|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
80-655 |
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: 833.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 159
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 LITSvellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrPTPSDMAIVMYTSG 239
Cdd:cd17639 81 IFTD--------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 240 STGRPKGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqssKIKKGS 318
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 319 KGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVKALLGGNVRMM 398
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 399 LSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYtINDKPNPRGEI 478
Cdd:cd17639 256 LSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGY-STDKPPPRGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 479 VIGGQNISMGYFKNEEKTAEDYsvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLID 558
Cdd:cd17639 334 LIRGPNVFKGYYKNPEKTKEAF----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 559 NICAFAKSDQSYVISFVVPNQKRLTLLAQQKGV-EGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPW 637
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 4758332 638 TPETGLVTDAFKLKRKEL 655
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
24-667 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 812.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 24 FDSLavIDIP--GADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWMNYLEVNRRVNNFGSGL 101
Cdd:PLN02387 46 FPEL--VETPweGATTLAALFEQSCKKYSDKRLLGTRKLISREFETSSDGRKFEKLHLGEYEWITYGQVFERVCNFASGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 102 TALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEllesKLKTaLLDIS-- 179
Cdd:PLN02387 124 VALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK----QLKK-LIDISsq 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 180 --CVKHIIYVDNKAINKAEYPEGFE---IHSMQSVEELG-SNPenlgIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSN 253
Cdd:PLN02387 199 leTVKRVIYMDDEGVDSDSSLSGSSnwtVSSFSEVEKLGkENP----VDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 254 LIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAV 333
Cdd:PLN02387 275 IVATVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTLMTAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 334 PEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKK------GYDAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSP 407
Cdd:PLN02387 355 PAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGswfgawGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 408 QTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISM 487
Cdd:PLN02387 435 DTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTL 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 488 GYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:PLN02387 515 GYFKNQEKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPF 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 568 QSYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTD 646
Cdd:PLN02387 595 HSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTA 674
|
650 660
....*....|....*....|.
gi 4758332 647 AFKLKRKELRNHYLKDIERMY 667
Cdd:PLN02387 675 ALKLKREQIRKKFKDDLKKLY 695
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
80-667 |
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: 536.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNT--IAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEA 157
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 158 SylitsvellesklktalldiscvkhIIYVDnkainkaeypEGFEIHSMQSVEELGSNPEnlgIPPSRPTPSDMAIVMYT 237
Cdd:cd05927 81 S-------------------------IVFCD----------AGVKVYSLEEFEKLGKKNK---VPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 238 SGSTGRPKGVMMHHSNLIAGMTGQC---ERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSS--PLTLSDqss 312
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 313 kikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKG--YDAPLCNLLLFKKVKAL 390
Cdd:cd05927 200 --------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 391 LGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTIND 470
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 471 kPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAA 550
Cdd:cd05927 352 -PNPRGEVCIRGPNVFSGYYKDPEKTAE--ALDEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 551 LKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQK-GVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIK 629
Cdd:cd05927 427 YARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKA 506
|
570 580 590
....*....|....*....|....*....|....*...
gi 4758332 630 VRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 667
Cdd:cd05927 507 IHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
31-670 |
1.90e-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: 1.90e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 31 DIPGADTLDKLFDHAVSKFGKKDSLGTREilseenemqpngkvfkkliLGNYKWMNYLEVNRRVNNFGSGLTALGLKPKN 110
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKE-------------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 111 TIAIFCETRAEWMIA--------AQTcfkynfplVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVK 182
Cdd:COG1022 67 RVAILSDNRPEWVIAdlailaagAVT--------VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 183 HIIYVDNKAInkaeyPEGFEIHSMQSVEELG---SNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT 259
Cdd:COG1022 139 HIVVLDPRGL-----RDDPRLLSLDELLALGrevADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 260 GQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYS-SPLTLSDqsskikkgskgDCTVLKPTLMAAVPEIMD 338
Cdd:COG1022 214 ALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------DLREVKPTFMLAVPRVWE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 339 RIYKNVMSKVQEMNYIQKTLF----KIGYDYKlEQIKKGYDAP--------LCNLLLFKKVKALLGGNVRMMLSGGAPLS 406
Cdd:COG1022 282 KVYAGIQAKAEEAGGLKRKLFrwalAVGRRYA-RARLAGKSPSlllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 407 PQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKlkdwqeggytINDKpnprGEIVIGGQ 483
Cdd:COG1022 361 PELARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK----------IAED----GEILVRGP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 484 NISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAF 563
Cdd:COG1022 423 NVMKGYYKNPEATAE--AFDADG--WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVV 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 564 AkSDQSYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEPWTPETG 642
Cdd:COG1022 499 G-DGRPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEV-DRANA-GLSRAEQIKRFRLLPKEFTIENG 575
|
650 660
....*....|....*....|....*...
gi 4758332 643 LVTDAFKLKRKELRNHYLKDIERMYGGK 670
Cdd:COG1022 576 ELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
15-667 |
2.00e-153 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 458.41 E-value: 2.00e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 15 GSPYRSVTHFDslaviDIPGADTLDKLFDHAVSKFGKKDSLGTReilseeneMQPNGKVfkklilGNYKWMNYLEVNRRV 94
Cdd:PLN02736 28 RSPLKLVSRFP-----DHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 95 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLkTA 174
Cdd:PLN02736 89 TAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLL-SC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 175 LLDISCVKHIIYV--DNKAINKAEYPEGFEIHSMQSVEELG-SNPEnlgiPPSRPTPSDMAIVMYTSGSTGRPKGVMMHH 251
Cdd:PLN02736 168 LSEIPSVRLIVVVggADEPLPSLPSGTGVEIVTYSKLLAQGrSSPQ----PFRPPKPEDVATICYTSGTTGTPKGVVLTH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 252 SNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSP--LTLSDqsskikkgskgDCTVLKPTL 329
Cdd:PLN02736 244 GNLIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGdnLKLMD-----------DLAALRPTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 330 MAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD-APLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQ 408
Cdd:PLN02736 312 FCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 409 THRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMG 488
Cdd:PLN02736 392 VMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 489 YFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:PLN02736 472 YYKDEVQTRE--VIDEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLN 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 569 SYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDA 647
Cdd:PLN02736 548 SSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPT 627
|
650 660
....*....|....*....|
gi 4758332 648 FKLKRKELRNHYLKDIERMY 667
Cdd:PLN02736 628 FKVKRPQAKAYFAKAISDMY 647
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
83-667 |
2.24e-144 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 436.72 E-value: 2.24e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 83 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT 162
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 163 S---VELLESKLKTALLDiSCVkhIIYVDnkainkaEYPEGFEIHSMQ-----SVEELG-SNPENLgiPPSRPTPSD-MA 232
Cdd:PTZ00216 200 NgknVPNLLRLMKSGGMP-NTT--IIYLD-------SLPASVDTEGCRlvawtDVVAKGhSAGSHH--PLNIPENNDdLA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 233 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGL-GPK---DTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLS 308
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGPPeedETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 309 DQSSKikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVK 388
Cdd:PTZ00216 348 DTFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 389 ALLGGNVRMMLSGGAPLSPQTHRFMNVCFcCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEggYTI 468
Cdd:PTZ00216 424 AVLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEE--YKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 469 NDKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVE 548
Cdd:PTZ00216 501 TDTPEPRGEILLRGPFLFKGYYKQEELTRE--VLDEDG--WFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALE 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 549 AALKNCPLIDN--ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEI 626
Cdd:PTZ00216 577 ALYGQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 4758332 627 PIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 667
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 ... |
80-655 |
5.39e-136 |
|
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: 5.39e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 159
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 LITSvellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrpTPSDMAIVMYTSG 239
Cdd:cd05907 81 LFVE---------------------------------------------------------------DPDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 240 STGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRIGYSSPL-TLSDQSSKIkkg 317
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAeTLLDDLSEV--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 318 skgdctvlKPTLMAAVPEIMDRIYKNVmsKVQEMNYIQKTLFKIGydykleqikkgydaplcnlllfkkvkalLGGNVRM 397
Cdd:cd05907 174 --------RPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLA----------------------------VGGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 398 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytindkpnpRGE 477
Cdd:cd05907 216 AASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--------------DGE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 478 IVIGGQNISMGYFKNEEKTAEDysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 557
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAEA--LDADG--WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLI 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 558 DNICAFAkSDQSYVISFVVPNQKRLTLLAQQKGVEGTWV-DICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEP 636
Cdd:cd05907 357 SQAVVIG-DGRPFLVALIVPDPEALEAWAEEHGIAYTDVaELAANPAVRAEIEAAV-EAANA-RLSRYEQIKKFLLLPEP 433
|
570
....*....|....*....
gi 4758332 637 WTPETGLVTDAFKLKRKEL 655
Cdd:cd05907 434 FTIENGELTPTLKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
3-667 |
1.04e-122 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 379.54 E-value: 1.04e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 3 KRIKAKPTSdkpGSPYRSVTHFDSLAVIDiPGADTLDKLFDHAVSKFGKKDSLGTREILseenemqpNGKVfkklilGNY 82
Cdd:PLN02430 13 KGKDGKPSV---GPVYRNLLSKKGFPPID-SDITTAWDIFSKSVEKYPDNKMLGWRRIV--------DGKV------GPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 83 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEasylIT 162
Cdd:PLN02430 75 MWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAE----ID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 163 SVELLESKLKtALLDISC-----VKHIIYVDN---KAINKAEyPEGFEIHSMQSVEELG-SNPENlgipPSRPTPSDMAI 233
Cdd:PLN02430 151 FVFVQDKKIK-ELLEPDCksakrLKAIVSFTSvteEESDKAS-QIGVKTYSWIDFLHMGkENPSE----TNPPKPLDICT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 234 VMYTSGSTGRPKGVMMHHSNLIAGMTG------QCEriPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltl 307
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGvdlfmeQFE--DKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYH---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 308 SDQSSKikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLLL 383
Cdd:PLN02430 299 GDLNAL-----RDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 FKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPLICCEIKLKDWQ 462
Cdd:PLN02430 374 FRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 463 EGGYTINDKPnPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYV 542
Cdd:PLN02430 454 EMGYDPLGEP-PRGEICVRGKCLFSGYYKNPELTEE---VMKDG--WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 543 SLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLE 622
Cdd:PLN02430 528 ALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLR 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 4758332 623 RFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 667
Cdd:PLN02430 608 GFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
6-667 |
1.27e-116 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 363.78 E-value: 1.27e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 6 KAKPTSD-KP--GSPYRSVTHFDSLavIDIP-GADTLDKLFDHAVSKFGKKDSLGTREILseenemqpNGKVfkklilGN 81
Cdd:PLN02861 11 ESRPATGgKPsaGPVYRSIYAKDGL--LDLPaDIDSPWQFFSDAVKKYPNNQMLGRRQVT--------DSKV------GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 82 YKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASylI 161
Cdd:PLN02861 75 YVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 162 TSVEllESKLKTALldiSCVKH--------IIYVDNKAINKAEYPE-GFEIHSMQSVEELGSNPENLgiPPSRPTpsDMA 232
Cdd:PLN02861 153 AFVQ--ESKISSIL---SCLPKcssnlktiVSFGDVSSEQKEEAEElGVSCFSWEEFSLMGSLDCEL--PPKQKT--DIC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 233 IVMYTSGSTGRPKGVMMHHSNLIAG------MTGQCERIpgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSplt 306
Cdd:PLN02861 224 TIMYTSGTTGEPKGVILTNRAIIAEvlstdhLLKVTDRV--ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQ--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 lSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLL 382
Cdd:PLN02861 299 -GDIRYLME-----DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 383 LFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGaGTVTEVTDY--TTGRVGAPLICCEIKLKD 460
Cdd:PLN02861 373 VFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANVfsMVGTVGVPMTTIEARLES 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 461 WQEGGY-TINDKPnpRGEIVIGGQNISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 539
Cdd:PLN02861 452 VPEMGYdALSDVP--RGEICLRGNTLFSGYHKRQDLTEEVLI-----DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQG 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 540 EYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM 619
Cdd:PLN02861 525 EYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 4758332 620 KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 667
Cdd:PLN02861 605 QLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
7-667 |
8.76e-114 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 356.25 E-value: 8.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 7 AKPTSD-KP--GSPYRSVTHFDSLAViDIPGADTLDKLFDHAVSKFGKKDSLGTREILseenemqpNGKVfkklilGNYK 83
Cdd:PLN02614 14 GKEGSDgRPsvGPVYRSIFAKDGFPN-PIEGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 84 WMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 163
Cdd:PLN02614 79 WQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 164 VELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE--GFEIHSMQSVEELGSNPEnLGIPPSRPtpSDMAIVMYTSGST 241
Cdd:PLN02614 159 EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLGEGKQ-YDLPIKKK--SDICTIMYTSGTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 242 GRPKGVMMHHSNLIAGMTGQCERI----PGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQSSKIKkg 317
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAGVIRLLksanAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR----GDVKLLIE-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 318 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLLLFKKVKALLGG 393
Cdd:PLN02614 310 ---DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 394 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCgAGTVTEVTDY--TTGRVGAPLICCEIKLKDWQEGGYTINDK 471
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVDIRLESVPEMEYDALAS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 472 pNPRGEIVIGGQNISMGYFKNEEKTAEDYsVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAAL 551
Cdd:PLN02614 466 -TPRGEICIRGKTLFSGYYKREDLTKEVL-IDG----WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIY 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 552 KNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVR 631
Cdd:PLN02614 540 GEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIH 619
|
650 660 670
....*....|....*....|....*....|....*.
gi 4758332 632 LSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMY 667
Cdd:PLN02614 620 LDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
77-537 |
9.00e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 345.45 E-value: 9.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 77 LILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESE 156
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 157 ASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEypegfeihsmqSVEELGSNPENLGIPPSRPTPSDMAIVMY 236
Cdd:pfam00501 94 AKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 237 TSGSTGRPKGVMMHHSNLIAGMTGQ---CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSPLTLSDQss 312
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALDP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 313 kikKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmskvqemnyiqktlfkigydykleqikkgydaplcnlllfKKVKALLG 392
Cdd:pfam00501 241 ---AALLELIERYKVTVLYGVPTLLNMLLEA-----------------------------------------GAPKRALL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 393 GNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDWQEGGYTin 469
Cdd:pfam00501 277 SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPlplDEDLRSLGSVGRPLPGTEVKIVDDETGEPV-- 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758332 470 dKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQ 537
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 ... |
80-652 |
4.68e-71 |
|
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: 4.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFkynfplvtlyaTLGKEAVVHGLNES--EA 157
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIM-----------ALGAVDVVRGSDSSveEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 158 SYLITSVEllesklktalldisCVkhIIYVDNkainkaeypegfeihsmqsveelgsnpenlgippsrpTPSDMAIVMYT 237
Cdd:cd17640 70 LYILNHSE--------------SV--ALVVEN-------------------------------------DSDDLATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 238 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGlGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkg 317
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPP-QPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKD-------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 318 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIgydykleqikkgydaplcnlllfkkvkALLGGNVRM 397
Cdd:cd17640 168 ---DLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF---------------------------FLSGGIFKF 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 398 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTindKPNPRGE 477
Cdd:cd17640 218 GISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVL---PPGEKGI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 478 IVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 557
Cdd:cd17640 294 VWVRGPQVMKGYYKNPEATSK--VLDSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFI 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 558 DNICAFAKsDQSYVISFVVPNQKRLTLLAQQKGV---EGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSP 634
Cdd:cd17640 370 EQIMVVGQ-DQKRLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLE 448
|
570
....*....|....*...
gi 4758332 635 EPWTpETGLVTDAFKLKR 652
Cdd:cd17640 449 EPFI-ENGEMTQTMKIKR 465
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
85-662 |
3.65e-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: 3.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 164
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpsdmAIVMYTSGSTGRP 244
Cdd:COG0318 103 -------------------------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI---GYSSPLTLSDQsskIKKGskg 320
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAAL-GLTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLvllPRFDPERVLEL---IERE--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 321 dctvlKPTLMAAVPEIMDRiyknvmskvqemnyiqktlfkigydykleqikkgydapLCNLLLFKKVKAllgGNVRMMLS 400
Cdd:COG0318 189 -----RVTVLFGVPTMLAR--------------------------------------LLRHPEFARYDL---SSLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 401 GGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDwqeggytINDKPNPR-- 475
Cdd:COG0318 223 GGAPLPPELlERFEER-FGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVD-------EDGRELPPge 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 476 -GEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNC 554
Cdd:COG0318 295 vGEIVVRGPNVMKGYWNDPEATAE---AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAH 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 555 PLIDNICAFAKSDQSY---VISFVVPNqkrltllaqqkgvEGTWVDicnnpamEAEILKEIREaanamKLERFEIPIKVR 631
Cdd:COG0318 369 PGVAEAAVVGVPDEKWgerVVAFVVLR-------------PGAELD-------AEELRAFLRE-----RLARYKVPRRVE 423
|
570 580 590
....*....|....*....|....*....|..
gi 4758332 632 LSPE-PWTPeTGlvtdafKLKRKELRNHYLKD 662
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 ... |
84-624 |
4.44e-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: 4.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 84 WMNYLEvnrRVNNFGSGLTALGLKPKNTIAIFCETRAEW---MIAAQTCFKYNFPLvtlYATLGKEAVVHGLNESEASYL 160
Cdd:cd17641 14 WADYAD---RVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALSLGI---YQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPEgfeIHSMQSVEELG-----SNPENLGIPPSRPTPSDMAIVM 235
Cdd:cd17641 88 IAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPR---LISFEDVVALGraldrRDPGLYEREVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 236 YTSGSTGRPKGVMMHHSNLIaGMTGQCERIPGLGPKDTYIGYLPLAHVLELT-----AEISCFTYGCrigYSSPLTLsdq 310
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFL-GHCAAYLAADPLGPGDEYVSVLPLPWIGEQMysvgqALVCGFIVNF---PEEPETM--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 311 sskikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYD--YK-LEQIKKGYDAP--------LC 379
Cdd:cd17641 238 --------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKlgLRaLDRGKRGRPVSlwlrlaswLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 380 NLLLFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCE 455
Cdd:cd17641 310 DALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 456 IKLKDwqeggytindkpnpRGEIVIGGQNISMGYFKNEEKTAEDysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 535
Cdd:cd17641 386 VRIDE--------------VGEILVRSPGVFVGYYKNPEATAED--FDEDG--WLHTGDAGYFKENGHLVVIDRAKDVGT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 536 LQAGEYVSLGKVEAALKNCPLIDNICAFAKsDQSYVISFVVPNQKRLTLLAQQKGVE-GTWVDICNNPAMEAEILKEIRE 614
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAEAVVLGA-GRPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEK 526
|
570
....*....|....
