEIMDRIYKNVMSKVQEmnYIQKTLFKIGYdykleqikkgYDAPLCnlllf 425
Cdd:cd17645 145 ADKSLVYA-SFSFDASAWEifPHLTAgAALHVVPSERRLDLDALND--YFNQEGITISF----------LPTGAA----- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 426 KKVKALLGGNVRMMLSGGAPLSpqthRFMNVCFccPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIklkdwqe 504
Cdd:cd17645 207 EQFMQLDNQSLRVLLTGGDKLK----KIERKGY--KLVNNYGPTENTVVATSFEIdKPYANIPIGKPIDNTRV------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 505 ggYTIND----KP-NPRGEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 577
Cdd:cd17645 274 --YILDEalqlQPiGVAGELCIAGEGLARGYLNRPELTAEKFIVHpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530422004 578 QaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVP 618
Cdd:cd17645 352 R-GYRIEPGEIEPFLMNHPLIELAAVLAKEDadgRKYLVAYVTA 394
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-631 |
6.28e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.97 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLESklktalLDISCVKHIIYVDNKAINKaeYPEgfeihsmqsveelgSNPENlgippsRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12467 3201 HLLEQ------LPAPAGDTALTLDRLDLNG--YSE--------------NNPST------RVMGENLAYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 286 KGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAhvLELTAEISCFTYGCrigysspltlsdqsskikkgskGDCTV 365
Cdd:PRK12467 3253 KGVGVRHGAL-ANHLCWIAEAYELDANDRVLLFMSFS--FDGAQERFLWTLIC----------------------GGCLV 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 366 LKPTLMAAvPEimdriyknvmSKVQEMNYiqktlfkigydyklEQIKKGYDAP--LCNLLLFKKVKAllGGNVRMMLSGG 443
Cdd:PRK12467 3308 VRDNDLWD-PE----------ELWQAIHA--------------HRISIACFPPayLQQFAEDAGGAD--CASLDIYVFGG 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 444 APLSPQT-----HRFMNVCfccpIGQGYGLTEscgagTVTEVTDYTTGRVGAP-LICCEIKLKDWQEGGYTINDKPNP-- 515
Cdd:PRK12467 3361 EAVPPAAfeqvkRKLKPRG----LTNGYGPTE-----AVVTVTLWKCGGDAVCeAPYAPIGRPVAGRSIYVLDGQLNPvp 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 516 ---RGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 589
Cdd:PRK12467 3432 vgvAGELYIGGVGLARGYHQRPSLTAERFVADpfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIE 3510
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 530422004 590 AALKNCPLIDNICAFAKSDQS--YVISFVVPNQKRLTLLAQQKG 631
Cdd:PRK12467 3511 ARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQGDWRETLRD 3554
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
250-611 |
1.09e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 74.43 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 250 VEELGSNPENLGIPPSRPtpsdmAIVMYTSGSTGRPKGVMMHHSNLiAGMTGQCERIPGLGPKDTyIGYL--PLAHVLEL 327
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSP-----ALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADINSD-VGFVgvPLFHIAGI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 328 TAEISCFTYGCRigysspltlsdqsskikkgskgdcTVLKPTLMAAVPEIMDriyknvmskVQEMNYIQkTLFKIGYDYK 407
Cdd:PRK07786 232 GSMLPGLLLGAP------------------------TVIYPLGAFDPGQLLD---------VLEAEKVT-GIFLVPAQWQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 408 L---EQIKKGYDAPLcnlllfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFccPIGQ---GYGLTEscgAGTVTEVT 481
Cdd:PRK07786 278 AvcaEQQARPRDLAL-----------------RVLSWGAAPASDTLLRQMAATF--PEAQilaAFGQTE---MSPVTCML 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 482 D-----YTTGRVGAPLICCEIKLKDwqeggYTIND-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGD 555
Cdd:PRK07786 336 LgedaiRKLGSVGKVIPTVAARVVD-----ENMNDvPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---AGG--WFHSGD 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 556 IGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY 611
Cdd:PRK07786 406 LVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW 460
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
262-592 |
3.13e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 72.74 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPPSRPTPSDMAIVM------------YTSGSTGRPKGVMMHH--------SNLIAGMTGQCEripglgpkdTYIGYLPL 321
Cdd:PLN03102 166 IQRGEPTPSLVARMFriqdehdpislnYTSGTTADPKGVVISHrgaylstlSAIIGWEMGTCP---------VYLWTLPM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 322 AHVLELTaeiscFTYGCrigysspltlsdqsskikkGSKGDCTVLKPTLMAavPEImdriYKNV-MSKVQEMNYIqKTLF 400
Cdd:PLN03102 237 FHCNGWT-----FTWGT-------------------AARGGTSVCMRHVTA--PEI----YKNIeMHNVTHMCCV-PTVF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 401 KIgydykleqIKKGYDAPLCNLllfkkvkallGGNVRMMLSGGAPLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEV 480
Cdd:PLN03102 286 NI--------LLKGNSLDLSPR----------SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEW 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 481 TD-----------YTTGRVGAP-LICCEIKLKDwqeggyTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSv 543
Cdd:PLN03102 346 QDewnrlpenqqmELKARQGVSiLGLADVDVKN------KETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAFK- 418
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530422004 544 dengQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAAL 592
Cdd:PLN03102 419 ----HGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVL 462
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
270-617 |
7.41e-13 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 70.37 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLE-------LTAEISCFTYGCRIGY 342
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiltcLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 343 SSPLtlsdqssKIKKGSKGDCTVLKPTLMAAVPEImdriYKNVMSKVQEMNYIQktlfkIGYDYKLEQikkgydaplcnl 422
Cdd:cd17635 81 KSLF-------KILTTNAVTTTCLVPTLLSKLVSE----LKSANATVPSLRLIG-----YGGSRAIAA------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 423 llfKKVKALLGGNVRmmlsggaplspqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKD 501
Cdd:cd17635 133 ---DVRFIEATGLTN------------------------TAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 502 wQEGGYTINDKpnpRGEIVIGGQNISMGYFKNEEKTAEDYsVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGE 581
Cdd:cd17635 186 -TDGIAGPSAS---FGTIWIKSPANMLGYWNNPERTAEVL-IDG----WVNTGDLGERREDGFLFITGRSSESIN-CGGV 255
|
330 340 350
....*....|....*....|....*....|....*....
gi 530422004 582 YVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 617
Cdd:cd17635 256 KIAPDEVERIAEGVSGVQECACYEISDEEFgelVGLAVV 294
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
268-659 |
1.01e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 71.23 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNL---IAGMTGQCERIPGLGPKDtYIGYLPLAHvleltaeiscfTYGCRIGYSs 344
Cdd:PRK12582 218 TPDTVAKYLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPV-SLDWMPWNH-----------TMGGNANFN- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 345 PLTLSDQSSKIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyiqktlfKIGYDYKLEQIKKgyDAP 418
Cdd:PRK12582 285 GLLWGGGTLYIDDG--------KPlpgmfeETIRNLREISPTVYGNV---------------PAGYAMLAEAMEK--DDA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 419 LCNLLlFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQ------GYGLTEScgAGTVTEVTDYT--TGRVGA 490
Cdd:PRK12582 340 LRRSF-FK--------NLRLMAYGGATLSDDLYERMQALAVRTTGHripfytGYGATET--APTTTGTHWDTerVGLIGL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 491 PLICCEIKLKdwqeggytindkpnPRG---EIVIGGQNISMGYFKNEEKTAEDYsvDENGqrWFCTGDIGEF-HPDGCLQ 566
Cdd:PRK12582 409 PLPGVELKLA--------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAF--DEEG--FYRLGDAARFvDPDDPEK 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 567 --IID-RKKDLVKLQAGEYVSLGKVEA-ALKNC-PLIDNIcAFAKSDQSYVISFVVPNQKRLTLLAqqKGVEGTWVDICN 641
Cdd:PRK12582 471 glIFDgRVAEDFKLSTGTWVSVGTLRPdAVAACsPVIHDA-VVAGQDRAFIGLLAWPNPAACRQLA--GDPDAAPEDVVK 547
|
410
....*....|....*...
gi 530422004 642 NPAMeAEILKEIREAANA 659
Cdd:PRK12582 548 HPAV-LAILREGLSAHNA 564
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
128-297 |
1.01e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 71.08 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKyNFPLVT-LYATLGKEAVVHGLNESEASYLITSVE 206
Cdd:PRK04319 76 YKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALK-NGAIVGpLFEAFMEEAVRDRLEDSEAKVLITTPA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 207 LLESKLKTallDISCVKHIIYVDNKAinkaEYPEGFeihsMQSVEELGSNPENLGIPPSrpTPSDMAIVMYTSGSTGRPK 286
Cdd:PRK04319 155 LLERKPAD---DLPSLKHVLLVGEDV----EEGPGT----LDFNALMEQASDEFDIEWT--DREDGAILHYTSGSTGKPK 221
|
170
....*....|.
gi 530422004 287 GVMMHHSNLIA 297
Cdd:PRK04319 222 GVLHVHNAMLQ 232
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-608 |
1.41e-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: 69.82 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVL-ELTAEISCFTYGCRIGYSSPLT 347
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVY-NAWMLALNSLFDPDDVLLCGLPLFHVNgSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LSDqsskikKGSKGDCTVL----KPTLMAAVPEIMDriyknvmskvqemnyiqktlfkigydyKLEQIKKGYDAplcnll 423
Cdd:cd05944 80 YRN------PGLFDNFWKLveryRITSLSTVPTVYA---------------------------ALLQVPVNADI------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 424 lfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-SCGAGTVTEVTDYTTGRVGAPLICCEIKLKDW 502
Cdd:cd05944 121 ----------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 503 QEGGYTIND-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 581
Cdd:cd05944 191 DGVGRLLRDcAPDEVGEICVAGPGVFGGYLYTEGNKNAFV-----ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGH 264
|
330 340
....*....|....*....|....*..