gi 4758332 615 A----ANAMKLERF 624
Cdd:cd17641 527 VnaslPEAQRIRRF 540
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
80-659 |
1.10e-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: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 159
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 LITSvellesKLKtalldiscvkhiiyvDNKAInKAEYPEGFEIHSMQSVEELGSNPENLGI----PPS----RPTPSDM 231
Cdd:cd05932 82 LFVG------KLD---------------DWKAM-APGVPEGLISISLPPPSAANCQYQWDDLiaqhPPLeerpTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 232 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTA-EISCFTYGCRIGYSSPLTLSDQ 310
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 311 sskikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKV--QEMNyiqkTLFKIgydykleqikkgydaPLCNLLLFKKVK 388
Cdd:cd05932 219 ----------DVQRARPTLFFSVPRLWTKFQQGVQDKIpqQKLN----LLLKI---------------PVVNSLVKRKVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 389 ALLGGN-VRMMLSGGAPLSPQT-HRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggy 466
Cdd:cd05932 270 KGLGLDqCRLAGCGSAPVPPALlEWYRSLGL--NILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 467 tindkpnpRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGK 546
Cdd:cd05932 342 --------DGEILVRSPALMMGYYKDPEATAE--AFTADG--FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAP 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 547 VEAALKNCPLIDNICAFAkSDQSYVISFVVPNQK-RLTLLAQQKGvegtwvdicnnpAMEAEiLKEIREAANAmKLERFE 625
Cdd:cd05932 410 IENKLAEHDRVEMVCVIG-SGLPAPLALVVLSEEaRLRADAFARA------------ELEAS-LRAHLARVNS-TLDSHE 474
|
570 580 590
....*....|....*....|....*....|....
gi 4758332 626 IPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHY 659
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 ... |
230-579 |
2.45e-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: 2.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI---GYSSPLT 306
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LSDqssKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQIK-KGYDAPlcnlllfk 385
Cdd:cd04433 80 ALE---LIER--------EKVTILLGVPTLLARL--------------------------LKAPEsAGYDLS-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 386 kvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwQE 463
Cdd:cd04433 115 --------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPVPGVEVRIVD-PD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 464 GGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVS 543
Cdd:cd04433 186 GGEL---PPGEIGELVVRGPSVMKGYWNNPEATAA---VDEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVY 256
|
330 340 350
....*....|....*....|....*....|....*....
gi 4758332 544 LGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 579
Cdd:cd04433 257 PAEVEAVLLGHPGVAEAAVVGVPDPEWgerVVAVVVLRP 295
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
85-567 |
4.06e-53 |
|
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: 190.12 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLEsKLKTALLDISCVKHIIYVDNKAiNKAEYPEgfeihsmQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:cd05911 91 DGLE-KVKEAAKELGPKDKIIVLDDKP-DGVLSIE-------DLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVleltaeiscftYGCRIGYSSPLtlsdqsskikkgsKGdCT 323
Cdd:cd05911 162 KGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHI-----------YGLFTTLASLL-------------NG-AT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 324 VLkptlmaavpeIMDRIYKNVMskvqeMNYIQKtlfkigydYKleqIKKGYDAPLCNLLLFK---KVKALLGgNVRMMLS 400
Cdd:cd05911 217 VI----------IMPKFDSELF-----LDLIEK--------YK---ITFLYLVPPIAAALAKsplLDKYDLS-SLRVILS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 401 GGAPLSPQTHRFMNVCFC-CPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGytiNDKPNPRGEIV 479
Cdd:cd05911 270 GGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKD---SLGPNEPGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 480 IGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDN 559
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKE--TFDEDG--WLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHPGVAD 421
|
....*...
gi 4758332 560 ICAFAKSD 567
Cdd:cd05911 422 AAVIGIPD 429
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
87-652 |
2.12e-52 |
|
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: 187.65 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSvel 166
Cdd:cd05914 10 YKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 lesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsNPEnlgippsrptpsDMAIVMYTSGSTGRPKG 246
Cdd:cd05914 87 ------------------------------------------------DED------------DVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVLELtaeisCFTYGCRIGYSSPLTLSDQ--SSKIKKGSKGDctv 324
Cdd:cd05914 107 VMLTYRNIVSNVDG-VKEVVLLGKGDKILSILPLHHIYPL-----TFTLLLPLLNGAHVVFLDKipSAKIIALAFAQ--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LKPTLMAAVPEIMDRIYKNVmskVQEMNYIQKTLFKIGYDYKLEQIKKgydaplcnlLLFKKVKALLGGNVRMMLSGGAP 404
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMD---IIPKLTLKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 405 LSPQTHRF---MNVCFCcpigQGYGLTES----CGAGTVTEVTDyttgRVGAPLICCEIKLkdwqeggytinDKPNPR-- 475
Cdd:cd05914 246 INPDVEEFlrtIGFPYT----IGYGMTETapiiSYSPPNRIRLG----SAGKVIDGVEVRI-----------DSPDPAtg 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 476 -GEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNC 554
Cdd:cd05914 307 eGEIIVRGPNVMKGYYKNPEATAE--AFDKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNM 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 555 PLIdnicafaksdqsyVISFVVPNQKRLTLLA-------QQKGVegtwvdicNNPAMEAEILKEIREAANaMKLERFEIP 627
Cdd:cd05914 383 PFV-------------LESLVVVQEKKLVALAyidpdflDVKAL--------KQRNIIDAIKWEVRDKVN-QKVPNYKKI 440
|
570 580
....*....|....*....|....*
gi 4758332 628 IKVRLSPEPWtPETGLvtdaFKLKR 652
Cdd:cd05914 441 SKVKIVKEEF-EKTPK----GKIKR 460
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
37-555 |
3.80e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 185.39 E-value: 3.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 37 TLDKLFDHAVSKFGKKdslgtrEILSEEnemqpnGKVFkklilgnykwmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFC 116
Cdd:PRK06187 7 TIGRILRHGARKHPDK------EAVYFD------GRRT-----------TYAELDERVNRLANALRALGVKKGDRVAVFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 117 ETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESkLKTALLDISCVKHIIYVDNKAiNKAE 196
Cdd:PRK06187 64 WNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPL-LAAILPQLPTVRTVIVEGDGP-AAPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 197 YPEGFEIHSMqsveeLGSNPENLGIPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIG 276
Cdd:PRK06187 142 APEVGEYEEL-----LAAASDTFDFPD--IDENDAAAMLYTSGTTGHPKGVVLSHRNLFL-HSLAVCAWLKLSRDDVYLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 277 YLPLAHVLELTAEISCFTYGCRIGYS---SPLTLSDQsskIKKgskgdctvLKPTLMAAVPEIMdriyknvmskvqemNY 353
Cdd:PRK06187 214 IVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPTIW--------------QM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 354 IQKTLFKIGYDYkleqikkgydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCG 432
Cdd:PRK06187 269 LLKAPRAYFVDF---------------------------SSLRLVIYGGAALPPALlREFKEK-FGIDLVQGYGMTETSP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 433 AGTVTEVTDYTTGR------VGAPLICCEIKLKD--WQE---GGYTIndkpnprGEIVIGGQNISMGYFKNEEKTAEDYs 501
Cdd:PRK06187 321 VVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVDddGDElppDGGEV-------GEIIVRGPWLMQGYWNRPEATAETI- 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 4758332 502 vdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCP 555
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 ... |
80-667 |
9.61e-50 |
|
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: 183.33 E-value: 9.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKW--MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAA-QTCFKYNFpLVTLYATLGKEAVVHGLNESE 156
Cdd:cd05933 2 RGDKWhtLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAvGAIFAGGI-AVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 157 ASYLItsVE---------LLESKLKTalldiscVKHIIyvdnkainkaEYPEGFEIH-----SMQSVEELG-SNPEN-LG 220
Cdd:cd05933 81 ANILV--VEnqkqlqkilQIQDKLPH-------LKAII----------QYKEPLKEKepnlySWDEFMELGrSIPDEqLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 221 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL--IAGMTGQ-CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYG 296
Cdd:cd05933 142 AIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNItwTAKAASQhMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 297 CRIGYSSPLTLsdqsskikKGSKGDcTV--LKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLF----KIGYDYKLEQI 370
Cdd:cd05933 222 GQVYFAQPDAL--------KGTLVK-TLreVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 371 KKGYDAPLC----NLLLFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDY 442
Cdd:cd05933 293 GGESPSPLFyrlaKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 443 TTGRVGAPLICCEIKLkdwqeggytINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDG 522
Cdd:cd05933 369 RLLSCGKALPGCKTKI---------HNPDADGIGEICFWGRHVFMGYLNMEDKTEE--AIDEDG--WLHSGDLGKLDEDG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 523 CLQIIDRKKDLVKLQAGEYVSLGKVEAALKN-CPLIDNicAFAKSDQSYVISFVVP-----NQK------RLTLLA---- 586
Cdd:cd05933 436 FLYITGRIKELIITAGGENVPPVPIEDAVKKeLPIISN--AMLIGDKRKFLSMLLTlkcevNPEtgepldELTEEAiefc 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 587 QQKGVEGTWVDICNN---PAMEAEILKEIREA-----ANAMKLERFEIpikvrlSPEPWTPETGLVTDAFKLKRKELRNH 658
Cdd:cd05933 514 RKLGSQATRVSEIAGgkdPKVYEAIEEGIKRVnkkaiSNAQKIQKWVI------LEKDFSVPGGELGPTMKLKRPVVAKK 587
|
....*....
gi 4758332 659 YLKDIERMY 667
Cdd:cd05933 588 YKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
38-645 |
1.35e-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: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 38 LDKLFDHAVSKFGKKDSLGTREilSEENEMQPNGKVFKKLiLGNYKWMNYLEVNRRVNNFGSGL-TALGLKPKNTIAIFC 116
Cdd:cd17632 24 LAQIIATVMTGYADRPALGQRA--TELVTDPATGRTTLRL-LPRFETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 117 ETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKtALLDISCVKHIIYVDNKA----- 191
Cdd:cd17632 101 FTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVE-AVLEGGTPPRLVVFDHRPevdah 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 192 --------INKAEYPEGFEIHSMQSVEELGSNPEnlgiPPSRPTPSDMAIVM--YTSGSTGRPKGVMMHHSNLIAGMTGQ 261
Cdd:cd17632 180 raalesarERLAAVGIPVTTLTLIAVRGRDLPPA----PLFRPEPDDDPLALliYTSGSTGTPKGAMYTERLVATFWLKV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 262 CERIPGLGPKDTYIGYLPLAHVLeltAEISCFTYGCRIGYSSPLTLSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIY 341
Cdd:cd17632 256 SSIQDIRPPASITLNFMPMSHIA---GRISLYGTLARGGTAYFAAASDMSTLFD-----DLALVRPTELFLVPRVCDMLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 342 KNVMSKVqemnyiqktlfkigyDYKLEQikkGYDAplcnLLLFKKVKA-----LLGGNVRMMLSGGAPLSPQTHRFMNVC 416
Cdd:cd17632 328 QRYQAEL---------------DRRSVA---GADA----ETLAERVKAelrerVLGGRLLAAVCGSAPLSAEMKAFMESL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 417 FCCPIGQGYGLTEscgAGTVT--------EVTDYttgrvgaplicceiKLKDWQEGGYTINDKPNPRGEIVIGGQNISMG 488
Cdd:cd17632 386 LDLDLHDGYGSTE---AGAVIldgvivrpPVLDY--------------KLVDVPELGYFRTDRPHPRGELLVKTDTLFPG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 489 YFKNEEKTAEDYsvDENGqrWFCTGDI-GEFHPDGcLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:cd17632 449 YYKRPEVTAEVF--DEDG--FYRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSE 523
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758332 568 QSYVISFVVPNQKRLTLLAQQkgvegtwvdicnnpAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVT 645
Cdd:cd17632 524 RAYLLAVVVPTQDALAGEDTA--------------RLRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
83-534 |
8.63e-44 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 163.89 E-value: 8.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 83 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT 162
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 163 SVELlesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsvEELGSNPENLGIPPSRpTPSDMAIVMYTSGSTG 242
Cdd:cd05936 103 AVSF-------------------------------------------TDLLAAGAPLGERVAL-TPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 243 RPKGVMMHHSNLIAGMTgQCERI--PGLGPKDTYIGYLPLAHVLELTAeisCFTYGCRIGYS-------SPLTLSDQssk 313
Cdd:cd05936 139 VPKGAMLTHRNLVANAL-QIKAWleDLLEGDDVVLAALPLFHVFGLTV---ALLLPLALGATivliprfRPIGVLKE--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 314 IKKGskgdctvlKPTLMAAVPeimdriyknvmskvqemnyiqkTLFkIGydykleqikkgydaplcnLLLFKKVKALLGG 393
Cdd:cd05936 212 IRKH--------RVTIFPGVP----------------------TMY-IA------------------LLNAPEFKKRDFS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 394 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKDwqeggytINDKP 472
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-------DDGEE 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758332 473 NPR---GEIVIGGQNISMGYFKNEEKTAEDYsVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
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 ... |
87-535 |
8.58e-41 |
|
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: 8.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEwmiaaqtcfkynFPLVTLYAT-LGkeAVVHGLN------------ 153
Cdd:cd05904 35 YAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIE------------FPVAFLAVLsLG--AVVTTANplstpaeiakqv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 154 -ESEASYLITSVELLEsKLKTALLDISCVkhiiyvdnkainkaeypEGFEIHSMQSVEELGSNPENlGIPPSRPTPSDMA 232
Cdd:cd05904 101 kDSGAKLAFTTAELAE-KLASLALPVVLL-----------------DSAEFDSLSFSDLLFEADEA-EPPVVVIKQDDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 233 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERI-PGLGPKDTYIGYLPLAHVLELTaeiSCFTYGCRIG--------YSS 303
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLS---SFALGLLRLGatvvvmprFDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 304 PLTLSdqssKIKKgskgdctvLKPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigydykleqikkGYDaplcnlll 383
Cdd:cd05904 239 EELLA----AIER--------YKVTHLPVVPPIVLALVKSPIVD-------------------------KYD-------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 fkkVKALlggnvRMMLSGGAPLSPQT-----HRFMNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVG-----APLIc 453
Cdd:cd05904 274 ---LSSL-----RQIMSGAAPLGKELieafrAKFPNV----DLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNV- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 454 cEIKLKDWQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDL 533
Cdd:cd05904 341 -EAKIVDPETGESL---PPNQTGELWIRGPSIMKGYLNNPEATAA--TIDKEG--WLHTGDLCYIDEDGYLFIVDRLKEL 412
|
..
gi 4758332 534 VK 535
Cdd:cd05904 413 IK 414
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
228-542 |
4.31e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 157.19 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCER--IPGLGPKdTYIGYLPLAHVLELTAEISCFTYGCRIgysspl 305
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsiFKKYNPK-THLSYLPISHIYERVIAYLSFMLGGTI------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 306 tlsDQSSK-IKKGSKgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKigydyKLEQIKKG-YDAPLCNLL- 382
Cdd:PTZ00342 376 ---NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVK-----KILSLRKSnNNGGFSKFLe 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 383 ----LFKKVKALLGGNVRMMLSGGAPLSPQTHR----FMNVCFCcpigQGYGLTESCGAGTVTEVTDYTTGRVGAPlIC- 453
Cdd:PTZ00342 447 githISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYGLTETTGPIFVQHADDNNTESIGGP-ISp 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 454 -CEIKLKDWQEggYTINDKPnPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PTZ00342 522 nTKYKVRTWET--YKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTED----GYFKTGDIVQINKNGSLTFLDRSKG 594
|
330
....*....|
gi 4758332 533 LVKLQAGEYV 542
Cdd:PTZ00342 595 LVKLSQGEYI 604
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
80-657 |
2.53e-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: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAaqtcfkynfplvtLYATLGKEAVVHGLNeseASY 159
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVA-------------FLAAARAGAVVAPLN---PAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 LITSVELLESKLKTALL------DISCVKHIIYVDNKAINKAEypEGFEIHSMQSVEELGsNPENLGI---PPSRPTPSD 230
Cdd:cd05926 74 KKAEFEFYLADLGSKLVltpkgeLGPASRAASKLGLAILELAL--DVGVLIRAPSAESLS-NLLADKKnakSEGVPLPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 231 MAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEI--SCFTYGCrigysspLTLS 308
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNIT-NTYKLTPDDRTLVVMPLFHVHGLVASLlsTLAAGGS-------VVLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 309 DQSSkikkGSK--GDCTVLKPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigydykleqikkgydaplcnlllFKK 386
Cdd:cd05926 223 PRFS----ASTfwPDVRDYNATWYTAVPTIHQILLNRPEPN------------------------------------PES 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 387 VKALLggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLiccEIKLKDWQEG 464
Cdd:cd05926 263 PPPKL----RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPV---GVEVRILDED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 465 GYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSL 544
Cdd:cd05926 336 GEIL--PPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD----GWFRTGDLGYLDADGYLFLTGRIKELIN-RGGEKISP 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 545 GKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNqkrltllaqqkgvEGTWVDicnnpamEAEILKEIREaanamKL 621
Cdd:cd05926 409 LEVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLR-------------EGASVT-------EEELRAFCRK-----HL 463
|
570 580 590
....*....|....*....|....*....|....*..
gi 4758332 622 ERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRN 657
Cdd:cd05926 464 AAFKVPKKVYFVDElPKTA-TG------KIQRRKVAE 493
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
77-576 |
2.87e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 139.71 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 77 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplvtlyatLGKEAVvhglnese 156
Cdd:PRK03640 21 IEFEEKKV-TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQ-----------LGAVAV-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 157 asylitsveLLESKLKTA----LLDISCVKHIIYVDnkainkaEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTPSDMA 232
Cdd:PRK03640 81 ---------LLNTRLSREellwQLDDAEVKCLITDD-------DFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 233 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLSDQ-- 310
Cdd:PRK03640 145 TIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNL-GLTEDDCWLAAVPIFHISGLSILMRSVIYGMRV------VLVEKfd 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 311 SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvMSKVQEMNYiqktlfkigydykleqikkgydaplcnlllfkkvkal 390
Cdd:PRK03640 218 AEKINKLLQTG----GVTIISVVSTMLQRL----LERLGEGTY------------------------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 391 lGGNVRMMLSGGAPLSPQT------HRFmnvcfccPIGQGYGLTESCgAGTVTEVTDYTT---GRVGAPLICCEIKL-KD 460
Cdd:PRK03640 253 -PSSFRCMLLGGGPAPKPLleqckeKGI-------PVYQSYGMTETA-SQIVTLSPEDALtklGSAGKPLFPCELKIeKD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 461 WQEGgytindKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 540
Cdd:PRK03640 324 GVVV------PPFEEGEIVVKGPNVTKGYLNREDATRE---TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGE 391
|
490 500 510
....*....|....*....|....*....|....*....
gi 4758332 541 YVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 576
Cdd:PRK03640 392 NIYPAEIEEVLLSHPGVAEAGVVGVPDDKWgqvPVAFVV 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
85-534 |
1.22e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 135.42 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGKEAVVHGLNE----SEASY- 159
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAA-------------LGALKAGAVVVPLNTrytaDEAAYi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 -------LITSVELLESKLKTALLDISCVKHIIYVdnkAINKAEyPEGFEIHSMQSVEELGSNPENlgiPPSRpTPSDMA 232
Cdd:PRK07656 98 largdakALFVLGLFLGVDYSATTRLPALEHVVIC---ETEEDD-PHTEKMKTFTDFLAAGDPAER---APEV-DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 233 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGcrigysspltlsdqs 311
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKAGVnAPLMRG--------------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 312 skikkgskgdCTVLkPTLMAAVPEIMDRIYK---NVMSKVQEMnyiqktlfkigYDYkleqikkgydaplcnLLLFKKVK 388
Cdd:PRK07656 234 ----------ATIL-PLPVFDPDEVFRLIETeriTVLPGPPTM-----------YNS---------------LLQHPDRS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 389 ALLGGNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD---YTTGRVGAPLICCEIKLKDWQEG 464
Cdd:PRK07656 277 AEDLSSLRLAVTGAASMPVAlLERFESELGVDIVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVNELGE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 465 GYTINDKpnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK07656 357 EVPVGEV----GELLVRGPNVMKGYYDDPEATAA--AIDADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
87-577 |
2.70e-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: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsvel 166
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 lesklktalldiscvkhiiyvdnkainkaeyPEGFEIHSMQsveelgsnpenlgippsrPTPSDMAIVMYTSGSTGRPKG 246
Cdd:cd05903 80 -------------------------------PERFRQFDPA------------------AMPDAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaeISCFTYGcrigysspltlsdqsskikkgskgdctVLK 326
Cdd:cd05903 111 VMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAH-------QTGFVYG---------------------------FTL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 327 PTLMAAvPEIMDRIYkNVMSKVQEMNYiQKTLFKIGYDYKLEQIKKGYD---APLCNLllfkkvkallggnvRMMLSGGA 403
Cdd:cd05903 156 PLLLGA-PVVLQDIW-DPDKALALMRE-HGVTFMMGATPFLTDLLNAVEeagEPLSRL--------------RTFVCGGA 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 404 PLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD-----YTTGRVGAPLiccEIKLKDwqEGGYTIndKPNPRGEI 478
Cdd:cd05903 219 TVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrlYTDGRPLPGV---EIKVVD--DTGATL--APGVEGEL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 479 VIGGQNISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLID 558
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAAP-----EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVI 365
|
490 500
....*....|....*....|..
gi 4758332 559 NICAFAKSDQ---SYVISFVVP 577
Cdd:cd05903 366 EAAVVALPDErlgERACAVVVT 387
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
85-551 |
2.70e-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: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEAsylitsv 164
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGA------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ellesklkTALLDiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpsDMAIVMYTSGSTGRP 244
Cdd:cd17631 94 --------KVLFD----------------------------------------------------DLALLMYTSGTTGRP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNL-----IAGMTGqceripGLGPKDTYIGYLPLAHVleltAEISCFTygcrigysSPLTLSDQSSKIKKGSK 319
Cdd:cd17631 114 KGAMLTHRNLlwnavNALAAL------DLGPDDVLLVVAPLFHI----GGLGVFT--------LPTLLRGGTVVILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 320 GDcTVL------KPTLMAAVPEIMDRIyknvmskvqemnyIQKTLFKigydykleqikkGYDAPlcnlllfkkvkallgg 393
Cdd:cd17631 176 PE-TVLdlierhRVTSFFLVPTMIQAL-------------LQHPRFA------------TTDLS---------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 394 NVRMMLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTT--GRVGAPLICCEIKLKDwqEGGYTIndK 471
Cdd:cd17631 214 SLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD--PDGREV--P 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 472 PNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 551
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 ... |
85-567 |
1.73e-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: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIA------AQTCFKYNFPLvtlyatLGKEAVVHGLNESEAS 158
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAmfgaalAGGVFVPINPL------LKAEQVAHILADCNVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 159 YLITSVELLEsKLKTALLDISCVKHIIYVDNKAiNKAEYPEGFEIHSMQSVEELGSnpenlGIPPSRPTPSDMAIVMYTS 238
Cdd:TIGR03098 100 LLVTSSERLD-LLHPALPGCHDLRTLIIVGDPA-HASEGHPGEEPASWPKLLALGD-----ADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 239 GSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGs 318
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATYLE-NRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDVLKALEKH- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 319 kgdctvlKPTLMAAVPEImdriyknvmskvqemnYIQktLFKIgyDYKLEqikkgyDAPLCNLLlfkkvkALLGGNV-RM 397
Cdd:TIGR03098 251 -------GITGLAAVPPL----------------WAQ--LAQL--DWPES------AAPSLRYL------TNSGGAMpRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 398 MLSGGAPLSPQTHRFMNvcfccpigqgYGLTESCGAGTV-TEVTDYTTGRVGAPLICCEIklkdwqeggYTINDK----- 471
Cdd:TIGR03098 292 TLSRLRSFLPNARLFLM----------YGLTEAFRSTYLpPEEVDRRPDSIGKAIPNAEV---------LVLREDgseca 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 472 PNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQR---------WfcTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYV 542
Cdd:TIGR03098 353 PGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGelhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIK-TSGYRV 429
|
490 500
....*....|....*....|....*
gi 4758332 543 SLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:TIGR03098 430 SPTEVEEVAYATGLVAEAVAFGVPD 454
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
229-580 |
1.96e-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: 121.30 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLS 308
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNL-GLTEDDNWLCALPLFHISGLSILMRSVIYGMTV------YLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 309 DQ--SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQIKKGYDAplcnlllfkk 386
Cdd:cd05912 150 DKfdAEQVLHLINSG----KVTIISVVPTMLQRL--------------------------LEILGEGYPN---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 387 vkallggNVRMMLSGGAPLSPQThrfMNVC--FCCPIGQGYGLTESCgAGTVTEVTDYT---TGRVGAPLICCEIKLKDw 461
Cdd:cd05912 190 -------NLRCILLGGGPAPKPL---LEQCkeKGIPVYQSYGMTETC-SQIVTLSPEDAlnkIGSAGKPLFPVELKIED- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 462 qeggytINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEY 541
Cdd:cd05912 258 ------DGQPPYEVGEILLKGPNVTKGYLNRPDATEE---SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGEN 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 4758332 542 VSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQK 580
Cdd:cd05912 326 IYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvPVAFVVSERP 367
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
142-569 |
1.68e-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: 119.74 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 142 TLGKEAVVHGLNESEASYLITSVELLEsKLK-TALLDISCVKHIIYVDN--KAINKAEYPEGFeIHSMQSVEELgsnpen 218
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQFIE-KLKlHHLFDVEYDARIVYLEDlrAKISKADKCKAF-LAGKFPPKWL------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 219 LGIPPSRPT-PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELT-AEISCFTYG 296
Cdd:cd05909 136 LRIFGVAPVqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 297 CRIG-YSSPLTLSDQSSKIKKGSkgdCTVL--KPTLMaavpeimdRIYknvmskvqeMNYIQKTLFKigydykleqikkg 373
Cdd:cd05909 215 IKVVfHPNPLDYKKIPELIYDKK---ATILlgTPTFL--------RGY---------ARAAHPEDFS------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 374 ydaplcnlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV-TEVTDYTTGRVGAPLI 452
Cdd:cd05909 262 --------------------SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 453 CCEIKLKDwQEGGytindKPNPRGE---IVIGGQNISMGYFKNEEKTAEDYsvdenGQRWFCTGDIGEFHPDGCLQIIDR 529
Cdd:cd05909 322 GMEVKIVS-VETH-----EEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF-----GDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 4758332 530 KKDLVKLqAGEYVSLGKVE-AALKNCPLIDNICAFAKSDQS 569
Cdd:cd05909 391 LSRFAKI-AGEMVSLEAIEdILSEILPEDNEVAVVSVPDGR 430
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
87-660 |
1.74e-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: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 166
Cdd:COG0365 42 YAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 LE--------SKLKTALLDISCVKHIIYVDNKAiNKAEYPEGFEIHsmqsvEELGSNPENLgipPSRPTPS-DMAIVMYT 237
Cdd:COG0365 122 LRggkvidlkEKVDEALEELPSLEHVIVVGRTG-ADVPMEGDLDWD-----ELLAAASAEF---EPEPTDAdDPLFILYT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 238 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY-----IG---------YLPLAHvleltaEISCFTYGCRIGYSS 303
Cdd:COG0365 193 SGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFwctadIGwatghsyivYGPLLN------GATVVLYEGRPDFPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 304 PLTLSDQSSKikkgskgdctvLKPTLMAAVPeimdRIYKNVMskvqemnyiqktlfKIGydyklEQIKKGYDapLCNLll 383
Cdd:COG0365 267 PGRLWELIEK-----------YGVTVFFTAP----TAIRALM--------------KAG-----DEPLKKYD--LSSL-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 fkkvkallggnvRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGA-GTVTEVTDYTTGRVGAPLICCEIKLkdW 461
Cdd:COG0365 309 ------------RLLGSAGEPLNPEVwEWWYEA-VGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAV--V 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 462 QEGGYTIndKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAG 539
Cdd:COG0365 374 DEDGNPV--PPGEEGELVIKGPWPGMfrGYWNDPERYRETYFGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINV-SG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 540 EYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNqkrltllaqqKGVEGTwvdicnnPAMEAEILKEIREaa 616
Cdd:COG0365 449 HRIGTAEIESALVSHPAVAEAAVVGVPDEirgQVVKAFVVLK----------PGVEPS-------DELAKELQAHVRE-- 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 4758332 617 namKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHYL 660
Cdd:COG0365 510 ---ELGPYAYPREIEFVDElPKTR-SG------KIMRRLLRKIAE 544
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
81-557 |
1.83e-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: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 81 NYKWMNYLEVNRRVnnfGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL 160
Cdd:cd17642 44 NYSYAEYLEMSVRL---AEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ITS------VELLESKLKTalldiscVKHIIYVDNKainkaeypegFEIHSMQSVEELGSNPENLG------IPPSRPTP 228
Cdd:cd17642 121 FCSkkglqkVLNVQKKLKI-------IKTIIILDSK----------EDYKGYQCLYTFITQNLPPGfneydfKPPSFDRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPG--LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGY----S 302
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykfE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 303 SPLTLSD-QSSKIKKgskgdcTVLKPTLMAAVPeimdriyknvmskvqemnyiqktlfkigydyKLEQIKKgYDapLCNL 381
Cdd:cd17642 264 EELFLRSlQDYKVQS------ALLVPTLFAFFA-------------------------------KSTLVDK-YD--LSNL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 382 LlfkkvkallggnvrMMLSGGAPLSPQTHRFMNVCFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 460
Cdd:cd17642 304 H--------------EIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 461 wQEGGYTINdkPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGE 540
Cdd:cd17642 370 -LDTGKTLG--PNERGELCVKGPMIMKGYVNNPEATKA--LIDKDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GY 441
|
490
....*....|....*..
gi 4758332 541 YVSLGKVEAALKNCPLI 557
Cdd:cd17642 442 QVPPAELESILLQHPKI 458
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
220-559 |
3.70e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 116.64 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 220 GIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA-GMTGQCeRIPGLGPKD-TYIGYLPLAHVLELTAeisCFTYGC 297
Cdd:PRK05605 210 DVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKA-WVPGLGDGPeRVLAALPMFHAYGLTL---CLTLAV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 298 RIG--------YSSPLTLsdqsSKIKKGskgdctvlKPTLMAAVPEimdrIYKNVMSKVQEmnyiqktlfkigydykleq 369
Cdd:PRK05605 286 SIGgelvllpaPDIDLIL----DAMKKH--------PPTWLPGVPP----LYEKIAEAAEE------------------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 370 ikKGYDaplcnlllfkkvkalLGGnVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY-TTGRVG 448
Cdd:PRK05605 331 --RGVD---------------LSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDrRPGYVG 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 449 APLICCEIKLKDWQEGGYTINDkpNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIID 528
Cdd:PRK05605 393 VPFPDTEVRIVDPEDPDETMPD--GEEGELLVRGPQVFKGYWNRPEETAK---SFLDG--WFRTGDVVVMEEDGFIRIVD 465
|
330 340 350
....*....|....*....|....*....|.
gi 4758332 529 RKKDLVkLQAGEYVSLGKVEAALKNCPLIDN 559
Cdd:PRK05605 466 RIKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
87-562 |
1.03e-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: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGL-TALGLKPKNTIAIFCEtRAEWMIAAQ-TCFK----YnFPLVTLYATLGKEAVvhgLNESEASYL 160
Cdd:TIGR01733 2 YRELDERANRLARHLrAAGGVGPGDRVAVLLE-RSAELVVAIlAVLKagaaY-VPLDPAYPAERLAFI---LEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ITSVELLESKLKTALLDISCVkhiiyvdnkainkaeypegfeihsmqSVEELGSNPENLGIPP-SRPTPSDMAIVMYTSG 239
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLD--------------------------PLELAALDDAPAPPPPdAPSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 240 STGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAH---VLELTAeiscftygcrigyssPLTLsdqsskikk 316
Cdd:TIGR01733 131 STGRPKGVVVTHRSLVN-LLAWLARRYGLDPDDRVLQFASLSFdasVEEIFG---------------ALLA--------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 317 gskGDCTVLKPtlmaAVPEIMDRIYKNVMSKVQEMNYIQKTlfkigydykleqikkgydAPLCNLLLFKKVKALLGgnVR 396
Cdd:TIGR01733 186 ---GATLVVPP----EDEERDDAALLAALIAEHPVTVLNLT------------------PSLLALLAAALPPALAS--LR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 397 MMLSGGAPLSPQTH-RFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIklkdwqeggYTIND 470
Cdd:TIGR01733 239 LVILGGEALTPALVdRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRL---------YVLDD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 471 --KPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEY 541
Cdd:TIGR01733 310 dlRPVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYR 388
|
490 500
....*....|....*....|.
gi 4758332 542 VSLGKVEAALKNCPLIDNICA 562
Cdd:TIGR01733 389 IELGEIEAALLRHPGVREAVV 409
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
230-568 |
1.36e-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: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIgysspl 305
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRF-GLGEDDVYLTVLPLFHinaqAVSVLAALSV---GATL------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 306 tlsdqsskikkgskgdctVLKPTLMAAvpeimdriykNVMSKVQE-----MNYIQKTLfkigyDYKLEQIKKGYDAplcn 380
Cdd:cd05934 152 ------------------VLLPRFSAS----------RFWSDVRRygatvTNYLGAML-----SYLLAQPPSPDDR---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 381 lllfkkvkallGGNVRmmLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 460
Cdd:cd05934 195 -----------AHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 461 wqeggytINDKPNPR---GEIVI---GGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:cd05934 262 -------DDGQELPAgepGELVIrglRGWGFFKGYYNMPEATAE---AMRNG--WFHTGDLGYRDADGFFYFVDRKKDMI 329
|
330 340 350
....*....|....*....|....*....|....
gi 4758332 535 KlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:cd05934 330 R-RRGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
87-588 |
1.55e-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: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCEtRAEWMIAAqtcfkynfplvtLYATL--G-----------KEAVVHGLN 153
Cdd:COG1020 504 YAELNARANRLAHHLRALGVGPGDLVGVCLE-RSLEMVVA------------LLAVLkaGaayvpldpaypAERLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 154 ESEASYLITsvellESKLKTALLDISCvkHIIYVDNKAInkAEYPEGFeihsmqsveelgsnpenlgiPPSRPTPSDMAI 233
Cdd:COG1020 571 DAGARLVLT-----QSALAARLPELGV--PVLALDALAL--AAEPATN--------------------PPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 234 VMYTSGSTGRPKGVMMHH---SNLIAGMTGQCeripGLGPKDTYIGYLPLAH---VLELtaeISCFTYGCRIGYSSPLTL 307
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHralVNLLAWMQRRY----GLGPGDRVLQFASLSFdasVWEI---FGALLSGATLVLAPPEAR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 308 SD--------QSSKIkkgskgdcTVLK--PTLMAAVPeimdriyknvmskvqemnyiqktlfkigydykleqikkgyDAP 377
Cdd:COG1020 695 RDpaalaellARHRV--------TVLNltPSLLRALL----------------------------------------DAA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 378 LCNLLlfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPL- 451
Cdd:COG1020 727 PEALP-----------SLRLVLVGGEALPPELvRRWRARLPGARLVNLYGPTETTVDSTYYEVTppDADGGSVpiGRPIa 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 452 -ICCEIkLKDWQEggytindkPNP---RGEIVIGGQNISMGYFKNEEKTAE---DYSVDENGQRWFCTGDIGEFHPDGCL 524
Cdd:COG1020 796 nTRVYV-LDAHLQ--------PVPvgvPGELYIGGAGLARGYLNRPELTAErfvADPFGFPGARLYRTGDLARWLPDGNL 866
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758332 525 QIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKRLTLLAQQ 588
Cdd:COG1020 867 EFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAREDAPgdkRLVAYVVPEAGAAAAAALL 932
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
230-635 |
3.07e-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: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIP---GLGPKDTYIGYLPLAHVLELTAEISCFTYgCRigySSPLT 306
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAA----NVRALVdawRWTEDDVLLHVLPLHHVHGLVNALLCPLF-AG---ASVEF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LSDQSSKIKKGSKGDCTVlkpTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKigydykleqikkgydaplcnlllfkk 386
Cdd:cd05941 162 LPKFDPKEVAISRLMPSI---TVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAE-------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 387 vkallggNVRMMLSGGAPLSPQTHRFmnvcFCCPIGQG----YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQ 462
Cdd:cd05941 213 -------RLRLMVSGSAALPVPTLEE----WEAITGHTllerYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVD-E 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 463 EGGytindKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 539
Cdd:cd05941 281 ETG-----EPLPRgevGEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGVVDEDGYYWILGRSSVDIIKSGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 540 EYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqQKGVegtwvdicnnPAMEAEILKEireaA 616
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVL----------RAGA----------AALSLEELKE----W 407
|
410
....*....|....*....