gi 530422004 582 YVSLGKVEAALKNCPLIDNICAFAKSD 608
Cdd:cd05944 265 NIDPALIEEALLRHPAVAFAGAVGQPD 291
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
144-608 |
1.89e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 70.37 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 144 ALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGKEAVV-------------HGLNESEASYLITSVELLEs 210
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAY-------------YAILRANAVVvpvnpmnreeelaHYVTDSGARVAIVGSELAP- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 211 KLKTALLDIScVKHII------YVDNKAINKAeyPEGFEI-HSMQSVEELGSNP------ENLGIPPSRPTPSDMAIVMY 277
Cdd:PRK08314 121 KVAPAVGNLR-LRHVIvaqysdYLPAEPEIAV--PAWLRAePPLQALAPGGVVAwkealaAGLAPPPHTAGPDDLAVLPY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 278 TSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLeltaeiscftyGCRIGYSSPLTLsdqsskikk 357
Cdd:PRK08314 198 TSGTTGVPKGCMHTHRTVMANAVGSV-LWSNSTPESVVLAVLPLFHVT-----------GMVHSMNAPIYA--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 358 gskGDCTVLKPTL-MAAVPEIMDRiyknvmSKVQEMNYIQKTLFKIGYDYKLEQikkgYDapLCNLllfkkvkALLGGnv 436
Cdd:PRK08314 257 ---GATVVLMPRWdREAAARLIER------YRVTHWTNIPTMVVDFLASPGLAE----RD--LSSL-------RYIGG-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 437 rmmlsGGAPLsPQT-----HRFMNVCFCcpigQGYGLTEScGAGTVTEVTDYTTGR-VGAPLICCEIKLKDWQEGgytIN 510
Cdd:PRK08314 313 -----GGAAM-PEAvaerlKELTGLDYV----EGYGLTET-MAQTHSNPPDRPKLQcLGIPTFGVDARVIDPETL---EE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 511 DKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEA 590
Cdd:PRK08314 379 LPPGEVGEIVVHGPQVFKGYWNRPEATAEAF-IEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVEN 456
|
490
....*....|....*...
gi 530422004 591 ALKNCPLIDNICAFAKSD 608
Cdd:PRK08314 457 LLYKHPAIQEACVIATPD 474
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
126-627 |
2.26e-12 |
|
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: 69.66 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYN-FPLVTLYatlgkeavvhGLNESEASYLITS 204
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGaVPVLALP----------SHRRSELSAFCAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 205 VELlesklktalldiscvkhiiyvdnKAINKAEYPEGFEiHSMQSVEELGSNPenlgippsrptpsDMAIVMYTSGSTGR 284
Cdd:cd05920 111 AEA-----------------------VAYIVPDRHAGFD-HRALARELAESIP-------------EVALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 285 PKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTAE--ISCFTYGCRIGYSSPltlsdqsskikkGSKGD 362
Cdd:cd05920 154 PKLIPRTHNDYAYNVR-ASAEVCGLDQDTVYLAVLPAAHNFPLACPgvLGTLLAGGRVVLAPD------------PSPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 363 CTVL----KPTLMAAVPEImdriyknVMSKVQEmnyiqktlfkigydykleqiKKGYDAPLCNLllfkkvkallggnvRM 438
Cdd:cd05920 221 AFPLiereGVTVTALVPAL-------VSLWLDA--------------------AASRRADLSSL--------------RL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 439 MLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTVT--------EVTDYTTGRVGAPLIccEIKLKDwQEGgytiN 510
Cdd:cd05920 260 LQVGGARLSPALARRVPPVLGCTLQQVFGMAE----GLLNytrlddpdEVIIHTQGRPMSPDD--EIRVVD-EEG----N 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 511 D-KPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 589
Cdd:cd05920 329 PvPPGEEGELLTRGPYTIRGYYRAPEHNAR--AFTPDG--FYRTGDLVRRTPDGYLVVEGRIKDQIN-RGGEKIAAEEVE 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 530422004 590 AALKNCPLIDNICAFAKSDQSY---VISFVVPNQKRLTLLA 627
Cdd:cd05920 404 NLLLRHPAVHDAAVVAMPDELLgerSCAFVVLRDPPPSAAQ 444
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
271-618 |
6.60e-12 |
|
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: 68.27 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAhvleltaeiscFTYGCRIGYSSPLtlsd 350
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLA-----------FTFGLGGVLLFPF---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 351 qsskikkgSKGDCTVLKPtlmAAVPEimdriykNVMSKVQEmnYIQKTLFKIGYDYKLEQIKKGYDAPLcnlllfkkvka 430
Cdd:cd05958 163 --------GVGASGVLLE---EATPD-------LLLSAIAR--YKPTVLFTAPTAYRAMLAHPDAAGPD----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 431 llGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytin 510
Cdd:cd05958 212 --LSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEG----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 511 dKPNPRGEI---VIGGQNismGYFKNEEKTAEDYSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGK 587
Cdd:cd05958 284 -NPVPDGTIgrlAVRGPT---GCRYLADKRQRTYVQGG----WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPE 354
|
330 340 350
....*....|....*....|....*....|....
gi 530422004 588 VEAALKNCPLIDNICAFAKSDQS---YVISFVVP 618
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESrgvVVKAFVVL 388
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
261-633 |
6.79e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.22 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 261 GIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcri 340
Cdd:PRK06814 784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLTG----------- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 341 GYSSPLtlsdqSSKIKkgskgdcTVLKPTLM--AAVPEImdrIYKnvmskvqemnyIQKTLFkIGYDYKLeqikKGYdAP 418
Cdd:PRK06814 852 GLVLPL-----LSGVK-------VFLYPSPLhyRIIPEL---IYD-----------TNATIL-FGTDTFL----NGY-AR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 419 LCNLLLFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTES-----------CGAGTVtevtdyttGR 487
Cdd:PRK06814 900 YAHPYDFR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapvialntpmhNKAGTV--------GR 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 488 VgAPLIccEIKLKDwQEGgytINDKpnprGEIVIGGQNISMGYFKNEEKTAedYSVDENGqrWFCTGDIGEFHPDGCLQI 567
Cdd:PRK06814 964 L-LPGI--EYRLEP-VPG---IDEG----GRLFVRGPNVMLGYLRAENPGV--LEPPADG--WYDTGDIVTIDEEGFITI 1028
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530422004 568 IDRKKDLVKLqAGEYVSLGKVEAAlkncplidnICAFAKSDQSYVISfvVPNQK---RLTLLAQQKGVE 633
Cdd:PRK06814 1029 KGRAKRFAKI-AGEMISLAAVEEL---------AAELWPDALHAAVS--IPDARkgeRIILLTTASDAT 1085
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
466-620 |
7.57e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.38 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 466 YGLTESCGAGTVTEVTD-----YTTGRVGAPLICCEIKLKDwqEGGytiNDKPNP-RGEIVIGGQNISMGYFKNEEKTAE 539
Cdd:PRK04813 293 YGPTEATVAVTSIEITDemldqYKRLPIGYAKPDSPLLIID--EEG---TKLPDGeQGEIVISGPSVSKGYLNNPEKTAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 540 DYsVDENGQRWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFV 616
Cdd:PRK04813 368 AF-FTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVESAVVVPYNKDHkvqYLIAYV 444
|
....
gi 530422004 617 VPNQ 620
Cdd:PRK04813 445 VPKE 448
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-619 |
1.18e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 67.79 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 72 DIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMqpngkvfkklilgNYKWMNYlEVNRRVNNFGSgltaLGLKPKN 151
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVYGHKTALIFESSGGVVRRY-------------SYLELNE-EINRTANLFYS----LGIRKGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 152 TIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDnk 231
Cdd:PRK08008 64 KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 232 ainkAEYPEGFEIHSMQsvEELGSNPENLG-IPPSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-AGMTG--QCerip 307
Cdd:PRK08008 142 ----VALPADDGVSSFT--QLKAQQPATLCyAPPL--STDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSawQC---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 308 GLGPKDTYIGYLPLAHV-LELTAEISCFTYGCRI----GYSSPlTLSDQSSKIKkgskgdctvlkptlmAAVPEIMDRIY 382
Cdd:PRK08008 210 ALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFvlleKYSAR-AFWGQVCKYR---------------ATITECIPMMI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 383 KNVMSKVQEMNYIQKTLFKIGYDYKL-EQIKKGYDAPLcnlllfkkvkallggNVRMMLSggaplspqthrfmnvcfccp 461
Cdd:PRK08008 274 RTLMVQPPSANDRQHCLREVMFYLNLsDQEKDAFEERF---------------GVRLLTS-------------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 462 igqgYGLTEScgagTVTEVTDYTTGR-----VGAPLICCEIKLKDwqEGGYTIndKPNPRGEIVIG---GQNISMGYFKN 533
Cdd:PRK08008 319 ----YGMTET----IVGIIGDRPGDKrrwpsIGRPGFCYEAEIRD--DHNRPL--PAGEIGEICIKgvpGKTIFKEYYLD 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 534 EEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QS 610
Cdd:PRK08008 387 PKATAK--VLEADG--WLHTGDTGYVDEEGFFYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVGIKDsirDE 461
|
....*....