gi 4758332 617 NAMKLERFEIPIKVRLSPE 635
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDE 426
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
86-555 |
3.44e-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: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 86 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCetraeWmiaaqTCFKYnfpLVTLYATLGKEAVVHGLN------------ 153
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLA-----W-----NTHRH---LELYYAVPGMGAVLHTINprlfpeqiayii 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 154 -ESEASYLITSVELLesKLKTALLD-ISCVKHIIYVDNKAINKAEYPEG---FE--IHSMQSVEELGSNPENlgippsrp 226
Cdd:cd12119 94 nHAEDRVVFVDRDFL--PLLEAIAPrLPTVEHVVVMTDDAAMPEPAGVGvlaYEelLAAESPEYDWPDFDEN-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 tpsDMAIVMYTSGSTGRPKGVMM-HHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPL 305
Cdd:cd12119 164 ---TAAAICYTSGTTGNPKGVVYsHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 306 TLSDQSSKIKKGSKgdctvlkPTLMAAVPEImdriYKNVMSKVQemnyiqktlfkigydykleqiKKGYDaplcnllLFK 385
Cdd:cd12119 241 LDPASLAELIEREG-------VTFAAGVPTV----WQGLLDHLE---------------------ANGRD-------LSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 386 kvkallggnVRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTESCGAGTVTEVTDY--------------TTGRVg 448
Cdd:cd12119 282 ---------LRRVVIGGSAVPRsliEAFEERGV----RVIHAWGMTETSPLGTVARPPSEhsnlsedeqlalraKQGRP- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 449 APLIccEIKLKDwqEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIID 528
Cdd:cd12119 348 VPGV--ELRIVD--DDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEA---LTEDG--WLRTGDVATIDEDGYLTITD 418
|
490 500
....*....|....*....|....*..
gi 4758332 529 RKKDLVKlQAGEYVSLGKVEAALKNCP 555
Cdd:cd12119 419 RSKDVIK-SGGEWISSVELENAIMAHP 444
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
227-588 |
3.52e-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: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPkdtyigylplahvleltaeiscftyGCRIGYSSPLT 306
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGP-------------------------GDVFLNQAPFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LsdqsskikkgskgDCTV--LKPTLMA-----AVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykleQIKKGYDAP-- 377
Cdd:cd05945 149 F-------------DLSVmdLYPALASgatlvPVPRDATADPKQLFRFLAEH-----------------GITVWVSTPsf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 378 --LCnlLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVT-----DYTTGRVGA 449
Cdd:cd05945 199 aaMC--LLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTpevldGYDRLPIGY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 450 PLICCEIKLKDwqEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDEnGQRWFCTGDIGEFHPDGCLQIIDR 529
Cdd:cd05945 277 AKPGAKLVILD--EDGRPV--PPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-GQRAYRTGDLVRLEADGLLFYRGR 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 530 KKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP----NQKRLTLLAQQ 588
Cdd:cd05945 352 LDFQVKLN-GYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVtelIAFVVPkpgaEAGLTKAIKAE 416
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
87-578 |
2.31e-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: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsvel 166
Cdd:cd17655 25 YRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 lESKLKTALLDIscvKHIIYVDNKAInkAEYPEgfeihsmqsveelgsnpENLGiPPSRPtpSDMAIVMYTSGSTGRPKG 246
Cdd:cd17655 101 -QSHLQPPIAFI---GLIDLLDEDTI--YHEES-----------------ENLE-PVSKS--DDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTLSDQSSKIKKGSKGDCTVLk 326
Cdd:cd17655 155 VMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIS--FDASVT-EIFA---------SLLSGNTLYIVRKETVLDGQAL- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 327 ptlmaavpeimdriyknvmskvqeMNYIQKtlfkigydYKLEQIkkgyDAPLCNLLLFKKVKALLGGNVRMMLSGGAPLS 406
Cdd:cd17655 221 ------------------------TQYIRQ--------NRITII----DLTPAHLKLLDAADDSEGLSLKHLIVGGEALS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 407 PQT-----HRFMNvcfCCPIGQGYGLTESC-GAGT-VTEVTDYTTGRV--GAPLICCEIKLKDwQEGgytindKPNP--- 474
Cdd:cd17655 265 TELakkiiELFGT---NPTITNAYGPTETTvDASIyQYEPETDQQVSVpiGKPLGNTRIYILD-QYG------RPQPvgv 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 475 RGEIVIGGQNISMGYFKNEEKTAEDYSVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALK 552
Cdd:cd17655 335 AGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR-GYRIELGEIEARLL 413
|
490 500
....*....|....*....|....*....
gi 4758332 553 NCPLIDNICAFAKSDQS---YVISFVVPN 578
Cdd:cd17655 414 QHPDIKEAVVIARKDEQgqnYLCAYIVSE 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
227-579 |
8.94e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 107.61 E-value: 8.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI------G 300
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLvvlpeeV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 301 YSSPLTLSD--QSSKIkkgskgdcTVLK--PTLMAAVpeimdriyknvmskvqeMNYIQKTLFKigydykleqikkgyda 376
Cdd:cd05930 170 RKDPEALADllAEEGI--------TVLHltPSLLRLL-----------------LQELELAALP---------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 377 plcnlllfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPL 451
Cdd:cd05930 209 -----------------SLRLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATYYRVPpdDEEDGRVpiGRPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 452 ICCEIKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQI 526
Cdd:cd05930 272 PNTRVYVLD-------ENLRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPNpfGPGERMYRTGDLVRWLPDGNLEF 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 527 IDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 579
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 ... |
85-568 |
2.85e-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: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELlesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpSDMAIVMYTSGSTGRP 244
Cdd:cd05935 82 EL--------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCriGYSSPLTLSDQSSKIKKGSKGDCTV 324
Cdd:cd05935 100 KGCMHTHFSAAANALQSA-VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG--GTYVLMARWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LkptlMAAVPEIMDriyknVMSKVQEMNYIQKTLfkigydykleqikkgydaplcnlllfkkvkallggnvRMMLSGGAP 404
Cdd:cd05935 177 W----TNIPTMLVD-----LLATPEFKTRDLSSL-------------------------------------KVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 405 LSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGgytINDKPNPRGEIVIGGQN 484
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETG---RELPPNEVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 485 ISMGYFKNEEKTAEDYSVDeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFA 564
Cdd:cd05935 288 IFKGYWNRPEETEESFIEI-KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
....
gi 4758332 565 KSDQ 568
Cdd:cd05935 366 VPDE 369
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
223-534 |
5.79e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.39 E-value: 5.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 223 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPG--LGP-KDTYIGYLPLAHvleltaeISCFTYGCRI 299
Cdd:PRK05677 201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANML-QCRALMGsnLNEgCEILIAPLPLYH-------IYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 300 gysspLTLSdqsskikkgskGDCTVLKPTlmaavPEIMDRIYKnVMSKVQEMNYIQ-KTLFkigydykleqikkgydAPL 378
Cdd:PRK05677 273 -----MMLI-----------GNHNILISN-----PRDLPAMVK-ELGKWKFSGFVGlNTLF----------------VAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 379 CNLLLFKKV--KALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEI 456
Cdd:PRK05677 315 CNNEAFRKLdfSAL-----KLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLC 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758332 457 KLKDwQEGgytiNDKP-NPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
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) ... |
230-659 |
1.16e-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: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysSPLTLSD 309
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVGGLAILVRSLLAG------AELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 310 QSSKIKKgskgDCTVLKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEqikkgYDAPLCNLLLFKKVka 389
Cdd:cd17630 74 RNQALAE----DLAPPGVTHVSLVPTQLQRL--------------------------LD-----SGQGPAALKSLRAV-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 390 llggnvrmmLSGGAPLSPQ-THRFMnvCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggyti 468
Cdd:cd17630 117 ---------LLGGAPIPPElLERAA--DRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 469 ndkpnpRGEIVIGGQNISMGYFKNEEKTAedysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVE 548
Cdd:cd17630 178 ------DGEIWVGGASLAMGYLRGQLVPE----FNEDG--WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 549 AALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqqkgvegtwvdicNNPAMEAEILKEIREaanamKLERFE 625
Cdd:cd17630 245 AALAAHPAVRDAFVVGVPDEELgqrPVAVIVG----------------------RGPADPAELRAWLKD-----KLARFK 297
|
410 420 430
....*....|....*....|....*....|....
gi 4758332 626 IPIkvRLSPEPWTPETGLVtdafKLKRKELRNHY 659
Cdd:cd17630 298 LPK--RIYPVPELPRTGGG----KVDRRALRAWL 325
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
87-584 |
8.93e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 102.52 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVel 166
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPT-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 LESKLKTALLDISCV------KHIIYVDNKAinkaeyPEgfeiHSMQSVEELGSNPENLGIPPsrPTPSD-MAIVMYTSG 239
Cdd:PRK06087 130 LFKQTRPVDLILPLQnqlpqlQQIVGVDKLA------PA----TSSLSLSQIIADYEPLTTAI--TTHGDeLAAVLFTSG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 240 STGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRigySSPLTLSDQSSKIKKGS 318
Cdd:PRK06087 198 TEGLPKGVMLTHNNILASERAYCARL-NLTWQDVFMMPAPLGHATGfLHGVTAPFLIGAR---SVLLDIFTPDACLALLE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 319 KGDCTvlkpTLMAAVPEIMDriyknvmskvqemnyIQKTLFKIGYDykleqikkgydaplcnlllfkkVKALlggnvRMM 398
Cdd:PRK06087 274 QQRCT----CMLGATPFIYD---------------LLNLLEKQPAD----------------------LSAL-----RFF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 399 LSGGAP----LSPQTHRFmNVCFCcpigQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDWqeggytiNDKP 472
Cdd:PRK06087 308 LCGGTTipkkVARECQQR-GIKLL----SVYGSTESSPHAVVNldDPLSRFMHTDGYAAAGVEIKVVDE-------ARKT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 473 NPRG---EIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEA 549
Cdd:PRK06087 376 LPPGcegEEASRGPNVFMGYLDEPELTAR--ALDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVED 450
|
490 500 510
....*....|....*....|....*....|....*...
gi 4758332 550 ALKNCPLIDNICAFAKSDQSY---VISFVVPNQKRLTL 584
Cdd:PRK06087 451 ILLQHPKIHDACVVAMPDERLgerSCAYVVLKAPHHSL 488
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
85-579 |
1.54e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.05 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK----YNfPLVTLYAtlgKEAVVHGLNESEASYL 160
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRigavLN-PLMPIFR---ERELSFMLKHAESKVL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 IT-------SVELLESKLKTALLDIscvKHIIYVDnkainkAEYPEGFEIHSMQSVEELGSNPENLgIPPSRPTPSDMAI 233
Cdd:PRK13295 132 VVpktfrgfDHAAMARRLRPELPAL---RHVVVVG------GDGADSFEALLITPAWEQEPDAPAI-LARLRPGPDDVTQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 234 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleLTAeiscFTYGCRIgyssPLTLsdqssk 313
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASPMAH---QTG----FMYGLMM----PVML------ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 314 ikkgskGDCTVLK----PTL-------------MAAVPEIMDriyknvMSKVQEMNyiqktlfkigydykleqikkGYDA 376
Cdd:PRK13295 264 ------GATAVLQdiwdPARaaelirtegvtftMASTPFLTD------LTRAVKES--------------------GRPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 377 PlcnlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEsCGAGTVT------EVTDYTTGRvgaP 450
Cdd:PRK13295 312 S----------------SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE-NGAVTLTklddpdERASTTDGC---P 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 451 LICCEIKLKDwqeggytINDKPNPRGEI---VIGGQNISMGYFKNEEKTAEDysvdenGQRWFCTGDIGEFHPDGCLQII 527
Cdd:PRK13295 372 LPGVEVRVVD-------ADGAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGTD------ADGWFDTGDLARIDADGYIRIS 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 4758332 528 DRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 579
Cdd:PRK13295 439 GRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDerlGERACAFVVPRP 492
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
85-570 |
2.42e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 101.39 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS- 163
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 164 -----------VELLESKLKTALLDISC-----VKHIIYVDnkainkAEYPEGFEI-HSMQSVEElGSNPENLGIPPSRP 226
Cdd:PRK12583 126 afktsdyhamlQELLPGLAEGQPGALACerlpeLRGVVSLA------PAPPPGFLAwHELQARGE-TVSREALAERQASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYss 303
Cdd:PRK12583 199 DRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVA--ESL-GLTEHDRLCVPVPLYHCFGMVlANLGCMTVGACLVY-- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 304 PLTLSDQSSKIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIQKTLFKIGydykleqikkgydaplcnl 381
Cdd:PRK12583 274 PNEAFDPLATLQAVEEERCTALYgvPTMFIA-----------------ELDHPQRGNFDLS------------------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 382 llfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD------YTTGRVGAPLicc 454
Cdd:PRK12583 318 ------------SLRTGIMAGAPCPIEVmRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADdlerrvETVGRTQPHL--- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 455 EIKLKDwqEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK12583 383 EVKVVD--PDGATV--PRGEIGELCTRGYSVMKGYWNNPEATAE--SIDEDG--WMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510
....*....|....*....|....*....|....*.
gi 4758332 535 kLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY 570
Cdd:PRK12583 455 -IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
230-567 |
1.35e-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: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLI-AGMtgQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCR---IGYSSPL 305
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 306 TLSD--QSSKIkkgskgdctvlkpTLMAAVPEIMDRIyknvmskvqeMNYIQKTlfkiGYDYKLEQIKKGYDAPlcnlll 383
Cdd:cd17637 79 EALEliEEEKV-------------TLMGSFPPILSNL----------LDAAEKS----GVDLSSLRHVLGLDAP------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 fKKVKALlggnvrmmlsggaplspqtHRFMNVCFCCpigqGYGLTESCGAGTVTEVTDyTTGRVGAPLICCEIKLKDwqe 463
Cdd:cd17637 126 -ETIQRF-------------------EETTGATFWS----LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVD--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 464 ggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRK--KDLVKlQA 538
Cdd:cd17637 178 ----DNDRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTF---RNG--WHHTGDLGRFDEDGYLWYAGRKpeKELIK-PG 247
|
330 340
....*....|....*....|....*....
gi 4758332 539 GEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:cd17637 248 GENVYPAEVEKVILEHPAIAEVCVIGVPD 276
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
222-577 |
1.76e-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: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHH---SNLIAGMTgqcERIpGLGPKDTYIGYLPLAH---VLELTAEIScfty 295
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISHraaLNTILDIN---RRF-AVGPDDRVLALSSLSFdlsVYDIFGALS---- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 296 gcrIGYSspLTLSDQsskikkGSKGDCTVLKP-------TLMAAVPEIMDRIyknvmskvqeMNYiqktlfkigydykLE 368
Cdd:cd12114 191 ---AGAT--LVLPDE------ARRRDPAHWAElierhgvTLWNSVPALLEML----------LDV-------------LE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 369 QIkkgyDAPLCNLllfkkvkallggnvRM-MLSG---GAPLSPQTHRFmnVCFCCPIGQGyGLTESCGAGTVTEVTDYTT 444
Cdd:cd12114 237 AA----QALLPSL--------------RLvLLSGdwiPLDLPARLRAL--APDARLISLG-GATEASIWSIYHPIDEVPP 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 445 GRV----GAPLI--CCEIkLKDWQeggytiNDKPN-PRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGE 517
Cdd:cd12114 296 DWRsipyGRPLAnqRYRV-LDPRG------RDCPDwVPGELWIGGRGVALGYLGDPELTAARFVTHPDGERLYRTGDLGR 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758332 518 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD--QSYVISFVVP 577
Cdd:cd12114 369 YRPDGTLEFLGRRDGQVKVR-GYRIELGEIEAALQAHPGVARAVVVVLGDpgGKRLAAFVVP 429
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
219-584 |
2.39e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 98.36 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 219 LGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP---------KDTYIGYLPLAHVLELTAE 289
Cdd:PRK12492 197 LSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplmkegQEVMIAPLPLYHIYAFTAN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 290 ISCFTYgcrigysspltlsdqsskikkgsKGDCTVLKpTLMAAVPEIMDRIYKNVMSKVQEMNyiqkTLFkigydykleq 369
Cdd:PRK12492 277 CMCMMV-----------------------SGNHNVLI-TNPRDIPGFIKELGKWRFSALLGLN----TLF---------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 370 ikkgydAPLCNLLLFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVTDYTT----G 445
Cdd:PRK12492 319 ------VALMDHPGFKDLDF---SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTET---SPVASTNPYGElarlG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 446 RVGAPLICCEIKLKDwQEGgytiNDKP-NPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCL 524
Cdd:PRK12492 387 TVGIPVPGTALKVID-DDG----NELPlGERGELCIKGPQVMKGYWQQPEATAE--ALDAEG--WFKTGDIAVIDPDGFV 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758332 525 QIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKRLTL 584
Cdd:PRK12492 458 RIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDErsgEAVKLFVVARDPGLSV 519
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
84-568 |
2.81e-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: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 84 WMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 163
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 164 VELLESklktalldiscvkhiiyvdnkainkaeYPEGFEIhsmqsVEELGSNPENLGIPPSRPT-PSDMAIVMYTSGSTG 242
Cdd:cd12116 92 DALPDR---------------------------LPAGLPV-----LLLALAAAAAAPAAPRTPVsPDDLAYVIYTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 243 RPKGVMMHHSNLIAGMTGQCERiPGLGPKDTYIGYLPLA---HVLELTAEISCftyGCRIGYSSPLTLSDqsskikkgsk 319
Cdd:cd12116 140 RPKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAVTTYAfdiSLLELLLPLLA---GARVVIAPRETQRD---------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 320 gdctvlkPTLMAAvpeIMDRIYKNVMskvqemnyiQKTlfkigydykleqikkgydaPLCNLLLFkkvKALLGGNVRM-M 398
Cdd:cd12116 206 -------PEALAR---LIEAHSITVM---------QAT-------------------PATWRMLL---DAGWQGRAGLtA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 399 LSGGAPLSPQTHRFmnvcFCCPIGQG---YGLTESCGAGTVTEVTDYTTG-RVGAPLICCEIKLKDwqEGGytindKPNP 474
Cdd:cd12116 245 LCGGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAAAGPiPIGRPLANTQVYVLD--AAL-----RPVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 475 R---GEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 548
Cdd:cd12116 314 PgvpGELYIGGDGVAQGYLGRPALTAERFVPDpfaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIR-GHRIELGEIE 392
|
490 500
....*....|....*....|
gi 4758332 549 AALKNCPLIDNICAFAKSDQ 568
Cdd:cd12116 393 AALAAHPGVAQAAVVVREDG 412
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
78-577 |
3.08e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 97.62 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 78 ILGNYKWMNYLEVNRRVNNFGSGLT-ALGLKPKNTIAIFcetraewmiaAQTCFKYnfpLVTLYATLGKEAVVHGLN--- 153
Cdd:PRK06839 21 IITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAIL----------SQNSLEY---IVLLFAIAKVECIAVPLNirl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 154 -ESEASYLI----TSVELLESKLKTALLDI---SCVKHIIYVdnkainkaEYPEGFEIHSMQSVEElgsnpenlgippsr 225
Cdd:PRK06839 88 tENELIFQLkdsgTTVLFVEKTFQNMALSMqkvSYVQRVISI--------TSLKEIEDRKIDNFVE-------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 226 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltAEISCFTY-----GCRIG 300
Cdd:PRK06839 146 KNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHI----GGIGLFAFptlfaGGVII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 301 YSSPLTLSDQSSKIKKGskgdctvlKPTLMAAVPEIMDRIyknvmskvqemnyIQKTLFkigydykleqIKKGYDaplcn 380
Cdd:PRK06839 221 VPRKFEPTKALSMIEKH--------KVTVVMGVPTIHQAL-------------INCSKF----------ETTNLQ----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 381 lllfkkvkallggNVRMMLSGGAPLS-PQTHRFMNVCFccPIGQGYGLTEScgAGTV----TEVTDYTTGRVGAPLICCE 455
Cdd:PRK06839 265 -------------SVRWFYNGGAPCPeELMREFIDRGF--LFGQGFGMTET--SPTVfmlsEEDARRKVGSIGKPVLFCD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 456 IKLKDWQEGgytiNDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 535
Cdd:PRK06839 328 YELIDENKN----KVEVGEVGELLIRGPNVMKEYWNRPDATEETI---QDG--WLCTGDLARVDEDGFVYIVGRKKEMI- 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 4758332 536 LQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 577
Cdd:PRK06839 398 ISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeiPIAFIVK 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-655 |
3.17e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.65 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLEsKLKTAlLDISCVkhiiyvdnkAINKAEYPEGFEIHSmqsveelgsnpenlgiPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 4657 HLLQ-RLPIP-DGLASL---------ALDRDEDWEGFPAHD----------------PAVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERiPGLGPKDTYIGYLPLAhvLELTAEiscftygcriGYSSPLTlsdqsskikkgsKGDCTV 324
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFS--FDGSHE----------GLYHPLI------------NGASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LKPTLMAAVPEIMDRIYKNVMSKVQemnyiqktlFKIGYDYKLEQikkgYDAPLCNLLLFKKV----KALLGGNVRMMLS 400
Cdd:PRK12316 4765 IRDDSLWDPERLYAEIHEHRVTVLV---------FPPVYLQQLAE----HAERDGEPPSLRVYcfggEAVAQASYDLAWR 4831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 401 GGAPLSpqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPlicceIKLKDWQEGGYTINDKPNPR---- 475
Cdd:PRK12316 4832 ALKPVY--------------LFNGYGPTETTVTVLLWKARDGDAcGAAYMP-----IGTPLGNRSGYVLDGQLNPLpvgv 4892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 476 -GEIVIGGQNISMGYFKNEEKTAEDY---SVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAAL 551
Cdd:PRK12316 4893 aGELYLGGEGVARGYLERPALTAERFvpdPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIR-GFRIELGEIEARL 4971
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 552 KNCPLIDNICAFAK--SDQSYVISFVVPNQKRLTllaqqkgvegtwvdicNNPAMEAEILKEIREAANAmKLERFEIPIK 629
Cdd:PRK12316 4972 REHPAVREAVVIAQegAVGKQLVGYVVPQDPALA----------------DADEAQAELRDELKAALRE-RLPEYMVPAH 5034
|
570 580
....*....|....*....|....*..
gi 4758332 630 -VRLSPEPWTPETglvtdafKLKRKEL 655
Cdd:PRK12316 5035 lVFLARMPLTPNG-------KLDRKAL 5054
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
222-657 |
3.21e-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: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 222 PPSRPTPSDMAIVM-YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltAEISC 292
Cdd:cd12118 125 EWIPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylnalANILEW---------EMKQHPVYLWTLPMFH-----CNGWC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 293 FTYGcrigysspltlsdqsskikkgskgdctvlkptlMAAV------------PEIMDRIYKNvmsKVQEMNyiqktlfk 360
Cdd:cd12118 191 FPWT---------------------------------VAAVggtnvclrkvdaKAIYDLIEKH---KVTHFC-------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 361 igydykleqikkgyDAPLCNLLLF---KKVKALLGGNVRMMlSGGAPLSPQTHRFMNvcfccPIG----QGYGLTESCGA 433
Cdd:cd12118 227 --------------GAPTVLNMLAnapPSDARPLPHRVHVM-TAGAPPPAAVLAKME-----ELGfdvtHVYGLTETYGP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 434 GTV-----------TEVTDYTTGRVGAPLICCE-IKLKDWQEGgytindKPNPR-----GEIVIGGQNISMGYFKNEEKT 496
Cdd:cd12118 287 ATVcawkpewdelpTEERARLKARQGVRYVGLEeVDVLDPETM------KPVPRdgktiGEIVFRGNIVMKGYLKNPEAT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 497 AEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS--- 573
Cdd:cd12118 361 AEAF---RGG--WFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVpca 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 574 FVvpnqkrlTLlaqQKGVEGTwvdicnnpamEAEILKEIREaanamKLERFEIPIKVRLSPEPWTPeTGlvtdafKLKRK 653
Cdd:cd12118 435 FV-------EL---KEGAKVT----------EEEIIAFCRE-----HLAGFMVPKTVVFGELPKTS-TG------KIQKF 482
|
....
gi 4758332 654 ELRN 657
Cdd:cd12118 483 VLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-657 |
6.46e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 96.94 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 86 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkYNFP-----LVTLYATLGKEAVVHGLNESEASYL 160
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA-MVEAH----FGVPmagavLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ITSVELleSKLKTALLDISCVKHIIYVDnkaINKAEYPEGFEIHSMqSVEEL--GSNPEnlgIPPSRPTPSDMAIVM-YT 237
Cdd:PRK08162 120 IVDTEF--AEVAREALALLPGPKPLVID---VDDPEYPGGRFIGAL-DYEAFlaSGDPD---FAWTLPADEWDAIALnYT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 238 SGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltaeiscftygCRiGYSSPLTLsd 309
Cdd:PRK08162 191 SGTTGNPKGVVYHHrgaylnalSNILAW---------GMPKHPVYLWTLPMFH--------------CN-GWCFPWTV-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 310 qsskikkgskgdctvlkpTLMAAVpeimdriykNV-MSKVQEmnyiqKTLFKIGYDyklEQIKKGYDAP-----LCNLLl 383
Cdd:PRK08162 245 ------------------AARAGT---------NVcLRKVDP-----KLIFDLIRE---HGVTHYCGAPivlsaLINAP- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 fKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCcpIGQGYGLTESCGAGTV----TEVTDYTTGRvgapliccEIKLK 459
Cdd:PRK08162 289 -AEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD--LTHVYGLTETYGPATVcawqPEWDALPLDE--------RAQLK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 460 DWQ------EGGYTIND----KPNPR-----GEIVIGGqNISM-GYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGC 523
Cdd:PRK08162 358 ARQgvryplQEGVTVLDpdtmQPVPAdgetiGEIMFRG-NIVMkGYLKNPKATEEAF---AGG--WFHTGDLAVLHPDGY 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 524 LQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVvpnqkrlTLlaqQKGVEGTwvdicn 600
Cdd:PRK08162 432 IKIKDRSKDII-ISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWgevPCAFV-------EL---KDGASAT------ 494
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 4758332 601 npamEAEILKEIREaanamKLERFEIPIKVRLSPEPWTpETGlvtdafKLKRKELRN 657
Cdd:PRK08162 495 ----EEEIIAHCRE-----HLAGFKVPKAVVFGELPKT-STG------KIQKFVLRE 535
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
137-551 |
8.97e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 97.69 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 137 VTLYATLGKEAVVHGLNESEASYLITSVELLES-KLKTALLDISCVKHIIYVDN--KAINKAEypegfEIHSMQSVEELg 213
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKFLEKlKNKGFDLELPENVKVIYLEDlkAKISKVD-----KLTALLAARLL- 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 214 snP----ENLGIPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTAE 289
Cdd:PRK08633 767 --ParllKRLYGPT--FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSLPFFHSFGLTVT 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 290 --------ISCftygcrIGYSSPLtlsdQSSKIKKgskgdcTVLK--PTLMAAVPEIMdRIYknvmskvqemnyiqktlf 359
Cdd:PRK08633 842 lwlpllegIKV------VYHPDPT----DALGIAK------LVAKhrATILLGTPTFL-RLY------------------ 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 360 kigydykleqikkgydaplcnlLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV--- 436
Cdd:PRK08633 887 ----------------------LRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVnlp 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 437 -TEVTDYTT------GRVGAPLICCEIKLKDwQEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEdYSVDENGQRW 509
Cdd:PRK08633 945 dVLAADFKRqtgskeGSVGMPLPGVAVRIVD-PETFEEL--PPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKDIDGIGW 1020
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 4758332 510 FCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAAL 551
Cdd:PRK08633 1021 YVTGDKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
87-579 |
1.04e-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: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 166
Cdd:cd05959 32 YAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 LEsKLKTAL-LDISCVKHIIYVDnkainkaeyPEGFEIHSMQSVEELGSNPENLgiPPSRPTPSDMAIVMYTSGSTGRPK 245
Cdd:cd05959 112 AP-VLAAALtKSEHTLVVLIVSG---------GAGPEAGALLLAELVAAEAEQL--KPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 246 GVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsdqsskikkgSKGDCTVL 325
Cdd:cd05959 180 GVVHLHADIYWTAELYARNVLGIREDDVC-----------FSAAKLFFAYGLGNSLTFPL------------SVGATTVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 326 KPTLMAAvpeimDRIYKnvmskvqEMNYIQKTLFkigydykleqikkgYDAP--LCNLLLFKKVKALLGGNVRMMLSGGA 403
Cdd:cd05959 237 MPERPTP-----AAVFK-------RIRRYRPTVF--------------FGVPtlYAAMLAAPNLPSRDLSSLRLCVSAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 404 PLSPQTHRFMNVCFCCPIGQGYGLTE------SCGAGTVtevtdyTTGRVGAPLICCEIKLKDwQEGGYTINDKPnprGE 477
Cdd:cd05959 291 ALPAEVGERWKARFGLDILDGIGSTEmlhiflSNRPGRV------RYGTTGKPVPGYEVELRD-EDGGDVADGEP---GE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 478 IVIGGQNISMGYFKNEEKTAEDYSvdenGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 557
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTFQ----GE-WTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEVESALVQHPAV 434
|
490 500
....*....|....*....|....*
gi 4758332 558 DNICAFAKSDQSYVI---SFVVPNQ 579
Cdd:cd05959 435 LEAAVVGVEDEDGLTkpkAFVVLRP 459
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
221-657 |
2.24e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 95.33 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 221 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP----KDTYIGYLPLAHVLELTAEISCFTY- 295
Cdd:PRK08751 200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTANGLVFMKi 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 296 -GCRIGYSSPltlSDQSSKIKKgskgdctvLKPTLMAAVPEImdriyknvmskvqemnyiqKTLFKigydykleqikKGY 374
Cdd:PRK08751 280 gGCNHLISNP---RDMPGFVKE--------LKKTRFTAFTGV-------------------NTLFN-----------GLL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 375 DAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHrfmnvcfcCPIGQGYGLTESCGAGTVTEVT--DYTtGRVGAPLI 452
Cdd:PRK08751 319 NTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTG--------LTLVEAYGLTETSPAACINPLTlkEYN-GSIGLPIP 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 453 CCEIKLKDWQEGGYTINDKpnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PRK08751 390 STDACIKDDAGTVLAIGEI----GELCIKGPQVMKGYWKRPEETAK--VMDADG--WLHTGDIARMDEQGFVYIVDRKKD 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 533 LVkLQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKrltllaqqKGVEGTWVDICNNPAMEAEILKEi 612
Cdd:PRK08751 462 MI-LVSGFNVYPNEIEDVIAMMPGVLEVAAVG-----------VPDEK--------SGEIVKVVIVKKDPALTAEDVKA- 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 4758332 613 REAANamkLERFEIPIKVRLSPEpwTPEtglvTDAFKLKRKELRN 657
Cdd:PRK08751 521 HARAN---LTGYKQPRIIEFRKE--LPK----TNVGKILRRELRD 556
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
221-576 |
3.29e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 94.66 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 221 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCE-RIPGLG--PKDTYIGYLPLAHVLELTAEISCftyGC 297
Cdd:PLN02246 171 LPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLYfhSDDVILCVLPMFHIYSLNSVLLC---GL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 298 RIGysspltlsdqsSKIKKGSKGDCTVL-------KPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigyDYKLEQI 370
Cdd:PLN02246 248 RVG-----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKSPVVE----------------KYDLSSI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 371 kkgydaplcnlllfkkvkallggnvRMMLSGGAPLSPQTH-----RFMNVCfccpIGQGYGLTEscgAGTV--------T 437
Cdd:PLN02246 301 -------------------------RMVLSGAAPLGKELEdafraKLPNAV----LGQGYGMTE---AGPVlamclafaK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 438 EVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGE 517
Cdd:PLN02246 349 EPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDPEATAN--TIDKDG--WLHTGDIGY 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758332 518 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVV 576
Cdd:PLN02246 422 IDDDDELFIVDRLKELIKYK-GFQVAPAELEALLISHPSIADAAVVPMKDEVageVPVAFVV 482
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
87-615 |
4.05e-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: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGlKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYA-TLGKEA--VVHGLNESEASYLITS 163
Cdd:cd05931 27 YAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpTPGRHAerLAAILADAGPRVVLTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 164 VELLEsklktALLDIscvkhiiyvdnkainkAEYPEGFEIHSMQSVEELGSNPENLGIPPSrPTPSDMAIVMYTSGSTGR 243
Cdd:cd05931 106 AAALA-----AVRAF----------------AASRPAAGTPRLLVVDLLPDTSAADWPPPS-PDPDDIAYLQYTSGSTGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 244 PKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIGYSSPLT-LSDQSSKIKKGS 318
Cdd:cd05931 164 PKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYHdmglIGGLLTPLYS---GGPSVLMSPAAfLRRPLRWLRLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 319 KGDCTvlkptlMAAVPeimdriyknvmskvqemNYiqktlfkiGYDYkleQIKKGYDAPLCNLLLfkkvkallgGNVRMM 398
Cdd:cd05931 240 RYRAT------ISAAP-----------------NF--------AYDL---CVRRVRDEDLEGLDL---------SSWRVA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 399 LSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTESC--------GAGTVTEVTDYTTG--------------- 445
Cdd:cd05931 277 LNGAEPVRPATlRRFAEAfapfgfrpeAFRP----SYGLAEATlfvsggppGTGPVVLRVDRDALagravavaaddpaar 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 446 ---RVGAPLICCEIKLKDwQEGGytindKPNPR---GEIVIGGQNISMGYFKNEEKTAE--DYSVDENGQRWFCTGDIGE 517
Cdd:cd05931 353 elvSCGRPLPDQEVRIVD-PETG-----RELPDgevGEIWVRGPSVASGYWGRPEATAEtfGALAATDEGGWLRTGDLGF 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 518 FHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPlidnicafAKSDQSYVISFVVPNQKRLTLLAQQKgVEGTWVd 597
Cdd:cd05931 427 LH-DGELYITGRLKDLI-IVRGRNHYPQDIEATAEEAH--------PALRPGCVAAFSVPDDGEERLVVVAE-VERGAD- 494
|
570
....*....|....*...