gi 530422004 611 YVISFVVPN 619
Cdd:PRK08008 462 AIKAFVVLN 470
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
128-706 |
1.46e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 67.24 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 207
Cdd:PRK08276 14 YGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 LESkLKTALLDISCVKHIIYVDnkainkAEYPEGFEIHSmqsvEELGSNPENLgiPPSRPTPSDMAivmYTSGSTGRPKG 287
Cdd:PRK08276 94 ADT-AAELAAELPAGVPLLLVV------AGPVPGFRSYE----EALAAQPDTP--IADETAGADML---YSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VM-----MHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrigySSPLTLSDQSSKIkkgskGD 362
Cdd:PRK08276 158 IKrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH-------------------TAPLRFGMSALAL-----GG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 363 CTVLkptlmaavpeiMDRiyknvMSKVQEMNYIQKtlFKIGYDY----------KL-EQIKKGYDaplcnlllfkkVKAL 431
Cdd:PRK08276 214 TVVV-----------MEK-----FDAEEALALIER--YRVTHSQlvptmfvrmlKLpEEVRARYD-----------VSSL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 432 lggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDYTT--GRVGAPLIcCEIKLKDwqeggytI 509
Cdd:PRK08276 265 -----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGV-TVITSEDWLAhpGSVGKAVL-GEVRILD-------E 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 510 NDKPNPRGEI-----VIGGQNISmgYFKNEEKTAEDYsvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVklqageyVS 584
Cdd:PRK08276 331 DGNELPPGEIgtvyfEMDGYPFE--YHNDPEKTAAAR----NPHGWVTVGDVGYLDEDGYLYLTDRKSDMI-------IS 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 585 LG------KVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQkrltllaqqkGVEGTwvdicnnPAMEAEILKEIRE 655
Cdd:PRK08276 398 GGvniypqEIENLLVTHPKVADVAVFGVPDEEMgerVKAVVQPAD----------GADAG-------DALAAELIAWLRG 460
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 530422004 656 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHYLKDIER 706
Cdd:PRK08276 461 -----RLAHYKCPRSIDFEDElPRTP-TG------KLYKRRLRDRYWEGRQR 500
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
127-702 |
2.27e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.56 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 127 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRA---EWMIAAQTCFKYnFPLVTLYATLGKEAVVhgLNESEASYLIT 203
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAAYI--VDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 204 SVELLESkLKTALLDISCVKHIIYVDNKAINkaeypEGFEIHSmQSVEELGSNPEnlgipPSRPTPSDMaivMYTSGSTG 283
Cdd:PRK13391 103 SAAKLDV-ARALLKQCPGVRHRLVLDGDGEL-----EGFVGYA-EAVAGLPATPI-----ADESLGTDM---LYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 284 RPKGVM--MHHSNLIA--GMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrigySSPLTLSdqSSKIKKGS 359
Cdd:PRK13391 168 RPKGIKrpLPEQPPDTplPLTAFLQRLWGFRSDMVYLSPAPLYH-------------------SAPQRAV--MLVIRLGG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 360 kgdcTVLkptlmaavpeIMDRiyknvMSKVQEMNYIQKtlFKIGYD----------YKL-EQIKKGYDaplcnlllfkkV 428
Cdd:PRK13391 227 ----TVI----------VMEH-----FDAEQYLALIEE--YGVTHTqlvptmfsrmLKLpEEVRDKYD-----------L 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 429 KALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDY-----TTGRV--GAPLICceiklkd 501
Cdd:PRK13391 275 SSL-----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGF-TACDSEEWlahpgTVGRAmfGDLHIL------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 502 wQEGGytindKPNPRGEIvigGQ-----NISMGYFKNEEKTAEDYSVDENgqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 576
Cdd:PRK13391 342 -DDDG-----AELPPGEP---GTiwfegGRPFEYLNDPAKTAEARHPDGT---WSTVGDIGYVDEDGYLYLTDRAAFMI- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 577 LQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKrltlLAQQ-KGVEGTWVDICNNPAMEAEILKEIRE 655
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNED----LGEEvKAVVQPVDGVDPGPALAAELIAFCRQ 473
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 530422004 656 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHYLK 702
Cdd:PRK13391 474 -----RLSRQKCPRSIDFEDElPRLP-TG------KLYKRLLRDRYWG 509
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
128-323 |
3.53e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.97 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynFPLVTLYATLG-------KEAVVHGLNESEASY 200
Cdd:PRK08279 65 YAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAW-------LGLAKLGAVVAllntqqrGAVLAHSLNLVDAKH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 LITSVELLESkLKTALLDIScVKHIIYVDNKAINKAeyPEGF-EIHSMQSveelGSNPENlgiPPSRP--TPSDMAIVMY 277
Cdd:PRK08279 138 LIVGEELVEA-FEEARADLA-RPPRLWVAGGDTLDD--PEGYeDLAAAAA----GAPTTN---PASRSgvTAKDTAFYIY 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530422004 278 TSGSTGRPKGVMMHHSNLI---AGMTGQCeripGLGPKDTYIGYLPLAH 323
Cdd:PRK08279 207 TSGTTGLPKAAVMSHMRWLkamGGFGGLL----RLTPDDVLYCCLPLYH 251
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
118-706 |
7.33e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 62.02 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 118 LILGNyKWMNYLEVNRRVNNFGSGLTALGLKP--------KNTIAIFCETRAEWMIAAqtcfkYNFPlVTLYATlgKEAV 189
Cdd:PRK12406 5 IISGD-RRRSFDELAQRAARAAGGLAALGVRPgdcvallmRNDFAFFEAAYAAMRLGA-----YAVP-VNWHFK--PEEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 190 VHGLNESEASYLITSVELLESkLKTALldiscvkhiiyvdnkainkaeyPEGFEIHSMQSVEELGSN----PENLGIP-- 263
Cdd:PRK12406 76 AYILEDSGARVLIAHADLLHG-LASAL----------------------PAGVTVLSVPTPPEIAAAyrisPALLTPPag 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 264 ----------------PSRPTPSDMaivMYTSGSTGRPKGVmmhhsnliagmtgqcERIPGLgPKDTyigylplAHVLEL 327
Cdd:PRK12406 133 aidwegwlaqqepydgPPVPQPQSM---IYTSGTTGHPKGV---------------RRAAPT-PEQA-------AAAEQM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 328 TAEISCFTYGCRIGYSSPLTLSDQSS-KIKKGSKGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYIQKTLFKIgydY 406
Cdd:PRK12406 187 RALIYGLKPGIRALLTGPLYHSAPNAyGLRAGRLGGVLVLQPRFDPE--ELLQLIERH---RITHMHMVPTMFIRL---L 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 407 KL-EQIKKGYDaplcnlllfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT--DY 483
Cdd:PRK12406 259 KLpEEVRAKYD-----------VSSL-----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTES---GAVTFATseDA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 484 TT--GRVGAPLICCEIKLKDwqeggytINDKPNPRGEI-----VIGGqNISMGYFKNEEKTAEdysVDENGqrWFCTGDI 556
Cdd:PRK12406 320 LShpGTVGKAAPGAELRFVD-------EDGRPLPQGEIgeiysRIAG-NPDFTYHNKPEKRAE---IDRGG--FITSGDV 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 557 GEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqQKGVE 633
Cdd:PRK12406 387 GYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEP----------QPGAT 455
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530422004 634 gtwVDicnnpamEAEILKEIREAanamkLERFEIPIKVRLSPEpwTPEtglvTDAFKLKRKELRNHYLKDIER 706
Cdd:PRK12406 456 ---LD-------EADIRAQLKAR-----LAGYKVPKHIEIMAE--LPR----EDSGKIFKRRLRDPYWANAGR 507
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
277-584 |
7.67e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 277 YTSGSTGRPKGVMM-HHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVleltaeiscFTYGcrIGYSSPltlSDQSSKI 355
Cdd:PRK06018 184 YTSGTTGDPKGVLYsHRSNVLHALMANNGDALGTSAADTMLPVVPLFHA---------NSWG--IAFSAP---SMGTKLV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 356 KKGSKGDCTVL-------KPTLMAAVPEIMDRIyknvmskvqeMNYIQKTlfkigyDYKLEQIKK----GYDAPLCNLLL 424
Cdd:PRK06018 250 MPGAKLDGASVyelldteKVTFTAGVPTVWLML----------LQYMEKE------GLKLPHLKMvvcgGSAMPRSMIKA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 425 FKKvkalLGGNVRmmlsggaplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVT---DYTTG--------RVGAPLI 493
Cdd:PRK06018 314 FED----MGVEVR--------------------------HAWGMTEMSPLGTLAALKppfSKLPGdarldvlqKQGYPPF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 494 CCEIKLKDwQEGgytiNDKP---NPRGEIVIGGQNISMGYFKneektAEDYSVDENGqrWFCTGDIGEFHPDGCLQIIDR 570
Cdd:PRK06018 364 GVEMKITD-DAG----KELPwdgKTFGRLKVRGPAVAAAYYR-----VDGEILDDDG--FFDTGDVATIDAYGYMRITDR 431
|
330
....*....|....
gi 530422004 571 KKDLVKlQAGEYVS 584
Cdd:PRK06018 432 SKDVIK-SGGEWIS 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
247-582 |
8.35e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.84 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 247 MQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIpglgpKDTYigylplahvle 326
Cdd:PRK09274 151 GTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA----QIEAL-----REDY----------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 327 ltaeiscftygcrigysspltlsdqssKIKKGSKGDCT-----VLKPTL-MAAV-PEiMDriyknvMSKVQEMN--YIQK 397
Cdd:PRK09274 211 ---------------------------GIEPGEIDLPTfplfaLFGPALgMTSViPD-MD------PTRPATVDpaKLFA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 398 TLFKigydyklEQIKKGYDAP--LCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTH-RFMNVcfccpIGQG------YGL 468
Cdd:PRK09274 257 AIER-------YGVTNLFGSPalLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIeRFRAM-----LPPDaeiltpYGA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 469 TESCGAGTVT--EVTDYTTGR--------VGAPLICCEIKLKDwqeggytINDKPNPR------------GEIVIGGQNI 526
Cdd:PRK09274 325 TEALPISSIEsrEILFATRAAtdngagicVGRPVDGVEVRIIA-------ISDAPIPEwddalrlatgeiGEIVVAGPMV 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 527 SMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEY 582
Cdd:PRK09274 398 TRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
118-575 |
1.02e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 61.54 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 118 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAE-W--MIAAQTC-FKYnfplVTLYATLGKEAVVHGL 193
Cdd:PRK06188 31 LVLGDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLmaIGAAQLAgLRR----TALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 194 NESEASYLIT-SVELLESKLktALLD-ISCVKHIIYVDnkainkaEYPEGfeihsmqsvEELGSNPENLGIPPSRP--TP 269
Cdd:PRK06188 106 EDAGISTLIVdPAPFVERAL--ALLArVPSLKHVLTLG-------PVPDG---------VDLLAAAAKFGPAPLVAaaLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 270 SDMAIVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKDTYIGYLPLAHVleltaeiscftygcrigysspltls 349
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRS-IATMAQIQLAEWEWPADPRFLMCTPLSHA------------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 350 dqsskikkgskGDCTVLkPTLMAAVPEIMDRIYK--NVMSKVQEMNyIQKTLFKIGYDYKLEQIKKGYDAPLCNLllfkk 427
Cdd:PRK06188 222 -----------GGAFFL-PTLLRGGTVIVLAKFDpaEVLRAIEEQR-ITATFLVPTMIYALLDHPDLRTRDLSSL----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 428 vkallggnvRMMLSGGAPLSPQ-----THRFMNVcfccpIGQGYGLTESCGAGTVTEVTDYTTGRV------GAPLICCE 496
Cdd:PRK06188 284 ---------ETVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 497 IKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKD 573
Cdd:PRK06188 350 VALLD-------EDGREVAQgevGEICVRGPLVMDGYWNRPEETAEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKD 417
|
..
gi 530422004 574 LV 575
Cdd:PRK06188 418 MI 419
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
184-699 |
1.70e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.95 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 184 LGKEAVVHGLNESEASYLITSVELLEsKLKTALLDISCVKHIIYVDNKAINKAE--YPEGFEIHSMQSveELGSNPENLG 261
Cdd:PRK05620 98 LMNDQIVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIGPSDADSAAahMPEGIKVYSYEA--LLDGRSTVYD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcri 340
Cdd:PRK05620 175 WPELDET--TAAAICYSTGTTGAPKGVVYSHRSLyLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSG--- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 341 gysSPLTLSDQSskikkgskgdctVLKPTLMAAVPEIMDRIYKNVMSK-VQEMNYIQKTLFKigydykleqikkgydapl 419
Cdd:PRK05620 250 ---TPLVFPGPD------------LSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPPE------------------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 420 cnlllfkkvkallggnvRMML----SGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--------EVTD---YT 484
Cdd:PRK05620 297 -----------------RMSLqeiyVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVArppsgvsgEARWayrVS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 485 TGRVGAPLiccEIKLKDwqeGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTA-------EDYSVDENGQR-----WFC 552
Cdd:PRK05620 360 QGRFPASL---EYRIVN---DGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaastfRGEDVEDANDRftadgWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 553 TGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVslgkVEAALKNcplidNICAFAKSDQSYVISFvvPNQK------RLTLL 626
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIR-SGGEWI----YSAQLEN-----YIMAAPEVVECAVIGY--PDDKwgerplAVTVL 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422004 627 AQqkGVEGTwvdicnnpameAEILKEIREAAnamkleRFEIPikVRLSPEPWT-PETGLVTDAFKLKRKELRNH 699
Cdd:PRK05620 502 AP--GIEPT-----------RETAERLRDQL------RDRLP--NWMLPEYWTfVDEIDKTSVGKFDKKDLRQH 554
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-592 |
1.77e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 206 ELLEsklktallDISCVKHIIYVDNKAINKAEYPE---GFEIHsmqsveelGSNpenlgippsrptpsdMAIVMYTSGST 282
Cdd:PRK05691 1237 HLLE--------RLPQAEGVSAIALDSLHLDSWPSqapGLHLH--------GDN---------------LAYVIYTSGST 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 283 GRPKGVMMHHSNLIagmtgqcERIPGLgpKDTYIgyLPLAHVLELTAEIS-------CF---TYGCRIgysspltlsdqs 352
Cdd:PRK05691 1286 GQPKGVGNTHAALA-------ERLQWM--QATYA--LDDSDVLMQKAPISfdvsvweCFwplITGCRL------------ 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 353 skikkgskgdctvlkptLMAAVPEIMD--RIYKNVMSK-VQEMNYIQKTLfkigydyklEQIKKGYDAPLCNLLlfkkvk 429
Cdd:PRK05691 1343 -----------------VLAGPGEHRDpqRIAELVQQYgVTTLHFVPPLL---------QLFIDEPLAAACTSL------ 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 430 allggnvRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTEScgAGTVT----EVTDYTTGRVGAPL--ICCEIKLKDW 502
Cdd:PRK05691 1391 -------RRLFSGGEALPAElRNRVLQRLPQVQLHNRYGPTET--AINVThwqcQAEDGERSPIGRPLgnVLCRVLDAEL 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 503 QeggytindkPNPRG---EIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVK 576
Cdd:PRK05691 1462 N---------LLPPGvagELCIGGAGLARGYLGRPALTAERFVPDplgEDGARLYRTGDRARWNADGALEYLGRLDQQVK 1532
|
490
....*....|....*.
gi 530422004 577 LQaGEYVSLGKVEAAL 592
Cdd:PRK05691 1533 LR-GFRVEPEEIQARL 1547
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
269-575 |
2.26e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPgLGPKDTYIGYLPLAHVLELtaeiscftygcrIGysspl 346
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGID-LNPDDVIVSWLPLYHDMGL------------IG----- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 347 tlsdqsskikkgskgdcTVLKPtLMAAVPEIMdriyknvMSKVQEMNYIQKTLFKIG-----------YDYKL--EQIKk 413
Cdd:PRK05691 227 -----------------GLLQP-IFSGVPCVL-------MSPAYFLERPLRWLEAISeyggtisggpdFAYRLcsERVS- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 414 gyDAPLCNLLLfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQ-----GYGLTESC--------GAG-TVT 478
Cdd:PRK05691 281 --ESALERLDL---------SRWRVAYSGSEPIRQDSlERFAEKFAACGFDPdsffaSYGLAEATlfvsggrrGQGiPAL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 479 EVTDYTTGR------VGAPLICC-------EIKLKDWQEGGyTINDkpNPRGEIVIGGQNISMGYFKNEEKTAEDYsVDE 545
Cdd:PRK05691 350 ELDAEALARnraepgTGSVLMSCgrsqpghAVLIVDPQSLE-VLGD--NRVGEIWASGPSIAHGYWRNPEASAKTF-VEH 425
|
330 340 350
....*....|....*....|....*....|
gi 530422004 546 NGQRWFCTGDIGeFHPDGCLQIIDRKKDLV 575
Cdd:PRK05691 426 DGRTWLRTGDLG-FLRDGELFVTGRLKDML 454
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
121-322 |
3.72e-09 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 59.95 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 LITSVELLE----SKLKT----ALLDISC-VKHIIYVDNKAINKAEYPEGFEIHSMQSVEelGSNPEnlgIPPSRPTPSD 271
Cdd:TIGR02188 164 VITADEGLRggkvIPLKAivdeALEKCPVsVEHVLVVRRTGNPVVPWVEGRDVWWHDLMA--KASAY---CEPEPMDSED 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530422004 272 MAIVMYTSGSTGRPKGVMmhHS----NLIAGMTgqCERIPGLGPKD--------------TYIGYLPLA 322
Cdd:TIGR02188 239 PLFILYTSGSTGKPKGVL--HTtggyLLYAAMT--MKYVFDIKDGDifwctadvgwitghSYIVYGPLA 303
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
258-575 |
3.93e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 59.62 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 258 ENLGIPPSRP---TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscf 334
Cdd:PRK07768 137 DLLAADPIDPvetGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGM------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 335 tygcrIGY-SSPLTLSdqsskikkgskgdCTVLKPTLMAAV------PEIMDRiYKNVMSKVQEMNY--IQKTLFKigyd 405
Cdd:PRK07768 210 -----VGFlTVPMYFG-------------AELVKVTPMDFLrdpllwAELISK-YRGTMTAAPNFAYalLARRLRR---- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 406 ykleQIKKG-YDAplcnlllfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTES--- 471
Cdd:PRK07768 267 ----QAKPGaFDL----------------SSLRFALNGAEPIDPADvEDLLDAgarfglrpeAILP----AYGMAEAtla 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 472 -----CGAGTVTEVTD------------YTTGRV------GAPLICCEIKLKDwqEGGYTIndkpNPR--GEIVIGGQNI 526
Cdd:PRK07768 323 vsfspCGAGLVVDEVDadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD--EDGQVL----PPRgvGVIELRGESV 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 530422004 527 SMGYFkneekTAEDY--SVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 575
Cdd:PRK07768 397 TPGYL-----TMDGFipAQDADG--WLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
128-315 |
4.08e-09 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 59.90 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT---- 203
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadgg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 204 -----SVELLESKLKTALLDISCVKHIIYVDNKAINkAEYPEGFEIHSMQSVEElgSNPENlgiPPSRPTPSDMAIVMYT 278
Cdd:cd17634 167 vragrSVPLKKNVDDALNPNVTSVEHVIVLKRTGSD-IDWQEGRDLWWRDLIAK--ASPEH---QPEAMNAEDPLFILYT 240
|
170 180 190
....*....|....*....|....*....|....*..