gi 4758332 598 icnnPAMEAEILKEIREA 615
Cdd:cd05931 495 ----PADLAAIAAAIRAA 508
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
228-580 |
1.16e-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: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKdtyigylPLAHVleltaEISCFTYGCRIG-YSSPLT 306
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAHAWRREYELDSF-------PVRLL-----QMASFSFDVFAGdFARSLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LSDQSSKIKKGSKGDCTVL-------KPTLMAAVPE----IMDRIYKNvmskvqEMNYIQKTLFKIGYDykleqikkgyd 375
Cdd:cd17650 159 NGGTLVICPDEVKLDPAALydlilksRITLMESTPAlirpVMAYVYRN------GLDLSAMRLLIVGSD----------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 376 apLCNLLLFKKVKALLGGNVRMMLSggaplspqthrfmnvcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAP 450
Cdd:cd17650 222 --GCKAQDFKTLAARFGQGMRIINS------------------------YGVTEATIDSTYYEEGRDPLGDsanvpIGRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 451 LICCEIklkdwqeggYTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGC 523
Cdd:cd17650 276 LPNTAM---------YVLDERLQPQpvgvaGELYIGGAGVARGYLNRPELTAERFVENpfAPGERMYRTGDLARWRADGN 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 524 LQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 580
Cdd:cd17650 347 VELLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVVAVREDkggEARLCAYVVAAAT 405
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
230-579 |
2.18e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 92.21 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTG----QCERIPGLGPKDTYIGYLPLAHVLELtaeiSCFTYGcrigysspl 305
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELfvrfEASQYEYPGSDNVYLAALPMFHIYGL----SLFVVG--------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 306 TLSDQSSKIkkgskgdctvlkptlmaavpeIMDRIYKNVMSKVQEMNYIqkTLFKIgydykleqikkgydAPLCNLLLFK 385
Cdd:PLN02574 266 LLSLGSTIV---------------------VMRRFDASDMVKVIDRFKV--THFPV--------------VPPILMALTK 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 386 KVKALLGG---NVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGT----VTEVTDYTTGRVGAPLIccEIK 457
Cdd:PLN02574 309 KAKGVCGEvlkSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIQGYGMTESTAVGTrgfnTEKLSKYSSVGLLAPNM--QAK 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 458 LKDWQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTaeDYSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQ 537
Cdd:PLN02574 387 VVDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNPKAT--QSTIDKDG--WLRTGDIAYFDEDGYLYIVDRLKEIIKYK 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 4758332 538 aGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQ 579
Cdd:PLN02574 460 -GFQIAPADLEAVLISHPEIIDAAVTAVPDKecgEIPVAFVVRRQ 503
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
60-564 |
2.22e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 92.13 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 60 ILSEENEMQPNgkvfKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAE---------WMIAAQTcf 130
Cdd:PRK06155 26 MLARQAERYPD----RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEfldvflgcaWLGAIAV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 131 kynfPLVTlyATLGKEaVVHGLNESEASYLITSVELLESkLKTALLDISCVKHIIYVDnkAINKAEYPEGFEIHSMQsve 210
Cdd:PRK06155 100 ----PINT--ALRGPQ-LEHILRNSGARLLVVEAALLAA-LEAADPGDLPLPAVWLLD--APASVSVPAGWSTAPLP--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 211 elgsnPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAG-MTGqceRIPGLGPKDTYIGYLPLAHVLELTA 288
Cdd:PRK06155 167 -----PLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyWWGrNSA---EDLEIGADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 289 EISCFTYGCRIgysspltlsdqsskikkgskgdctVLKPTLMAAvpEIMDRIYKNvmskvqemnyiQKTLFkigydYKLe 368
Cdd:PRK06155 239 FFQALLAGATY------------------------VLEPRFSAS--GFWPAVRRH-----------GATVT-----YLL- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 369 qikkGYDAPLcnLLLFKKVKALLGGNVRMMLSGGAPlsPQTHRFMNVCFCCPIGQGYGLTES---CGaGTVTEVTDYTTG 445
Cdd:PRK06155 276 ----GAMVSI--LLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETnfvIA-VTHGSQRPGSMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 446 RVgAPLIccEIKLKDwqEGGYTIndKPNPRGEIVIGGQN---ISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDG 522
Cdd:PRK06155 347 RL-APGF--EARVVD--EHDQEL--PDGEPGELLLRADEpfaFATGYFGMPEKTVEAWR-----NLWFHTGDRVVRDADG 414
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 4758332 523 CLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 564
Cdd:PRK06155 415 WFRFVDRIKDAIRRR-GENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-656 |
2.89e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 89.64 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYSSP 304
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERL-GLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 305 LTlsDQSSKIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIQKTLFKIGydykleqikkgydaplcnll 382
Cdd:cd05917 78 SF--DPLAVLEAIEKEKCTALHgvPTMFIA-----------------ELEHPDFDKFDLS-------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 383 lfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR---VGAPLICCEIKL 458
Cdd:cd05917 119 -----------SLRTGIMAGAPCPPELmKRVIEVMNMKDVTIAYGMTETSPVSTQTRTDDSIEKRvntVGRIMPHTEAKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 459 KDwQEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDysvdENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQA 538
Cdd:cd05917 188 VD-PEGGIVP--PVGVPGELCIRGYSVMKGYWNDPEKTAEA----IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 539 GEYVSLGKVEAALKNCPLIDNICAFAKSDQSYvisfvvpnqkrltllaqqkGVE-GTWVDICNNPAMEAEilkEIREAAN 617
Cdd:cd05917 260 GENIYPREIEEFLHTHPKVSDVQVVGVPDERY-------------------GEEvCAWIRLKEGAELTEE---DIKAYCK 317
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 4758332 618 AmKLERFEIPIKVRLSPE-PwtpetglVTDAFKLKRKELR 656
Cdd:cd05917 318 G-KIAHYKVPRYVFFVDEfP-------LTVSGKIQKFKLR 349
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
81-580 |
3.99e-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: 91.00 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 81 NYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL 160
Cdd:cd17656 11 NQKL-TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ITSVELlESKLKtalldiscvkhiiyvDNKAINKAEYPegfeIHSMQSVEELGSNPENlgippsrptpSDMAIVMYTSGS 240
Cdd:cd17656 90 LTQRHL-KSKLS---------------FNKSTILLEDP----SISQEDTSNIDYINNS----------DDLLYIIYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 241 TGRPKGVMMHHSNLIAGMtgQCERipglgpkdTYIGYLPLAHVLELTAeiscftygcrigYSSPLTLSDQSSKIKKGskG 320
Cdd:cd17656 140 TGKPKGVQLEHKNMVNLL--HFER--------EKTNINFSDKVLQFAT------------CSFDVCYQEIFSTLLSG--G 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 321 DCTVLKPTLMAAVPEIMDRIYKNvmskvqemnYIQKTLFKIGYdykLEQI--KKGYDAPLcnlllFKKVKALLGGNVRMM 398
Cdd:cd17656 196 TLYIIREETKRDVEQLFDLVKRH---------NIEVVFLPVAF---LKFIfsEREFINRF-----PTCVKHIITAGEQLV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 399 LSggaplspQTHRFMNVCFCCPIGQGYGLTEScgagtvTEVTDYTTGR---------VGAPLICCEIKLKDWQEggytin 469
Cdd:cd17656 259 IT-------NEFKEMLHEHNVHLHNHYGPSET------HVVTTYTINPeaeipelppIGKPISNTWIYILDQEQ------ 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 470 dKPNPRG---EIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 544
Cdd:cd17656 320 -QLQPQGivgELYISGASVARGYLNRQELTAEKFFPDpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR-GYRIEL 397
|
490 500 510
....*....|....*....|....*....|....*....
gi 4758332 545 GKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 580
Cdd:cd17656 398 GEIEAQLLNHPGVSEAVVLDKADdkgEKYLCAYFVMEQE 436
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
227-659 |
4.36e-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: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLA---HVLE-LTAEISCftyGCRIGYS 302
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAL-GLTSESRVLQFASYTfdvSILEiFTTLAAG---GCLCIPS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 303 SPLTLSDQSSKIKKgSKGDCTVLKPTLMA-----AVPEImdriyknvmskvqemnyiqKTLFKIGydyklEQIKKgydap 377
Cdd:cd05918 180 EEDRLNDLAGFINR-LRVTWAFLTPSVARlldpeDVPSL-------------------RTLVLGG-----EALTQ----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 378 lcnlllfkKVKALLGGNVRMMlsggaplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVTDYTTGR-VGAPL--ICC 454
Cdd:cd05918 230 --------SDVDTWADRVRLI------------------------NAYGPAECTIAATVSPVVPSTDPRnIGRPLgaTCW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 455 EIKLKDwqeggytiNDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDY---------SVDENGQRWFCTGDIGEFHPDG 522
Cdd:cd05918 278 VVDPDN--------HDRLVPIgavGELLIEGPILARGYLNDPEKTAAAFiedpawlkqEGSGRGRRLYRTGDLVRYNPDG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 523 CLQIIDRKKDLVKLQaGEYVSLGKVEAALKNC-PLIDNICAFA-----KSDQSYVISFVVPNQkrltllAQQKGVEGTWV 596
Cdd:cd05918 350 SLEYVGRKDTQVKIR-GQRVELGEIEHHLRQSlPGAKEVVVEVvkpkdGSSSPQLVAFVVLDG------SSSGSGDGDSL 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758332 597 DICNNPAMEAEIlKEIREAANAmKLERFEIP-IKVRLSPEPWTPeTGlvtdafKLKRKELRNHY 659
Cdd:cd05918 423 FLEPSDEFRALV-AELRSKLRQ-RLPSYMVPsVFLPLSHLPLTA-SG------KIDRRALRELA 477
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
92-567 |
6.56e-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: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 92 RRVNNFGSGLTALGLKPKNTIAI-------FCETRAEWMIAAQTCFKYnfpLVTLYATLgKEAVVHGLNESEASYLITSV 164
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLilpnrftYIELSFAVAYAGGRLGLV---FVPLNPTL-KESVLRYLVADAGGRIVLAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLESKLKTALldISCVKHIIYVDNKAINKAEYPegfeihsmqsveelgsnpenlgIPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:cd05922 77 AGAADRLRDAL--PASPDPGTVLDADGIRAARAS----------------------APAHEVSHEDLALLLYTSGSTGSP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI----GYSSPLTLSDqsskikkgskg 320
Cdd:cd05922 133 KLVRLSHQNLLANARSIAEYL-GITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDDAFWE----------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 321 DCTVLKPTLMAAVPeimdriyknvmskvqemnYIQKTLFKIGYDykleqikkgyDAPLCNLllfkkvkallggnvRMMLS 400
Cdd:cd05922 201 DLREHGATGLAGVP------------------STYAMLTRLGFD----------PAKLPSL--------------RYLTQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 401 GGAPLSPQT-HRFmnvcfcCPIGQG------YGLTEsCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDwQEGGYTind 470
Cdd:cd05922 239 AGGRLPQETiARL------RELLPGaqvyvmYGQTE-ATRRMTYlppERILEKPGSIGLAIPGGEFEILD-DDGTPT--- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 471 KPNPRGEIVIGGQNISMGYFKNEektAEDYSVDENGQRWFcTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAA 550
Cdd:cd05922 308 PPGEPGEIVHRGPNVMKGYWNDP---PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIEAA 382
|
490
....*....|....*..
gi 4758332 551 LKNCPLIDNICAFAKSD 567
Cdd:cd05922 383 ARSIGLIIEAAAVGLPD 399
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
191-588 |
8.90e-19 |
|
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: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 191 AINKAEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGP 270
Cdd:cd05906 131 EFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 271 KDTYIGYLPLAHVLELT-AEISCFTYGCR-IGYSSPLTLSDqsskikkgskgdctvlkPTLMaavpeimdriyknvmskv 348
Cdd:cd05906 208 QDVFLNWVPLDHVGGLVeLHLRAVYLGCQqVHVPTEEILAD-----------------PLRW------------------ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 349 qeMNYIQKtlFKIGYDYkleqikkgydAP--LCNLLL-----FKKVKALLgGNVRMMLSGGAPLSPQTHRFM-------- 413
Cdd:cd05906 253 --LDLIDR--YRVTITW----------APnfAFALLNdlleeIEDGTWDL-SSLRYLVNAGEAVVAKTIRRLlrllepyg 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 414 ---NVcfccpIGQGYGLTESCgAGTVTEVTDYTTGR--------VGAPLICCEIKLKDwqeggytINDKPNPRGEI---V 479
Cdd:cd05906 318 lppDA-----IRPAFGMTETC-SGVIYSRSFPTYDHsqalefvsLGRPIPGVSMRIVD-------DEGQLLPEGEVgrlQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 480 IGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVKLQAGEYvSLGKVEAALKNCPLIDN 559
Cdd:cd05906 385 VRGPVVTKGYYNNPEANAE--AFTEDG--WFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNY-YSHEIEAAVEEVPGVEP 458
|
410 420 430
....*....|....*....|....*....|....*.
gi 4758332 560 --ICAFAKSDQS-----YVIsFVVPNQKRLTLLAQQ 588
Cdd:cd05906 459 sfTAAFAVRDPGaeteeLAI-FFVPEYDLQDALSET 493
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
204-534 |
1.05e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 89.55 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 204 HSMQSVEELGSNPEN------LGIPPSRPT----PSDMAIVMYTSGSTGRPKGVMMHHSNLIA-GMTgqCERIPGLGPKD 272
Cdd:PRK07514 121 AGAPHVETLDADGTGslleaaAAAPDDFETvprgADDLAAILYTSGTTGRSKGAMLSHGNLLSnALT--LVDYWRFTPDD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 273 TYIGYLPLAHVLELTAEISCftygcrigyssplTLSDQSSKIkkgskgdctvLKPTL-MAAVPEIMDRiyKNVMSKVqem 351
Cdd:PRK07514 199 VLIHALPIFHTHGLFVATNV-------------ALLAGASMI----------FLPKFdPDAVLALMPR--ATVMMGV--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 352 nyiqKTLfkigYDYKLEQikKGYDAPLCnlllfkkvkallgGNVRMMLSGGAPLSPQTHRfmnvCFCCPIGQG----YGL 427
Cdd:PRK07514 251 ----PTF----YTRLLQE--PRLTREAA-------------AHMRLFISGSAPLLAETHR----EFQERTGHAilerYGM 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 428 TESC--------G---AGTVtevtdyttgrvGAPLICCEIKLKDWQEGgytindKPNPRGE---IVIGGQNISMGYFKNE 493
Cdd:PRK07514 304 TETNmntsnpydGerrAGTV-----------GFPLPGVSLRVTDPETG------AELPPGEigmIEVKGPNVFKGYWRMP 366
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 4758332 494 EKTAEDYSVDenGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK07514 367 EKTAEEFRAD--G--FFITGDLGKIDERGYVHIVGRGKDLI 403
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
204-557 |
1.06e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 89.56 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 204 HSMQSVEELGSNpeNLGIPPSRPT-PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH 282
Cdd:PRK06145 125 AAQADSRRLAQG--GLEIPPQAAVaPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIAL-GLTASERLLVVGPLYH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 283 V--LELTAeISCFTYGCRIGYSSPLTLSDQSSKIKKgSKGDCTVLKPTLMAAVPEIMDRiyknvmskvqemnyiqktlfk 360
Cdd:PRK06145 202 VgaFDLPG-IAVLWVGGTLRIHREFDPEAVLAAIER-HRLTCAWMAPVMLSRVLTVPDR--------------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 361 igYDYKLeqikkgydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQTHR-----FMNVCFCcpigQGYGLTESCGAGT 435
Cdd:PRK06145 259 --DRFDL-------------------------DSLAWCIGGGEKTPESRIRdftrvFTRARYI----DAYGLTETCSGDT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 436 VTEVTDY--TTGRVGAPLICCEIKLKDwQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDengqrWFCTG 513
Cdd:PRK06145 308 LMEAGREieKIGSTGRALAHVEIRIAD-GAGRWL---PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----WFRSG 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 4758332 514 DIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLI 557
Cdd:PRK06145 379 DVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEV 421
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
83-568 |
1.06e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 90.04 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 83 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEW------MIAAQTCFKYNFPlVTLYATLGKEAvvhglnESE 156
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYgivalgIMAAGGVFSGANP-TALESEIKKQA------EAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 157 ASYLITSVELLESKLKTALLDIscvkhIIYVDNKAINKAEYPEgfeihSMQSVEELGSNPENLGIppsrpTPSDMAIVMY 236
Cdd:PLN02330 127 GAKLIVTNDTNYGKVKGLGLPV-----IVLGEEKIEGAVNWKE-----LLEAADRAGDTSDNEEI-----LQTDLCALPF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 237 TSGSTGRPKGVMMHHSNLIAGMtgqCERIPGLGP----KDTYIGYLPLAHVLELTAeISCFTYgcrigysspltlsDQSS 312
Cdd:PLN02330 192 SSGTTGISKGVMLTHRNLVANL---CSSLFSVGPemigQVVTLGLIPFFHIYGITG-ICCATL-------------RNKG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 313 KIKKGSKGDCTVLKPTLMAA-------VPEIMDRIYKNVMskVQEmnyiqktlfkigydYKLEQIKkgydaplcnlllfk 385
Cdd:PLN02330 255 KVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKNPI--VEE--------------FDLSKLK-------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 386 kvkallggnVRMMLSGGAPLSPQ-----THRFMNVcfccPIGQGYGLTE-SCGagTVTEvTDYTTGR-------VGAPLI 452
Cdd:PLN02330 305 ---------LQAIMTAAAPLAPElltafEAKFPGV----QVQEAYGLTEhSCI--TLTH-GDPEKGHgiakknsVGFILP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 453 CCEIKLKDWQEGGYTINDKPnprGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PLN02330 369 NLEVKFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYNNKEETDR--TIDEDG--WLHTGDIGYIDDDGDIFIVDRIKE 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 4758332 533 LVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:PLN02330 442 LIKYK-GFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
230-555 |
1.94e-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: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCRIGYSSPLTlsd 309
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFH-----------TFGYKAGIVACLL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 310 qsskikKGSkgdcTVLkPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGY--DYKLEQIKKGYD-APLCNLLLFKK 386
Cdd:cd17638 66 ------TGA----TVV-PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGrkKFDLSSLRAAVTgAATVPVELVRR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 387 VKALLGgnvrmmlsggaplspqthrFMNVCfccpigQGYGLTEsCGAGTVTEVTDYTT---GRVGAPLICCEIKLKDwqe 463
Cdd:cd17638 135 MRSELG-------------------FETVL------TAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 464 ggytindkpnpRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVS 543
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAE--AIDADG--WLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVY 249
|
330
....*....|..
gi 4758332 544 LGKVEAALKNCP 555
Cdd:cd17638 250 PAEVEGALAEHP 261
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
226-602 |
3.21e-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: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 226 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-------AGMTgqceripgLGPKDTyigylpLAHVLELTAEISCFTYGCR 298
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyvsqppARLD--------VGPGSR------VAQVLSIAFDACIGEIFST 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 299 IGYSSPLTLSDQSSKIKKGSKG-DCTVLKPTLMAAVPeimdriyknvmskvqemnyiqktlfkigydykleqiKKGYDap 377
Cdd:cd17653 168 LCNGGTLVLADPSDPFAHVARTvDALMSTPSILSTLS------------------------------------PQDFP-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 378 lcnlllfkkvkallggNVRMMLSGGAPLSP-------QTHRFMNvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAP 450
Cdd:cd17653 210 ----------------NLKTIFLGGEAVPPslldrwsPGRRLYN---------AYGPTECTISSTMTELLPGQPVTIGKP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 451 LICCEIKLKDwqeggytINDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQ 525
Cdd:cd17653 265 IPNSTCYILD-------ADLQPVPegvVGEICISGVQVARGYLGNPALTASKFVPDpfWPGSRMYRTGDYGRWTEDGGLE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 526 IIDRKKDLVKLQaGEYVSLGKVEA-ALKNCPLIDNICAFAKSDQsyVISFVVPN-------QKRLTLLAQQKGVEGTWVD 597
Cdd:cd17653 338 FLGREDNQVKVR-GFRINLEEIEEvVLQSQPEVTQAAAIVVNGR--LVAFVTPEtvdvdglRSELAKHLPSYAVPDRIIA 414
|
....*
gi 4758332 598 ICNNP 602
Cdd:cd17653 415 LDSFP 419
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
87-552 |
3.69e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 88.02 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK---------YNF---PLVTLYATLGKEAVVHglne 154
Cdd:PRK07798 31 YAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKaravpvnvnYRYvedELRYLLDDSDAVALVY---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 155 sEASYLITSVELLESKLKtalldiscVKHIIYVDNKAINkaEYPEGfeIHSMQSVEELGSnPENLGIPPSrptPSDMaIV 234
Cdd:PRK07798 107 -EREFAPRVAEVLPRLPK--------LRTLVVVEDGSGN--DLLPG--AVDYEDALAAGS-PERDFGERS---PDDL-YL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 235 MYTSGSTGRPKGVMMHHSNLiagmtgqceRIPGLGPKDTYIGylPLAHVLELTAEISCFTYGCRIGYSSPL--------T 306
Cdd:PRK07798 169 LYTGGTTGMPKGVMWRQEDI---------FRVLLGGRDFATG--EPIEDEEELAKRAAAGPGMRRFPAPPLmhgagqwaA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LSDQSSkikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmsKVQEMnyiqktlFKIGydykleqikkgyDA---PLcnlll 383
Cdd:PRK07798 238 FAALFS-------GQTVVLLPDVRFDADEVWRTIERE---KVNVI-------TIVG------------DAmarPL----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 fkkVKALLGGN------VRMMLSGGAPLSPQTHR-----FMNVCfccpIGQGYGLTES--CGAGTVTEVTDYTTG-RVGA 449
Cdd:PRK07798 284 ---LDALEARGpydlssLFAIASGGALFSPSVKEallelLPNVV----LTDSIGSSETgfGGSGTVAKGAVHTGGpRFTI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 450 plicceiklkdwqeGGYTI----NDKPNPRGEIVIG----GQNISMGYFKNEEKTAEDYSVdENGQRWFCTGDIGEFHPD 521
Cdd:PRK07798 357 --------------GPRTVvldeDGNPVEPGSGEIGwiarRGHIPLGYYKDPEKTAETFPT-IDGVRYAIPGDRARVEAD 421
|
490 500 510
....*....|....*....|....*....|.