gi 530422004 279 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY 315
Cdd:cd17634 241 SGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIY 277
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
63-437 |
4.41e-09 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 60.25 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 63 THFDSLAvidipGADTLDKLFDHAVSKFGKKDSLGtreilsEENEmqpngkvfkkliLGNYKWMNYLEVNRRVNNFGSGL 142
Cdd:PTZ00297 418 REYNPLA-----GVRSLGEMWERSVTRHSTFRCLG------QTSE------------SGESEWLTYGTVDARARELGSGL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 143 TALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLyatLGKEAVVHGLneseasylitsveLLESKLKTALLDISCV 222
Cdd:PTZ00297 475 LALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPL---VGKGSTMRTL-------------IDEHKIKVVFADRNSV 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 223 KHIIYVDNKAINKAEYPEGFEIHSMQSV-----------EELGSNPENLGIPPSRPTPSDMAIVMY----TSGSTGRPKG 287
Cdd:PTZ00297 539 AAILTCRSRKLETVVYTHSFYDEDDHAVardlnitlipyEFVEQKGRLCPVPLKEHVTTDTVFTYVvdntTSASGDGLAV 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VMMHHSNLIAG-----MTGQcerIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIkkgskgd 362
Cdd:PTZ00297 619 VRVTHADVLRDistlvMTGV---LPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVKF------- 688
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530422004 363 ctvlKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIK-KGYDAPLCNLLLFKKVKALLGGNVR 437
Cdd:PTZ00297 689 ----QPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRSRLINiHRRDSSLLRFIFFRATQELLGGCVE 760
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
128-624 |
5.51e-09 |
|
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: 59.06 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplvtlyatLGkeAVVHGLN----ESEASYLIT 203
Cdd:cd05923 31 YSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHR-----------LG--AVPALINprlkAAELAELIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 204 SVELlesklktalldiscvKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGSnPENLG--IPPSRPTPSDMAIVMYTSGS 281
Cdd:cd05923 98 RGEM---------------TAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGE-PESAGplIEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 282 TGRPKGVMM---HHSNLIAGMTGQCeripGL--GPKDTYIGYLPLAHVleltaeiscftygcrIGYSSPLTLSdqsskik 356
Cdd:cd05923 162 TGLPKGAVIpqrAAESRVLFMSTQA----GLrhGRHNVVLGLMPLYHV---------------IGFFAVLVAA------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 357 kgSKGDCTVLkptlmaaVPEIMDRiyknvmskVQEMNYIQKtlfkigydyklEQIKKGYDAP-----LCNLLLFKKVKAl 431
Cdd:cd05923 216 --LALDGTYV-------VVEEFDP--------ADALKLIEQ-----------ERVTSLFATPthldaLAAAAEFAGLKL- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 432 lgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgAGTVTEVTDYTTGRVGAPLICCEIKLKdwQEGGYTIND 511
Cdd:cd05923 267 --SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE---AMNSLYMRDARTGTEMRPGFFSEVRIV--RIGGSPDEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 512 KPN-PRGEIVI--GGQNISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKV 588
Cdd:cd05923 340 LANgEEGELIVaaAADAAFTGYLNQPEATAKKLQ-----DGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEI 413
|
490 500 510
....*....|....*....|....*....|....*....
gi 530422004 589 EAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKRLT 624
Cdd:cd05923 414 ERVLSRHPGVTEVVVIGVADERWgqsVTACVVPREGTLS 452
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
128-293 |
7.71e-09 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 58.73 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 207
Cdd:cd05966 87 YRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 --------LESKLKTALLDISCVKHIIYVDNKAiNKAEYPEGFEI--HsmqsvEELGSNPENlgIPPSRPTPSDMAIVMY 277
Cdd:cd05966 167 yrggkvipLKEIVDEALEKCPSVEKVLVVKRTG-GEVPMTEGRDLwwH-----DLMAKQSPE--CEPEWMDSEDPLFILY 238
|
170
....*....|....*.
gi 530422004 278 TSGSTGRPKGVMmhHS 293
Cdd:cd05966 239 TSGSTGKPKGVV--HT 252
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-292 |
8.33e-09 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 58.66 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 121 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 201 LITS---------VELLESKLKTALLDIScVKHIIYVDNKAINKAEYPEGFeihsMQSVEELGSNPENLgippSRPTPSD 271
Cdd:cd05968 167 LITAdgftrrgreVNLKEEADKACAQCPT-VEKVVVVRHLGNDFTPAKGRD----LSYDEEKETAGDGA----ERTESED 237
|
170 180
....*....|....*....|.
gi 530422004 272 MAIVMYTSGSTGRPKGVMMHH 292
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
434-620 |
1.20e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 58.08 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 434 GNVRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTEScgAGTVTEVT--DYTTGR--VGAPLICCEIKLKdwqegg 506
Cdd:PRK07445 230 AQFRTILLGGAPAWPsllEQARQLQL----RLAPTYGMTET--ASQIATLKpdDFLAGNnsSGQVLPHAQITIP------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 507 ytindkPNPRGEIVIGGQNISMGYfkneektaedYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLG 586
Cdd:PRK07445 298 ------ANQTGNITIQAQSLALGY----------YPQILDSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPA 360
|
170 180 190
....*....|....*....|....*....|....*..
gi 530422004 587 KVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 620
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLGLPDPHWgevVTAIYVPKD 397
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
142-703 |
2.05e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.32 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 142 LTALGLKPKNTIAIFCETRAEWMIAAQTCfKYN----FPLVTLYATLGKEAVVHGLN----ESEASYLITSVELLEsklk 213
Cdd:PRK09192 66 LLALGLKPGDRVALIAETDGDFVEAFFAC-QYAglvpVPLPLPMGFGGRESYIAQLRgmlaSAQPAAIITPDELLP---- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 214 taLLdiscvkhiiyvdNKAINKAEYPEGFeihsmqSVEELGSNPENlGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 293
Cdd:PRK09192 141 --WV------------NEATHGNPLLHVL------SHAWFKALPEA-DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 294 NLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeISCFTygcrigysSPLTlsDQSSkikkgskgdcTVLKPTLMAA 373
Cdd:PRK09192 200 ALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGL---VGFLL--------TPVA--TQLS----------VDYLPTRDFA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 374 VPEI--MDRIYKNVMSkvqeMNYIQktlfKIGYDykleqikkgydapLCNLLLFKKVKALL-------GGNvrmmlsGGA 444
Cdd:PRK09192 257 RRPLqwLDLISRNRGT----ISYSP----PFGYE-------------LCARRVNSKDLAELdlscwrvAGI------GAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 445 PLSPQT-HRFMNvCFcCPIG-------QGYGLTESC--------GAGTVTEVTDYT--------------TGRV------ 488
Cdd:PRK09192 310 MIRPDVlHQFAE-AF-APAGfddkafmPSYGLAEATlavsfsplGSGIVVEEVDRDrleyqgkavapgaeTRRVrtfvnc 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 489 GAPLICCEIKLKDwqEGGYTINDKpnPRGEIVIGGQNISMGYFKNEEkTAEDYSVDEngqrWFCTGDIGeFHPDGCLQII 568
Cdd:PRK09192 388 GKALPGHEIEIRN--EAGMPLPER--VVGHICVRGPSLMSGYFRDEE-SQDVLAADG----WLDTGDLG-YLLDGYLYIT 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 569 DRKKDLVKLQaGEYVSLGKVEAALKNCPLID--NICAFAKSDqsyvisfvvPNQKRLTLLAQqkgvegtwvdiCNnpAME 646
Cdd:PRK09192 458 GRAKDLIIIN-GRNIWPQDIEWIAEQEPELRsgDAAAFSIAQ---------ENGEKIVLLVQ-----------CR--ISD 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 530422004 647 AEILKEIREAANAMKLERFEIPIKVRLSPepwtPETGLVTDAFKLKRKELRNHYLKD 703
Cdd:PRK09192 515 EERRGQLIHALAALVRSEFGVEAAVELVP----PHSLPRTSSGKLSRAKAKKRYLSG 567
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
118-632 |
2.16e-08 |
|
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: 57.46 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 118 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYN-FPLVTLYAtlgkeavvHGLNE- 195
Cdd:COG1021 44 VVDGERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGaIPVFALPA--------HRRAEi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 196 ------SEASYLITS--------VELLESkLKTALldiSCVKHIIYVDNkainkaeyPEGFeihsmQSVEELGSNPENLG 261
Cdd:COG1021 115 shfaeqSEAVAYIIPdrhrgfdyRALARE-LQAEV---PSLRHVLVVGD--------AGEF-----TSLDALLAAPADLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 262 IPpsRPTPSDMAIVMYTSGSTGRPKgvmmhhsnLI-------AGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscf 334
Cdd:COG1021 178 EP--RPDPDDVAFFQLSGGTTGLPK--------LIprthddyLYSVRASAEICGLDADTVYLAALPAAHNFPL------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 335 tygcrigySSPLTLsdqsskikkG--SKGDCTVLKP----------------TLMAAVPEIMDRIyknvmskvqeMNYIQ 396
Cdd:COG1021 241 --------SSPGVL---------GvlYAGGTVVLAPdpspdtafplierervTVTALVPPLALLW----------LDAAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 397 KtlfkigYDYKLeqikkgydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGT 476
Cdd:COG1021 294 R------SRYDL-------------------------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE----GL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 477 VT--------EVTDYTTGRvgaPlICC--EIKLKDwqeggytINDKPNPRGE----IVIGGQNISmGYFKNEEKTAEdyS 542
Cdd:COG1021 339 VNytrlddpeEVILTTQGR---P-ISPddEVRIVD-------EDGNPVPPGEvgelLTRGPYTIR-GYYRAPEHNAR--A 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 543 VDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPN 619
Cdd:COG1021 405 FTPDG--FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgerSCAFVVPR 481
|
570
....*....|....*...
gi 530422004 620 QKRLTLLA-----QQKGV 632
Cdd:COG1021 482 GEPLTLAElrrflRERGL 499
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
128-698 |
3.46e-08 |
|
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: 56.59 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWmiaaqtcfkynfpLVTLYATLGKEAVVHGLNeseasYLITSVEL 207
Cdd:cd05940 6 YAELDAMANRYARWLKSLGLKPGDVVALFMENRPEY-------------VLLWLGLVKIGAVAALIN-----YNLRGESL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 208 LESklktalLDISCVKHIIYvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpsDMAIVMYTSGSTGRPKG 287
Cdd:cd05940 68 AHC------LNVSSAKHLVV-------------------------------------------DAALYIYTSGTTGLPKA 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 288 VMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVlelTAEISCFTYGCRIGYSspltlsdqsskikkgskgdcTVLK 367
Cdd:cd05940 99 AIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYHS---TALIVGWSACLASGAT--------------------LVIR 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 368 PTLMAAvpEIMDRIYKNvmskvqemnyiQKTLFkigydykleqikkGYDAPLCNLLLFKKVKAL-LGGNVRMMLSGGapL 446
Cdd:cd05940 155 KKFSAS--NFWDDIRKY-----------QATIF-------------QYIGELCRYLLNQPPKPTeRKHKVRMIFGNG--L 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 447 SPQTHRFMNVCFCCP-IGQGYGLTE-SCG-------AGTVTEVTDYTTGRVGAPLICCEIK----LKDwqEGGYTINDKP 513
Cdd:cd05940 207 RPDIWEEFKERFGVPrIAEFYAATEgNSGfinffgkPGAIGRNPSLLRKVAPLALVKYDLEsgepIRD--AEGRCIKVPR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 514 NPRGEIV--IGGQNISMGYFKN---EEKTAEDysVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 588
Cdd:cd05940 285 GEPGLLIsrINPLEPFDGYTDPaatEKKILRD--VFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK-GENVSTTEV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 589 EAALKncplidnicAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDIcnnPAMEAEILKEireaanamkLERFEIP 668
Cdd:cd05940 362 AAVLG---------AFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDL---SALAAHLEKN---------LPGYARP 420
|
570 580 590
....*....|....*....|....*....|
gi 530422004 669 IKVRLSPEPWTPETglvtdaFKLKRKELRN 698
Cdd:cd05940 421 LFLRLQPEMEITGT------FKQQKVDLRN 444
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-609 |
4.32e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.82 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 264 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGpkdTYIGYLPLAHVLELTAEISCFTYGcrigyS 343
Cdd:PRK07824 29 VGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG---QWLLALPAHHIAGLQVLVRSVIAG-----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 344 SPLTLsDQSSKIKkgskgdctvlKPTLMAAVPEI-MDRIYKNVMSKvqemnyiqktlfkigydykleQIKKGYDAPlcnl 422
Cdd:PRK07824 101 EPVEL-DVSAGFD----------PTALPRAVAELgGGRRYTSLVPM---------------------QLAKALDDP---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 423 llfKKVKALLGGNVrmMLSGGAPLSPQTHRfMNVCFCCPIGQGYGLTESCGaGTVTEvtdyttgrvGAPLICCEIKLKDw 502
Cdd:PRK07824 145 ---AATAALAELDA--VLVGGGPAPAPVLD-AAAAAGINVVRTYGMSETSG-GCVYD---------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 503 qeggytindkpnprGEIVIGGQNISMGYfKNEEktaEDYSVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVKlQAGEY 582
Cdd:PRK07824 208 --------------GRIALGGPTLAKGY-RNPV---DPDPFAEPG--WFRTDDLGALD-DGVLTVLGRADDAIS-TGGLT 265
|
330 340
....*....|....*....|....*..
gi 530422004 583 VSLGKVEAALKNCPLIDNICAFAKSDQ 609
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGLPDD 292
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
457-618 |
1.43e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.49 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 457 CFCcpigqGYGLTEScgAGTVTEV-TDYTTGrVGAPLICCEIKLKDwqeggytindkpnprGEIVIGGQNISMGYFKNEE 535
Cdd:PRK09029 267 CWC-----GYGLTEM--ASTVCAKrADGLAG-VGSPLPGREVKLVD---------------GEIWLRGASLALGYWRQGQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 536 KTAedySVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNicafaksdqsyviSF 615
Cdd:PRK09029 324 LVP---LVNDEG--WFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQ-------------VF 383
|
...
gi 530422004 616 VVP 618
Cdd:PRK09029 384 VVP 386
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
126-697 |
2.05e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 54.36 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 126 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLGkeAVVHGLN----ESEASYL 201
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ITS-----------------VELLESKLKTALLDiscVKHIIYVDNKAinkAEYPEGFEIHSMQSVE-ELGSNPENLGIP 263
Cdd:PRK06164 103 LGRgrarwlvvwpgfkgidfAAILAAVPPDALPP---LRAIAVVDDAA---DATPAPAPGARVQLFAlPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 264 PSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYG----CR 339
Cdd:PRK06164 177 AA--DPDAGALLFTTSGTTSGPKLVLHRQATLLR-HARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGaplvCE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 340 IGYSSPLTLSD-QSSKIKKGSKGDctvlkptlmaavpEIMDRIYKnvmSKVQEMNYIQKTLFKIGyDY-----KLEQIKK 413
Cdd:PRK06164 254 PVFDAARTARAlRRHRVTHTFGND-------------EMLRRILD---TAGERADFPSARLFGFA-SFapalgELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 414 GYDAPLCNLLLFKKVKALLGG-------NVRMmLSGGAPLSPQthrfmnvcfccpigqgygltescgaGTVtEVTDYTTG 486
Cdd:PRK06164 317 ARGVPLTGLYGSSEVQALVALqpatdpvSVRI-EGGGRPASPE-------------------------ARV-RARDPQDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 487 RVGAPlicceiklkdwqeggytindkpNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDEngqrWFCTGDIGEFHPDGCLQ 566
Cdd:PRK06164 370 ALLPD----------------------GESGEIEIRAPSLMRGYLDNPDATARALTDDG----YFRTGDLGYTRGDGQFV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 567 IIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDN--ICAFAKSDQSYVISFVVPNqkrltllaqqkgvEGTWVDicnnpa 644
Cdd:PRK06164 424 YQTRMGDSLRL-GGFLVNPAEIEHALEALPGVAAaqVVGATRDGKTVPVAFVIPT-------------DGASPD------ 483
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 530422004 645 mEAEILKEIREAanamkLERFEIPIKVRLSPEPWTPETGlvtDAFKLKRKELR 697
Cdd:PRK06164 484 -EAGLMAACREA-----LAGFKVPARVQVVEAFPVTESA---NGAKIQKHRLR 527
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
261-575 |
2.18e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 54.18 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 261 GIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA----GMTGQCERIPGLGPKD-TYIGYLPLAH----VLELTAEI 331
Cdd:PRK05850 151 GSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYFGDTGGVPPPDtTVVSWLPFYHdmglVLGVCAPI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 332 SCftyGCRIGYSSPLTLsdqsskikkgskgdctVLKPT----LMAAVPEImdriyknvmskvqemnyiqktlFKIGYDYK 407
Cdd:PRK05850 231 LG---GCPAVLTSPVAF----------------LQRPArwmqLLASNPHA----------------------FSAAPNFA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 408 LE-QIKKGYDAPLCNLLLfkkvkallgGNVRMMLSGGAPLSPQT-HRFMN--VCFCCP---IGQGYGLTE------SCGA 474
Cdd:PRK05850 270 FElAVRKTSDDDMAGLDL---------GGVLGIISGSERVHPATlKRFADrfAPFNLRetaIRPSYGLAEatvyvaTREP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 475 GTVTEVTDY-----TTGRV-------GAPLIcceiklkdwqegGYTINDKPNPR---------------GEIVIGGQNIS 527
Cdd:PRK05850 341 GQPPESVRFdyeklSAGHAkrcetggGTPLV------------SYGSPRSPTVRivdpdtciecpagtvGEIWVHGDNVA 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 530422004 528 MGYFKNEEKTAE-------DYSVDENGQRWFCTGDIGEFHpDGCLQIIDRKKDLV 575
Cdd:PRK05850 409 AGYWQKPEETERtfgatlvDPSPGTPEGPWLRTGDLGFIS-EGELFIVGRIKDLL 462
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
264-575 |
3.03e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.58 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 264 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLiagMTGQCERIPGLGPK--DTYIGYLPLAHVLELTAEISCFTYGCRIG 341
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNL---PTNVLQVIDALEGQegDRGVSWLPFFHDMGLITVLLPALLGHYIT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 342 YSSPLTLsdqsskikkgskgdctVLKP----TLMAAVPEIMDRIyknvmskvqemnyiqktlFKIGYDYKLEQ-----IK 412
Cdd:PRK07769 251 FMSPAAF----------------VRRPgrwiRELARKPGGTGGT------------------FSAAPNFAFEHaaargLP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 413 KGYDAPLcNLllfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCcPIG-------QGYGLTESC------------- 472
Cdd:PRK07769 297 KDGEPPL-DL-----------SNVKGLLNGSEPVSPASMRKFNEAFA-PYGlpptaikPSYGMAEATlfvsttpmdeept 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 473 ---------GAGTVTEVTDYTTGRVgAPLICCEIKLKDWQE--GGYTINDKPNPR-GEIVIGGQNISMGYFKNEEKTAED 540
Cdd:PRK07769 364 viyvdrdelNAGRFVEVPADAPNAV-AQVSAGKVGVSEWAVivDPETASELPDGQiGEIWLHGNNIGTGYWGKPEETAAT 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530422004 541 Y--------------SVDENGqRWFCTGDIGEFHpDGCLQIIDRKKDLV 575
Cdd:PRK07769 443 FqnilksrlseshaeGAPDDA-LWVRTGDYGVYF-DGELYITGRVKDLV 489
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
263-605 |
5.07e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 53.51 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS---NLIAGMTGQCeripGLGPKDTyigylplahVLELTAeiscftygCR 339
Cdd:PRK10252 591 PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTaivNRLLWMQNHY----PLTADDV---------VLQKTP--------CS 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 340 IGYSS-----PLTLsdqsskikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmSKVQEMNYIQKTLfkigydykleqikKG 414