gi 4758332 522 GCLQIIDRkKDLVKLQAGEYVSLGKVEAALK 552
Cdd:PRK07798 422 GTITLLGR-GSVCINTGGEKVFPEEVEEALK 451
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
227-579 |
6.88e-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: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIgylpLAH-------VLELtaeISCFTYGCRI 299
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDDVWT----LFHsyafdfsVWEI---WGALLHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 300 GYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAavpeimdriYKNVMSKVQEMNyiqktlfkigydykleqikkgyDAPLc 379
Cdd:cd17643 163 VVVPYEVARSPEDFARLLRDEGVTVLNQTPSA---------FYQLVEAADRDG----------------------RDPL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 380 nlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQ---GYGLTESCGAGTVTEVTDYTTGRVGAPLICCEI 456
Cdd:cd17643 211 --------------ALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETTVHVTFRPLDAADLPAAAASPIGRPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 457 klkdwqeGGYTI-----NDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVDEN---GQRWFCTGDIGEFHPDGCLQ 525
Cdd:cd17643 277 -------PGLRVyvldaDGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpGSRMYRTGDLARRLPDGELE 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 4758332 526 IIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 579
Cdd:cd17643 350 YLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDepgDTRLVAYVVADD 405
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
219-583 |
7.78e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 87.38 E-value: 7.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 219 LGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCE-------RIPGLGPKDTYIGYLPLAHVLELTAeis 291
Cdd:PRK07059 194 QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-QMEawlqpafEKKPRPDQLNFVCALPLYHIFALTV--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 292 CFTYGCRIGYSSPLTLS--DQSSKIKKGSKgdctvLKPTLMAAVpeimdriyknvmskvqemnyiqKTLFkigydykleq 369
Cdd:PRK07059 270 CGLLGMRTGGRNILIPNprDIPGFIKELKK-----YQVHIFPAV----------------------NTLY---------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 370 ikkgydaplcNLLL---------FKKVKALLGGnvrmmlsGGAPLSPQTHRFMNVCfCCPIGQGYGLTESCGAGTV--TE 438
Cdd:PRK07059 313 ----------NALLnnpdfdkldFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCnpVD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 439 VTDYTtGRVGAPLICCEIKLKDwQEGgytiNDKPNPR-GEIVIGGQNISMGYFKNEEKTAEDYSVDEngqrWFCTGDIGE 517
Cdd:PRK07059 375 ATEFS-GTIGLPLPSTEVSIRD-DDG----NDLPLGEpGEICIRGPQVMAGYWNRPDETAKVMTADG----FFRTGDVGV 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758332 518 FHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKRLT 583
Cdd:PRK07059 445 MDERGYTKIVDRKKDMI-LVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEhsgEAVKLFVVKKDPALT 512
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-577 |
8.55e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 164
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-- 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ellESKLKTALLDISCVkhiIYVDNKAINKAEYPegfeihsmqsveelgsnpenlgiPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 3161 ---QSHLRLPLAQGVQV---LDLDRGDENYAEAN-----------------------PAIRTMPENLAYVIYTSGSTGKP 3211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLI--AGMTGQCEripGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQsskikkgskgdc 322
Cdd:PRK12316 3212 KGVGIRHSALSnhLCWMQQAY---GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP------------ 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 323 tvlkptlmAAVPEIMDRIYKNVMSKVQEMnyIQKtlfkigydykleqikkgydaplcnllLFKKVKALLGGNVRMMLSGG 402
Cdd:PRK12316 3277 --------ALLVELINSEGVDVLHAYPSM--LQA--------------------------FLEEEDAHRCTSLKRIVCGG 3320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 403 APLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwqeggytINDKPNPRG---E 477
Cdd:PRK12316 3321 EALPADLQQQVFAGL--PLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-------GSLEPVPVGalgE 3391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 478 IVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCP 555
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLTAERFVPDpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHP 3470
|
490 500
....*....|....*....|..
gi 4758332 556 LIDNICAFAKSDQSyVISFVVP 577
Cdd:PRK12316 3471 WVREAVVLAVDGRQ-LVAYVVP 3491
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
229-656 |
1.01e-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: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLS 308
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPT-AAYWLGLRPDDIH-----------WNIADPGWAKGAWSSFFGPWLLG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 309 dqsskikkgskgdCTVLKPTLMAAVPEimdRIYKnVMSKvqemnyiqktlfkigydyklEQIKKGYDAPLCNLLLFKKvk 388
Cdd:cd05972 149 -------------ATVFVYEGPRFDAE---RILE-LLER--------------------YGVTSFCGPPTAYRMLIKQ-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 389 ALLGGN---VRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGG 465
Cdd:cd05972 190 DLSSYKfshLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 466 YTindKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYSVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVS 543
Cdd:cd05972 269 EL---PPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD-----YYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 544 LGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVpnqkrltllaQQKGVEGTwvdicnnPAMEAEILKEIREaanamK 620
Cdd:cd05972 340 PFEVESALLEHPAVAEAAVVGSPDPVRgevVKAFVV----------LTSGYEPS-------EELAEELQGHVKK-----V 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 4758332 621 LERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELR 656
Cdd:cd05972 398 LAPYKYPREIEFVEElPKTI-SG------KIRRVELR 427
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
87-534 |
1.28e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 86.93 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAifcetraewmiaaqtcfkYNFPLV--TLYATLGKEA---------------VV 149
Cdd:PRK07529 61 YAELLADVTRTANLLHSLGVGPGDVVA------------------FLLPNLpeTHFALWGGEAagianpinpllepeqIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 150 HGLNESEASYLITSVELLES----KLKTALLDISCVKHIIYVDnkaINKAEYPEGFEIHSMQSV----------EELGSN 215
Cdd:PRK07529 123 ELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVD---LARYLPGPKRLAVPLIRRkaharildfdAELARQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 216 PENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFT 294
Cdd:PRK07529 200 PGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA-NAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGlAPLA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 295 YGCRIGYSSPLtlsdqsskikkGSKGdctvlkPTLMAAVPEIMDRIYKNVMSKVqemnyiqKTLFkigydykleqikkgy 374
Cdd:PRK07529 279 RGAHVVLATPQ-----------GYRG------PGVIANFWKIVERYRINFLSGV-------PTVY--------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 375 daplcNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHR-FMNVCfCCPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLI 452
Cdd:PRK07529 320 -----AALLQVPVDGHDISSLRYALCGAAPLPVEVFRrFEAAT-GVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 453 CCEIK-LKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFkNEEKTAEDYSvdenGQRWFCTGDIGEFHPDGCLQIIDRKK 531
Cdd:PRK07529 394 YQRVRvVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL----EDGWLNTGDLGRIDADGYFWLTGRAK 468
|
...
gi 4758332 532 DLV 534
Cdd:PRK07529 469 DLI 471
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-577 |
1.37e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.71 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLEsklktaLLDISCVKHIIYVDNKAINKAEYPEGfeihsmqsveelgsNPEnlgippSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 617 HLGR------KLPLAAGVQVLDLDRPAAWLEGYSEE--------------NPG------TELNPENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkgskgdctv 324
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRD--------------- 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 lkptlMAAVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykleqikkgydapLCNLLLFKKVKALLggNVRMMLSGGAP 404
Cdd:PRK12316 735 -----PAKLVELINREGVDTLHFVPSM--------------------------LQAFLQDEDVASCT--SLRRIVCSGEA 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 405 LS-----------PQTHRFmNVcfccpigqgYGLTESCGAGT----VTEVTDytTGRVGAPLIcceiklkdwQEGGYTIN 469
Cdd:PRK12316 782 LPadaqeqvfaklPQAGLY-NL---------YGPTEAAIDVThwtcVEEGGD--SVPIGRPIA---------NLACYILD 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 470 DKPNP-----RGEIVIGGQNISMGYFKNEEKTAEDYSVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYV 542
Cdd:PRK12316 841 ANLEPvpvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRI 919
|
490 500 510
....*....|....*....|....*....|....*
gi 4758332 543 SLGKVEAALKNCPLIDNICAFAKSDQSYViSFVVP 577
Cdd:PRK12316 920 ELGEIEARLLEHPWVREAAVLAVDGKQLV-GYVVL 953
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
222-577 |
1.72e-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: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLA---HVLELTAEISCftyGCR 298
Cdd:cd17646 131 PLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYP-LGPGDRVLQKTPLSfdvSVWELFWPLVA---GAR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 299 IGYSSPLTLSDqsskikkgskgdctvlkptlMAAVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykLEQIKKGYDAPL 378
Cdd:cd17646 207 LVVARPGGHRD--------------------PAYLAALIREHGVTTCHFVPSM---------------LRVFLAEPAAGS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 379 CnlllfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTEscgagTVTEVTDYT-TGRVGAPLIccEI 456
Cdd:cd17646 252 C-------------ASLRRVFCSGEALPPELaARFLAL-PGAELHNLYGPTE-----AAIDVTHWPvRGPAETPSV--PI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 457 KLKDWQEGGYTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDR 529
Cdd:cd17646 311 GRPVPNTRLYVLDDALRPVpvgvpGELYLGGVQLARGYLGRPALTAERFVPDpfGPGSRMYRTGDLARWRPDGALEFLGR 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 4758332 530 KKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd17646 391 SDDQVKIR-GFRVEPGEIEAALAAHPAVTHAVVVARAAPAgaaRLVGYVVP 440
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
36-534 |
1.96e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.02 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 36 DTLDKLFDHAVSKFGKKDSLGTREilseenemqpngkvfkklilGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIF 115
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRD--------------------QGLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 116 CETRAEWmiaaqtcfkynfpLVTLYAT--LGkeAVV-------------HGLNESEASYLITS--------VELLES--- 169
Cdd:PRK08315 75 APNVPEW-------------VLTQFATakIG--AILvtinpayrlseleYALNQSGCKALIAAdgfkdsdyVAMLYElap 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 170 --------KLKTALLdiSCVKHIIYVDnkainkAEYPEGFeiHSMQSVEELGSNPENLGIPPSRPT--PSDmAIVM-YTS 238
Cdd:PRK08315 140 elatcepgQLQSARL--PELRRVIFLG------DEKHPGM--LNFDELLALGRAVDDAELAARQATldPDD-PINIqYTS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 239 GSTGRPKGVMMHHSNLI--AGMTGQCERipgLGPKDTYIGYLPLAH----VLeltAEISCFTYGCRIGYssPLTLSDQSS 312
Cdd:PRK08315 209 GTTGFPKGATLTHRNILnnGYFIGEAMK---LTEEDRLCIPVPLYHcfgmVL---GNLACVTHGATMVY--PGEGFDPLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 313 KIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIqktLFKigyDYKLEQIKKGYDA-PLCNLLLFKKVKA 389
Cdd:PRK08315 281 TLAAVEEERCTALYgvPTMFIA-----------------ELDHP---DFA---RFDLSSLRTGIMAgSPCPIEVMKRVID 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 390 llggnvRMMLSGgaplspqthrfmnVCFCcpigqgYGLTESCGAGTVTEVTD-----YTTgrVGAPLICCEIKLKDwQEG 464
Cdd:PRK08315 338 ------KMHMSE-------------VTIA------YGMTETSPVSTQTRTDDplekrVTT--VGRALPHLEVKIVD-PET 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 465 GYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK08315 390 GETV--PRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDADG--WMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
230-577 |
1.99e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 86.09 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI-----GYSS 303
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYHGHGLIAALlATLASGGAVllparGRFS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 304 PLTLSDqsskikkgskgDCTVLKPTLMAAVPeimdriyknvmskvqemnyiqkTLFKIGYDYKLEQIKKGYDAPLcnlll 383
Cdd:PRK05852 256 AHTFWD-----------DIKAVGATWYTAVP----------------------TIHQILLERAATEPSGRKPAAL----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 fkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY--------TTGRVG---APLI 452
Cdd:PRK05852 298 ------------RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIgqtenpvvSTGLVGrstGAQI 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 453 ccEIKLKDWQEGGytindkPNPRGEIVIGGQNISMGYFKNEEKTAEDYSvdeNGqrWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PRK05852 366 --RIVGSDGLPLP------AGAVGEVWLRGTTVVRGYLGDPTITAANFT---DG--WLRTGDLGSLSAAGDLSIRGRIKE 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 4758332 533 LVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 577
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) ... |
222-583 |
3.48e-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: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPL---AHVLELtaeiscFTYGCr 298
Cdd:cd17651 129 PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS-LGPGARTLQFAGLgfdVSVQEI------FSTLC- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 299 igysspltlsdqsskikkgsKGDCTVLKP--------TLMAAVPEimdriyknvmskvqemnyiqktlfkigydYKLEQI 370
Cdd:cd17651 201 --------------------AGATLVLPPeevrtdppALAAWLDE-----------------------------QRISRV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 371 kkgyDAP---LCNLLLFKKVKALLGGNVRMMLSGGAPLS--------PQTHRFMNVCFccpigqGYGLTESCGAgTVTEV 439
Cdd:cd17651 232 ----FLPtvaLRALAEHGRPLGVRLAALRYLLTGGEQLVltedlrefCAGLPGLRLHN------HYGPTETHVV-TALSL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 440 TDYTTGR-----VGAPLICCEIKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVDE--NGQRW 509
Cdd:cd17651 301 PGDPAAWpapppIGRPIDNTRVYVLD-------AALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPfvPGARM 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758332 510 FCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQsyvisfvvPNQKRLT 583
Cdd:cd17651 374 YRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALARHPGVREAVVLAREDR--------PGEKRLV 438
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
77-659 |
3.50e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 84.98 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 77 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESE 156
Cdd:PRK08316 30 LVFGDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 157 ASYLITSVELLEskLKTALLDISCVKHIIYVDnkAINKAEYPEGFeiHSMQSVEELGSNPEnlgiPPSRPTPSDMAIVMY 236
Cdd:PRK08316 109 ARAFLVDPALAP--TAEAALALLPVDTLILSL--VLGGREAPGGW--LDFADWAEAGSVAE----PDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 237 TSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvlelTAEISCFTygcrigysSPLTLSDQSSKIkk 316
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVS-CIVAGDMSADDIPLHALPLYH----CAQLDVFL--------GPYLYVGATNVI-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 317 gskgdctVLKPTLmaavPEIMDRIYKnvmskvqemnYIQKTLFK-----IG------YD-YKLEQIKKGYdaplcnlllf 384
Cdd:PRK08316 244 -------LDAPDP----ELILRTIEA----------ERITSFFApptvwISllrhpdFDtRDLSSLRKGY---------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 385 kkvkallggnvrmmlsGGAPLSPQT------HRFMNVCF--CcpigqgYGLTESCGAGTV--TEVTDYTTGRVGAPLICC 454
Cdd:PRK08316 293 ----------------YGASIMPVEvlkelrERLPGLRFynC------YGQTEIAPLATVlgPEEHLRRPGSAGRPVLNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 455 EIKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKK 531
Cdd:PRK08316 351 ETRVVD-------DDGNDVAPgevGEIVHRSPQLMLGYWDDPEKTAEAF---RGG--WFHSGDLGVMDEEGYITVVDRKK 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 532 DLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqqkgVEGTWVDicnnpamEAEI 608
Cdd:PRK08316 419 DMIK-TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWieaVTAVVVP-------------KAGATVT-------EDEL 477
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 4758332 609 LKEIREaanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHY 659
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 ... |
85-579 |
4.50e-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: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLESkLKTALLDISCVKHIIyvdnkAINKAEYPEgfeihsMQSVEELGSNPEnlGIPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:TIGR02262 111 ALLPV-IKAALGKSPHLEHRV-----VVGRPEAGE------VQLAELLATESE--QFKPAATQADDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLsdqsskikkgskGDCTV 324
Cdd:TIGR02262 177 KGVVHTHSNPYWTAELYARNTLGIREDDVC-----------FSAAKLFFAYGLGNALTFPMSV------------GATTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 lkptLMAAVPeIMDRIYKnvmskvqEMNYIQKTLFkigydykleqikkgYDAP--LCNLLLFKKVKALLGGNVRMMLSGG 402
Cdd:TIGR02262 234 ----LMGERP-TPDAVFD-------RLRRHQPTIF--------------YGVPtlYAAMLADPNLPSEDQVRLRLCTSAG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 403 APLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGGYTINDKPnprGEIVIGG 482
Cdd:TIGR02262 288 EALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG-DGGQDVADGEP---GELLISG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 483 QNISMGYFKNEEKTAEDYSVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICA 562
Cdd:TIGR02262 364 PSSATMYWNNRAKSRDTFQGE-----WTRSGDKYVRNDDGSYTYAGRTDDMLKV-SGIYVSPFEIESALIQHPAVLEAAV 437
|
490 500
....*....|....*....|
gi 4758332 563 FAKSDQSYVI---SFVVPNQ 579
Cdd:TIGR02262 438 VGVADEDGLIkpkAFVVLRP 457
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
93-656 |
5.32e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.85 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 93 RVNNFGSGLTALGLKPKNTIAIFC---ETRAEWMIAaqtcfkynfplVTLYAtlgkeAVVHGLNE----SEASYLITSVE 165
Cdd:PLN02860 41 GVLSLAAGLLRLGLRNGDVVAIAAlnsDLYLEWLLA-----------VACAG-----GIVAPLNYrwsfEEAKSAMLLVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 166 llesklKTAL-LDISCVKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGS--NPENL---GIPPSRPT----PSDMAIVM 235