Cdd:PRK10252 650 FDVSVweffwPFIA------------GAKLVMAEPEAHRDPLAMQQFFAE--YGVTTTHFVPSML-------------AA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 415 YDAPLCNLLLFKKVKALlggnVRMMLSGGA---PLSPQTHRFMNVcfccPIGQGYGLTEScgAGTVT------EVTDYTT 485
Cdd:PRK10252 703 FVASLTPEGARQSCASL----RQVFCSGEAlpaDLCREWQQLTGA----PLHNLYGPTEA--AVDVSwypafgEELAAVR 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 486 GR---VGAPLicceiklkdWQEGGYTINDKPNP-----RGEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGD 555
Cdd:PRK10252 773 GSsvpIGYPV---------WNTGLRILDARMRPvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADpfAPGERMYRTGD 843
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 530422004 556 IGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 605
Cdd:PRK10252 844 VARWLDDGAVEYLGRSDDQLKIR-GQRIELGEIDRAMQALPDVEQAVTHA 892
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
525-596 |
5.22e-07 |
|
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: 52.38 E-value: 5.22e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530422004 525 NISMGYFKNEEKTAEDYsVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCP 596
Cdd:cd05924 222 HIPLGYYGDEAKTAETF-PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-TGGEKVFPEEVEEALKSHP 291
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
466-598 |
5.41e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 52.74 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 466 YGLTESCGAGTVT---EVTDYT-TGR---VGAPLICCEIKLKDWQEGgytindKPNP---RGEIVIGGQNISMGYFKNEE 535
Cdd:PRK06178 360 WGMTETHTCDTFTagfQDDDFDlLSQpvfVGLPVPGTEFKICDFETG------ELLPlgaEGEIVVRTPSLLKGYWNKPE 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530422004 536 KTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLI 598
Cdd:PRK06178 434 ATAE---ALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAV 490
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
269-625 |
1.19e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 51.74 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCrigysspltl 348
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRA-CLKFFSPKEDDVMMSFLPPFH-----------AYGF---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 349 sdqsskikkgskgDCTVLKPtLMAAVPEIMDriYKNVMSK--VQEMNYIQKTLF---KIGYDYKLEQIKKGyDAPLCNLL 423
Cdd:PRK06334 240 -------------NSCTLFP-LLSGVPVVFA--YNPLYPKkiVEMIDEAKVTFLgstPVFFDYILKTAKKQ-ESCLPSLR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 424 LfkkvkALLGGNV--RMMLSGGAPLSPQTHrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTTGR-VGAPLICCEIKLK 500
Cdd:PRK06334 303 F-----VVIGGDAfkDSLYQEALKTFPHIQ----------LRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 501 dwQEGGYTindkPNPRGE---IVIGGQNISMGYFKNEEKTAedySVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 577
Cdd:PRK06334 368 --SEETKV----PVSSGEtglVLTRGTSLFSGYLGEDFGQG---FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 530422004 578 qAGEYVSLGKVEAALkncplidnICAFAKSDQSYVISFVV---PNQK-RLTL 625
Cdd:PRK06334 439 -GAEMVSLEALESIL--------MEGFGQNAADHAGPLVVcglPGEKvRLCL 481
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
268-697 |
2.07e-06 |
|
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: 50.89 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNliagmtgqceripglgpkdTYIGYLPLAHVLELTAEIScfTYGCRIGYSSPLT 347
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRR-------------------TLVTSNLLSHDLNLKNGDR--TYTCMPLYHGTAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 348 LSDQSSKIKKGSkgdCTVLKPTLMAAvpeimdRIYKNVMSkvQEMNYIQktlfkigydykleqikkgYDAPLCNLLLF-- 425
Cdd:cd05937 144 FLGACNCLMSGG---TLALSRKFSAS------QFWKDVRD--SGATIIQ------------------YVGELCRYLLStp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 426 --KKVKAllgGNVRMMLSGGapLSPQT-HRFMNVcFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 501
Cdd:cd05937 195 psPYDRD---HKVRVAWGNG--LRPDIwERFRER-FNVPeIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFEN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 502 WQ-------EGGYTINDKPN------PRGEiviGGQNIS----------MGYFKNEEKTAEDYSVD--ENGQRWFCTGDI 556
Cdd:cd05937 269 QVvlvkmdpETDDPIRDPKTgfcvraPVGE---PGEMLGrvpfknreafQGYLHNEDATESKLVRDvfRKGDIYFRTGDL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 557 GEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEaalkncpliDNICAFAKSDQSYVISFVVPNQKrltllaQQKGVEGtw 636
Cdd:cd05937 346 LRQDADGRWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHPDIAEANVYGVKVPGHD------GRAGCAA-- 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530422004 637 VDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEpwtpetGLVTDAFKLKRKELR 697
Cdd:cd05937 408 ITLEESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VATTDNHKQQKGVLR 462
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
277-586 |
2.56e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 50.81 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 277 YTSGSTGRPKGVMMHHSNLIAGMTGQ-CERIPGLGPKDTYIGYLPLAHvleltaeiscftyGCRIgysspltlsDQSSKI 355
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFVITNHlADLMPGTTEQDASLVVAPLSH-------------GAGI---------HQLCQV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 356 KKGSKgdcTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKigyDYKLEQikkgYDAplcnlllfkkvkallgGN 435
Cdd:PRK07470 228 ARGAA---TVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVE---HPAVDR----YDH----------------SS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 436 VRMMLSGGAPL--SPQTH---RFMNVcfccpIGQGYGLTESCGAGTVT-----EVTDYTTGRVGapliCC-------EIK 498
Cdd:PRK07470 282 LRYVIYAGAPMyrADQKRalaKLGKV-----LVQYFGLGEVTGNITVLppalhDAEDGPDARIG----TCgfertgmEVQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 499 LKDwqEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLvklq 578
Cdd:PRK07470 353 IQD--DEGREL--PPGETGEICVIGPAVFAGYYNNPEANAKAF---RDG--WFRTGDLGHLDARGFLYITGRASDM---- 419
|
....*...
gi 530422004 579 ageYVSLG 586
Cdd:PRK07470 420 ---YISGG 424
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
250-580 |
2.60e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.53 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 250 VEELGSNPENLGIPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK05851 134 LATAAHTNRSASLTP--PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 330 EISCFTYGcrigysSPLTLSDQSSkikkgskgdctvlkptlMAAVPeimdriyknvMSKVQEMNYIQKTLFK---IGYDY 406
Cdd:PRK05851 212 LLTAALAG------APLWLAPTTA-----------------FSASP----------FRWLSWLSDSRATLTAapnFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 407 kleqIKKgYDaplcnlllfKKVKALLGGNVRMMLSGGAPLSPQ-THRFMNVcfCCPIG-------QGYGLTES------- 471
Cdd:PRK05851 259 ----IGK-YA---------RRVSDVDLGALRVALNGGEPVDCDgFERFATA--MAPFGfdagaaaPSYGLAEStcavtvp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 472 -CGAG-TVTEVTDYTTG------RVGAPLICCEIKLKDwQEGGYTINDKpnPRGEIVIGGQNISMGYFKNEEKTAEDysv 543
Cdd:PRK05851 323 vPGIGlRVDEVTTDDGSgarrhaVLGNPIPGMEVRISP-GDGAAGVAGR--EIGEIEIRGASMMSGYLGQAPIDPDD--- 396
|
330 340 350
....*....|....*....|....*....|....*..
gi 530422004 544 dengqrWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAG 580
Cdd:PRK05851 397 ------WFPTGDLGYL-VDGGLVVCGRAKELITV-AG 425
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
517-589 |
3.30e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 50.48 E-value: 3.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530422004 517 GEIVIGGQNISMGYFKNEEKTAEDysvdengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 589
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASPLVD--------GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
274-619 |
1.91e-05 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 47.30 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 274 IVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysspltlsdqss 353
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLA-QALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAG---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 354 kikkgskGDCTVLKPTLMAAVPEIMDRiyknvmSKVQEMNYIQKTLfkigydyklEQIKKGYDAPLCNLLLFKKVKALLG 433
Cdd:cd17636 67 -------GTNVFVRRVDAEEVLELIEA------ERCTHAFLLPPTI---------DQIVELNADGLYDLSSLRSSPAAPE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 434 GNvrMMLSggAPLSPQTHRFMnvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytiNDKP 513
Cdd:cd17636 125 WN--DMAT--VDTSPWGRKPG----------GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDG----REVP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 514 NPR-GEIVIGGQNISMGYFKNEEktaedysvdENGQR----WFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKV 588
Cdd:cd17636 186 DGEvGEIVARGPTVMAGYWNRPE---------VNARRtrggWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEV 255
|
330 340 350
....*....|....*....|....*....|....*
gi 530422004 589 EAALKNCPLIDNICAFAKSD----QSyVISFVVPN 619
Cdd:cd17636 256 ERCLRQHPAVADAAVIGVPDprwaQS-VKAIVVLK 289
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
128-300 |
2.00e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 47.83 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLG-KEAVVHG----------LNES 196
Cdd:PRK00174 101 YRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC-----------ARIGaVHSVVFGgfsaealadrIIDA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 197 EASYLITSVELLE----SKLKT----ALLDISCVKHIIYVdNKAINKAEYPEGFEI--HSMQSveelGSNPEnlgIPPSR 266
Cdd:PRK00174 170 GAKLVITADEGVRggkpIPLKAnvdeALANCPSVEKVIVV-RRTGGDVDWVEGRDLwwHELVA----GASDE---CEPEP 241
|
170 180 190
....*....|....*....|....*....|....*...
gi 530422004 267 PTPSDMAIVMYTSGSTGRPKGVMmhHS----NLIAGMT 300
Cdd:PRK00174 242 MDAEDPLFILYTSGSTGKPKGVL--HTtggyLVYAAMT 277
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
251-323 |
3.52e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.98 E-value: 3.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422004 251 EELGSNPENLgIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTgQCERIpGLGPKDTYIGYLPLAH 323
Cdd:PRK07867 134 DELAAHRDAE-PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVM-LAQRF-GLGPDDVCYVSMPLFH 204
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
127-310 |
5.35e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.09 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 127 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEW--MIAAQtcFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 204
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLlgMIVGS--FKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 205 VELLEskLKTALLDiscvkhiiyvdnkAINKAEYPEGFEIHSMQSVEELGSNPenlGIppsRPTPSDMAIVMYTSGSTGR 284
Cdd:PRK05691 3825 AACRE--QARALLD-------------ELGCANRPRLLVWEEVQAGEVASHNP---GI---YSGPDNLAYVIYTSGSTGL 3883
|
170 180
....*....|....*....|....*..
gi 530422004 285 PKGVMMHHsnliAGM-TGQCERIPGLG 310
Cdd:PRK05691 3884 PKGVMVEQ----RGMlNNQLSKVPYLA 3906
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
250-697 |
1.16e-04 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 45.06 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 250 VEELGSNPENLgIPPSRPtPSDMaivMYTSGSTGRPKGVMMHHS------NLIAGMTGQCeripGLGPKDTYIGYLPLAH 323
Cdd:cd05929 110 EAAEGGSPETP-IEDEAA-GWKM---LYSGGTTGRPKGIKRGLPggppdnDTLMAAALGF----GPGADSVYLSPAPLYH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 324 vleltaeiscftygcrigySSPLTLSDQSSKIkkgskGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYIqKTLF-KI 402
Cdd:cd05929 181 -------------------AAPFRWSMTALFM-----GGTLVLMEKFDPE--EFLRLIERY---RVTFAQFV-PTMFvRL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 403 gydYKL-EQIKKGYDaplcnlllfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEsCGAGTVTEVT 481
Cdd:cd05929 231 ---LKLpEAVRNAYD-----------LSSL-----KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE-GQGLTIINGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 482 DYTT--GRVGAPLicceiklkdwqEGGYTI---NDKPNPRGEI--VIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTG 554
Cdd:cd05929 291 EWLThpGSVGRAV-----------LGKVHIldeDGNEVPPGEIgeVYFANGPGFEYTNDPEKTAA--ARNEGG--WSTLG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 555 DIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKrltlLAQQ-KGVE 633
Cdd:cd05929 356 DVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVG-----------VPDEE----LGQRvHAVV 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422004 634 GTWVDICNNPAMEAEILKEIREAanamkLERFEIPIKVRLSPEPwtpetgLVTDAFKLKRKELR 697
Cdd:cd05929 420 QPAPGADAGTALAEELIAFLRDR-----LSRYKCPRSIEFVAEL------PRDDTGKLYRRLLR 472
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
277-601 |
1.59e-04 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 44.32 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 277 YTSGSTGRPKGVMMHHSNLIAGMTGQcERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIK 356
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 357 KGSKgdctvlkpTLMAAVPEIMDRIYK--NVMSKVQEMNYIQKTLFKIgydyKLEQIKKGydAPLCNLLLFkkvkallgg 434
Cdd:cd17633 86 QYNA--------TVIYLVPTMLQALARtlEPESKIKSIFSSGQKLFES----TKKKLKNI--FPKANLIEF--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 435 nvrmmlSGGAPLSPQTHRFMNvcfccpigqgygltescgagtvtevTDYTTGRVGAPLICCEIKLKDwQEGGYTindkpn 514
Cdd:cd17633 143 ------YGTSELSFITYNFNQ-------------------------ESRPPNSVGRPFPNVEIEIRN-ADGGEI------ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 515 prGEIVIGGQNISMGYFKNEEktaedYSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKN 594
Cdd:cd17633 185 --GKIFVKSEMVFSGYVRGGF-----SNPDG----WMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKA 252
|
....*..
gi 530422004 595 CPLIDNI 601
Cdd:cd17633 253 IPGIEEA 259
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-599 |
1.81e-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: 44.76 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 260 LGIPPSrptpSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL----AHVLELTAEIScft 335
Cdd:cd05910 79 IGIPKA----DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY-GIRPGEVDLATFPLfalfGPALGLTSVIP--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 336 ygcRIGYSSPLTLSDQS--SKIKKgskgdctvLKPTLMAAVPEIMDRIYKNVMSkvqemnyIQKTLfkigydykleqikk 413
Cdd:cd05910 151 ---DMDPTRPARADPQKlvGAIRQ--------YGVSIVFGSPALLERVARYCAQ-------HGITL-------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 414 gydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQTH-RFMN-VCFCCPIGQGYGLTESC------GAGTVTEVTDYTT 485
Cdd:cd05910 199 --------------------PSLRRVLSAGAPVPIALAaRLRKmLSDEAEILTPYGATEALpvssigSRELLATTTAATS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 486 GR----VGAPLICCEIKL-----KDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDI 556
Cdd:cd05910 259 GGagtcVGRPIPGVRVRIieiddEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530422004 557 GEFHPDGCLQIIDRKKDLVKLQAGEYVSLgKVEAALKNCPLID 599
Cdd:cd05910 339 GYLDDEGRLWFCGRKAHRVITTGGTLYTE-PVERVFNTHPGVR 380
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
519-610 |
2.52e-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: 44.34 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 519 IVIGGQNISMGYFKNEEKTaeDYSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 598
Cdd:cd05915 363 VQLKGPWITGGYYGNEEAT--RSALTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLENALMGHPKV 437
|
90
....*....|..
gi 530422004 599 DNICAFAKSDQS 610
Cdd:cd05915 438 KEAAVVAIPHPK 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
263-599 |
3.09e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAEISCftyGCR 339
Cdd:PRK05691 2326 LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF-GMRADDCELHFYSInfdAASERLLVPLLC---GAR 2401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 340 IgysspltlsdqsskikkgskgdctVLKPTLMAAVPEIMDRIyknvmsKVQEMNYIQktlFKIGYDYKLEQIKKGYDAPL 419
Cdd:PRK05691 2402 V------------------------VLRAQGQWGAEEICQLI------REQQVSILG---FTPSYGSQLAQWLAGQGEQL 2448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 420 cnlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCcP--IGQGYGLTESC--------------GAGTVTevtdy 483
Cdd:PRK05691 2449 ---------------PVRMCITGGEALTGEHLQRIRQAFA-PqlFFNAYGPTETVvmplaclapeqleeGAASVP----- 2507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 484 tTGR-VGAPLicceiklkdwqegGYTINDK--PNPRG---EIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTG 554
Cdd:PRK05691 2508 -IGRvVGARV-------------AYILDADlaLVPQGatgELYVGGAGLAQGYHDRPGLTAERFVADpfaADGGRLYRTG 2573
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530422004 555 DIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLID 599
Cdd:PRK05691 2574 DLVRLRADGLVEYVGRIDHQVKIR-GFRIELGEIESRLLEHPAVR 2617
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
48-323 |
7.40e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 43.17 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 48 AKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAvskfgkKDSLGtrEILSEENEMQPNGKVFkkliLGNYKWMN 127
Cdd:PRK07868 407 ARGAADAAVAANRSVRTLAVETARTLPRLARLGQINDHT------RISLG--RIIAEQARDAPKGEFL----LFDGRVHT 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAaqtcfkynfplVTLYATLGKEAVV----HGLNES----EAS 199
Cdd:PRK07868 475 YEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVA-----------IAALSRLGAVAVLmppdTDLAAAvrlgGVT 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 200 YLITSVELLESKLKTALldiscvkHIIYVDNKAINKAEYPEGFEIHSMQSVEelgsnPENLGIPP-SRPTPS---DMAIV 275
Cdd:PRK07868 544 EIITDPTNLEAARQLPG-------RVLVLGGGESRDLDLPDDADVIDMEKID-----PDAVELPGwYRPNPGlarDLAFI 611
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 530422004 276 MY-TSGSTGRPKGVMMHHSNLIAGMTGQCERipgLGPKDTYIGYLPLAH 323
Cdd:PRK07868 612 AFsTAGGELVAKQITNYRWALSAFGTASAAA---LDRRDTVYCLTPLHH 657
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
443-596 |
7.88e-04 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 42.48 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 443 GAPLSPQT-HRFMNVCfCCPIGQGYGLTEScgagTVTEVT----DYTTGRVGAPLICCEIKLKDwQEGGYTindKPNPRG 517
Cdd:cd05970 310 GEALNPEVfNTFKEKT-GIKLMEGFGQTET----TLTIATfpwmEPKPGSMGKPAPGYEIDLID-REGRSC---EAGEEG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 518 EIVI---GGQNISM--GYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 592
Cdd:cd05970 381 EIVIrtsKGKPVGLfgGYYKDAEKTAE---VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESAL 454
|
....
gi 530422004 593 KNCP 596
Cdd:cd05970 455 IQHP 458
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
128-324 |
1.87e-03 |
|
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: 41.51 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 128 YLEVNRRVNNFGSGL-TALGLKPKNTIAIFC--ETRAEWM---IAAQTCfkynfPLVTLYATLGKEAVVHGLNESEASYL 201
Cdd:cd05938 8 YRDVDRRSNQAARALlAHAGLRPGDTVALLLgnEPAFLWIwlgLAKLGC-----PVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422004 202 ITSVELLES------KLKTALLdiscvkHIIYVDNKAInkaeyPEGFeIHSMQSVEELGSNPenlgIPPS---RPTPSDM 272
Cdd:cd05938 83 VVAPELQEAveevlpALRADGV------SVWYLSHTSN-----TEGV-ISLLDKVDAASDEP----VPASlraHVTIKSP 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530422004 273 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQceRIPGLGPKDTYIGYLPLAHV 324
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISHLRVLQCSGFL--SLCGVTADDVIYITLPLYHS 196
|
|
| |