Cdd:PLN02860 105 ------PVMLvTDETCSSWYEELQNDRLPSLMWQVFLESPSSSVFIFLNSflTTEMLkqrALGTTELDyawaPDDAVLIC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 236 YTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVleltaeiscftyGcriGYSSPLTLSdqsskik 315
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALIVQSLAKIA-IVGYGEDDVYLHTAPLCHI------------G---GLSSALAML------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 316 kgSKGDCTVLKPTLMA-AVPEIMDRIYKNVMSKVQEMnyiqktlfkigydykleqikkgydapLCNLLLFKKVKALLGGN 394
Cdd:PLN02860 236 --MVGACHVLLPKFDAkAALQAIKQHNVTSMITVPAM--------------------------MADLISLTRKSMTWKVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 395 --VRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPL-ICCEIKLKDWQEGGYTIND 470
Cdd:PLN02860 288 psVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLqTVNQTKSSSVHQPQGVCVG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 471 KPNPRGEIVIG-------------GQNISMGYFKNEEKTAEDYSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQ 537
Cdd:PLN02860 368 KPAPHVELKIGldessrvgriltrGPHVMLGYWGQNSETASVLSNDG----WLDTGDIGWIDKAGNLWLIGRSNDRIK-T 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 538 AGEYVSLGKVEAALKNCPLIdnicafaksdqSYVISFVVPNQkRLT--LLAQQKGVEG-TWVDIcNNPAMEAEIL---KE 611
Cdd:PLN02860 443 GGENVYPEEVEAVLSQHPGV-----------ASVVVVGVPDS-RLTemVVACVRLRDGwIWSDN-EKENAKKNLTlssET 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 4758332 612 IREAANAMKLERFEIP--IKVRLSPEPWTpETGlvtdafKLKRKELR 656
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 ... |
227-583 |
6.09e-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: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPlAHVLELTAEiscftygcrigyssPLT 306
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFS-NYVFDFFVE--------------QMT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LSDQSskikkgskGDCTVLKPTLMAAVPeimDRIYKnvmskvqemnYIQKTlfKIGYDYKLEQIKKGYDAPLCNLLlfkk 386
Cdd:cd17648 157 LALLN--------GQKLVVPPDEMRFDP---DRFYA----------YINRE--KVTYLSGTPSVLQQYDLARLPHL---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 387 vkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgagTVTE-VTDYTTGRVGAPLICCEIKLKDWqegg 465
Cdd:cd17648 210 ---------KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET----TVTNhKRFFPGDQRFDKSLGRPVRNTKC---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 466 YTIND--KPNP---RGEIVIGGQNISMGYFKNEEKTAEDY----------SVDENGQRWFCTGDIGEFHPDGCLQIIDRK 530
Cdd:cd17648 273 YVLNDamKRVPvgaVGELYLGGDGVARGYLNRPELTAERFlpnpfqteqeRARGRNARLYKTGDLVRWLPSGELEYLGRN 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758332 531 KDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD--------QSYVISFVVPNQKRLT 583
Cdd:cd17648 353 DFQVKIR-GQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriQKYLVGYYLPEPGHVP 412
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
87-577 |
9.07e-17 |
|
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: 9.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAqtcfkynfplvtLYATLGkeavvhglneSEASYLItsvel 166
Cdd:cd12115 27 YAELNRRANRLAARLRAAGVGPESRVGVCLERTPD-LVVA------------LLAVLK----------AGAAYVP----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 lesklktalLDiscvkhiiyvdnkainkAEYPEgfeihsmqsvEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKG 246
Cdd:cd12115 79 ---------LD-----------------PAYPP----------ERLRFILEDAQARLVLTDPDDLAYVIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VMMHHSNLIAGMTGQCERIPglgpKDTyigylpLAHVLELTA---EISCF------TYGCRIGY-SSPLTLSDQSSKikk 316
Cdd:cd12115 123 VAIEHRNAAAFLQWAAAAFS----AEE------LAGVLASTSicfDLSVFelfgplATGGKVVLaDNVLALPDLPAA--- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 317 gskgdCTVlkpTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQikkgyDAplcnlllfkkvkalLGGNVR 396
Cdd:cd12115 190 -----AEV---TLINTVPSAAAEL--------------------------LRH-----DA--------------LPASVR 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 397 MMLSGGAPLS----------PQTHRFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGRV--GAPLicceiklkdwqeG 464
Cdd:cd12115 217 VVNLAGEPLPrdlvqrlyarLQVERVVNL---------YGPSEDTTYSTVAPVPPGASGEVsiGRPL------------A 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 465 G---YTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:cd12115 276 NtqaYVLDRALQPVplgvpGELYIGGAGVARGYLGRPGLTAERFLPDpfGPGARLYRTGDLVRWRPDGLLEFLGRADNQV 355
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 4758332 535 KLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd12115 356 KVR-GFRIELGEIEAALRSIPGVREAVVVAIGDAAgerRLVAYIVA 400
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
221-557 |
1.05e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 83.32 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 221 IPPSRPTpsdmaIVMYTSGSTGRPKGVMMHHSNLIA-----GMTGQceripgLGPKDTYIGYLPLAHVLELTAEI-SCFT 294
Cdd:PRK09088 132 IPPERVS-----LILFTSGTSGQPKGVMLSERNLQQtahnfGVLGR------VDAHSSFLCDAPMFHIIGLITSVrPVLA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 295 YGCRI----GYSSPLTLsdqsskikkGSKGDCTvLKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykleQI 370
Cdd:PRK09088 201 VGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAF----------------------------RA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 371 KKGYDAplcnlllfkkvKALlgGNVRMMLSGGAPlSPQTHRFMNVCFCCPIGQGYGLTEscgAGTV------TEVTDYTT 444
Cdd:PRK09088 243 QPGFDA-----------AAL--RHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSE---AGTVfgmsvdCDVIRAKA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 445 GRVGAPLICCEIKLKDWQEggytiND-KPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGC 523
Cdd:PRK09088 306 GAAGIPTPTVQTRVVDDQG-----NDcPAGVPGELLLRGPNLSPGYWRRPQATAR--AFTGDG--WFRTGDIARRDADGF 376
|
330 340 350
....*....|....*....|....*....|....
gi 4758332 524 LQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLI 557
Cdd:PRK09088 377 FWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
208-670 |
1.26e-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: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 208 SVEELGSNPENLGIPPSRP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKD-TYIGYLPLAHvl 284
Cdd:cd05921 142 SFAELAATPPTAAVDAAFAavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNH-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 285 eltaeiscfTYGCRIGYSspLTLSDQSS-KIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyiqkt 357
Cdd:cd05921 220 ---------TFGGNHNFN--LVLYNGGTlYIDDG--------KPmpggfeETLRNLREISPTVYFNV------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 358 lfKIGYDYKLEQIKKgyDAPLCNLLlFKkvkallggNVRMMLSGGAPLSPQT-------------HRFmnvcfccPIGQG 424
Cdd:cd05921 268 --PAGWEMLVAALEK--DEALRRRF-FK--------RLKLMFYAGAGLSQDVwdrlqalavatvgERI-------PMMAG 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 425 YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLkdwqeggYTINDKPnprgEIVIGGQNISMGYFKNEEKTAEdySVDE 504
Cdd:cd05921 328 LGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKY----EVRVKGPNVTPGYWRQPELTAQ--AFDE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 505 NGqrWFCTGDIGEF----HPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNC--PLIDNIcAFAKSDQSYVISFVVPN 578
Cdd:cd05921 395 EG--FYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRARAVAAcaPLVHDA-VVAGEDRAEVGALVFPD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 579 QKRLTLLAQqkgvegtwvdicNNPAMEAEILK--EIREAANAMkLERFE--------IPIKVRLSPEPWTPETGLVTDAF 648
Cdd:cd05921 472 LLACRRLVG------------LQEASDAEVLRhaKVRAAFRDR-LAALNgeatgsssRIARALLLDEPPSIDKGEITDKG 538
|
490 500
....*....|....*....|..
gi 4758332 649 KLKRKELRNHYLKDIERMYGGK 670
Cdd:cd05921 539 YINQRAVLERRAALVERLYADT 560
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-579 |
1.63e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.44 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLesklktALLDISCVKHIIYVDNKAINKAEYPEGFeihsmqsveelgsnpenlgiPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12467 618 HLL------AQLPVPAGLRSLCLDEPADLLCGYSGHN--------------------PEVALDPDNLAYVIYTSGSTGQP 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTV 324
Cdd:PRK12467 672 KGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTV 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LKptlmaAVPeimdriyknvmskvqemNYIQKTLfkigydykleqikkgyDAPLCNLLLfkKVKALLGGNVRMMLSGGAP 404
Cdd:PRK12467 751 LK-----IVP-----------------SHLQALL----------------QASRVALPR--PQRALVCGGEALQVDLLAR 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 405 ---LSPQThRFMNVcfccpigqgYGLTESCGAGTVTEVT----DYTTGRVGAPLICCEIKLKDWQeggytINDKPNP-RG 476
Cdd:PRK12467 791 vraLGPGA-RLINH---------YGPTETTVGVSTYELSdeerDFGNVPIGQPLANLGLYILDHY-----LNPVPVGvVG 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 477 EIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKN 553
Cdd:PRK12467 856 ELYIGGAGLARGYHRRPALTAERFVPDpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR-GFRIELGEIEARLLA 934
|
490 500
....*....|....*....|....*...
gi 4758332 554 CPLIDN--ICAFAKSDQSYVISFVVPNQ 579
Cdd:PRK12467 935 QPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
230-551 |
2.09e-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: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsd 309
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRV-----------FSSAKMFFGYGLGNSLWFPL---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 310 qsskikkgSKGDCTVLKPTlmAAVPEimdriykNVMSKVQEMnyiQKTLFkigydykleqikkgYDAP--LCNLLLFKKV 387
Cdd:cd05919 157 --------AVGASAVLNPG--WPTAE-------RVLATLARF---RPTVL--------------YGVPtfYANLLDSCAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 388 KALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYT 467
Cdd:cd05919 203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD--EEGHT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 468 IndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKV 547
Cdd:cd05919 281 I--PPGEEGDLLVRGPSAAVGYWNNPEKSRATF----NGG-WYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEV 352
|
....
gi 4758332 548 EAAL 551
Cdd:cd05919 353 ESLI 356
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
225-583 |
2.77e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 82.41 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 225 RP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERI--PGLGP-KDTYIGYLPLAHVLELTaeISCFTYgcri 299
Cdd:PRK08974 200 KPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QAKAAygPLLHPgKELVVTALPLYHIFALT--VNCLLF---- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 300 gysspltlsdqsskIKKGSKGdctvLKPTLMAAVPEIMDRIYKNVMSKVQEMNyiqkTLFkigydykleqikkgydaplc 379
Cdd:PRK08974 273 --------------IELGGQN----LLITNPRDIPGFVKELKKYPFTAITGVN----TLF-------------------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 380 NLLL----FKKVKAllgGNVRMMLSGGAPL-SPQTHRFMNVCfCCPIGQGYGLTEsCG---AGTVTEVTDYTtGRVGAPL 451
Cdd:PRK08974 311 NALLnneeFQELDF---SSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTE-CSplvSVNPYDLDYYS-GSIGLPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 452 ICCEIKLKDwQEGgytiNDKPN-PRGEIVIGGQNISMGYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRK 530
Cdd:PRK08974 385 PSTEIKLVD-DDG----NEVPPgEPGELWVKGPQVMLGYWQRPEATDE---VIKDG--WLATGDIAVMDEEGFLRIVDRK 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 531 KDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKRLT 583
Cdd:PRK08974 455 KDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLT 509
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
227-669 |
5.06e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 81.85 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPGLGPKdTYIGYLPLAHVLeltaeiscftygcriGYSSP 304
Cdd:PRK08180 207 GPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqMLAQTFPFLAEEPP-VLVDWLPWNHTF---------------GGNHN 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 305 LTLsdqsskikkgskgdctVL-----------KPTlmaavPEIMDRIYKNvmskvqeMNYIQKTLF---KIGYDYKLEQI 370
Cdd:PRK08180 271 LGI----------------VLynggtlyiddgKPT-----PGGFDETLRN-------LREISPTVYfnvPKGWEMLVPAL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 371 KKgyDAPLCNLLLfkkvkallgGNVRMMLSGGAPLSPQT----HRF-MNVC-----FCCpigqGYGLTESCGAGTVTEVT 440
Cdd:PRK08180 323 ER--DAALRRRFF---------SRLKLLFYAGAALSQDVwdrlDRVaEATCgerirMMT----GLGMTETAPSATFTTGP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 441 DYTTGRVGAPLICCEIKLKDwqEGGytindkpnpRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFH- 519
Cdd:PRK08180 388 LSRAGNIGLPAPGCEVKLVP--VGG---------KLEVRVKGPNVTPGYWRAPELTAE--AFDEEG--YYRSGDAVRFVd 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 520 PDgclqiiDRKKDLV---------KLQAGEYVSLG----KVEAALKncPLIDNICaFAKSDQSYVISFVVPNQKRLTLLA 586
Cdd:PRK08180 453 PA------DPERGLMfdgriaedfKLSSGTWVSVGplraRAVSAGA--PLVQDVV-ITGHDRDEIGLLVFPNLDACRRLA 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 587 QQkGVEGTWVDICNNPAMEA---EILKEIREAA--NAMKLERfeipikVRLSPEPWTPETGLVTDAFKLKRKELRNHYLK 661
Cdd:PRK08180 524 GL-LADASLAEVLAHPAVRAafrERLARLNAQAtgSSTRVAR------ALLLDEPPSLDAGEITDKGYINQRAVLARRAA 596
|
....*...
gi 4758332 662 DIERMYGG 669
Cdd:PRK08180 597 LVEALYAD 604
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
85-577 |
5.31e-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: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 164
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsNPENLgippsrptpsdmAIVMYTSGSTGRP 244
Cdd:cd17644 104 --------------------------------------------------QPENL------------AYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDtyigylplaHVLELtaeiSCFTYGCRIGYSSPLTLSdqsskikkgskGDCTV 324
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEY-GITSSD---------RVLQF----ASIAFDVAAEEIYVTLLS-----------GATLV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LKPTLMAAVPEIMdriyknvmskvqeMNYIQK---TLFKIGYDYKLEQIKKGydaplcnlllfKKVKALLGGNVRMMLSG 401
Cdd:cd17644 177 LRPEEMRSSLEDF-------------VQYIQQwqlTVLSLPPAYWHLLVLEL-----------LLSTIDLPSSLRLVIVG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 402 GAPLSPQTH-----------RFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIKLKDWqegg 465
Cdd:cd17644 233 GEAVQPELVrqwqknvgnfiQLINV---------YGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILDE---- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 466 ytiNDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYSVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQa 538
Cdd:cd17644 300 ---NLQPVPvgvPGELHIGGVGLARGYLNRPELTAEKFISHpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIR- 375
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 4758332 539 GEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd17644 376 GFRIELGEIEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVP 417
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
209-555 |
5.33e-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: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 209 VEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERipGLGPKDTYIGYLPL---AHVLE 285
Cdd:cd12117 116 VIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV--TLGPDDRVLQTSPLafdASTFE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 286 LtaeiscftYGCRIgysspltlsdqsskikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSkvqemnyiqkTLFKIgydy 365
Cdd:cd12117 194 I--------WGALL------------------NGARLVLAPKGTLLDPDALGALIAEEGVT----------VLWLT---- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 366 kleqikkgydAPLCNLLLFKKVKALLGgnVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DY 442
Cdd:cd12117 234 ----------AALFNQLADEDPECFAG--LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTelDE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 443 TTGRV--GAPLICCEIKLKDwqEGGytindKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDI 515
Cdd:cd12117 302 VAGSIpiGRPIANTRVYVLD--EDG-----RPVPPgvpGELYVGGDGLALGYLNRPALTAERFVADpfGPGERLYRTGDL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 4758332 516 GEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCP 555
Cdd:cd12117 375 ARWLPDGRLEFLGRIDDQVKIR-GFRIELGEIEAALRAHP 413
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
83-534 |
8.57e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 80.85 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 83 KWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL-- 160
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlc 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ----------ITSVELLESKLKTALLD-ISCVKHIIY--VDNKAINK-AEYPEGFEIHSMQSVE-------ELGSNPENl 219
Cdd:PRK06710 128 ldlvfprvtnVQSATKIEHVIVTRIADfLPFPKNLLYpfVQKKQSNLvVKVSESETIHLWNSVEkevntgvEVPCDPEN- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 220 gippsrptpsDMAIVMYTSGSTGRPKGVMMHHSNLIAG-MTGQCERIPGLGPKDTYIGYLPLAHVLELTAEIS-CFTYGC 297
Cdd:PRK06710 207 ----------DLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNlSIMQGY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 298 RIGYSSPLTLSDQSSKIKKGskgdctvlKPTLMAAVPEImdriyknvmskvqemnYIQktlfkigydykleqikkgydap 377
Cdd:PRK06710 277 KMVLIPKFDMKMVFEAIKKH--------KVTLFPGAPTI----------------YIA---------------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 378 LCNLLLFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT----DYTTGRVGAPLIC 453
Cdd:PRK06710 311 LLNSPLLKEYDI---SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES---SPVTHSNflweKRVPGSIGVPWPD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 454 CEIKLKDWQEGGYTindKPNPRGEIVIGGQNISMGYFKNEEKTAedySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDL 533
Cdd:PRK06710 385 TEAMIMSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETA---AVLQDG--WLHTGDVGYMDEDGFFYVKDRKKDM 456
|
.
gi 4758332 534 V 534
Cdd:PRK06710 457 I 457
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
227-656 |
1.08e-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: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCE---RIPGLGPKDTYIGYLPL---AHVLELTAEISCftygcrig 300
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQataERYGLTPGDRELQFASFnfdGAHEQLLPPLIC-------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 301 ysspltlsdqsskikkgskGDCTVLKP-TLMAAVPEIMDRIYKNVMSKVQemnyiqktlFKIGYDYKLeqikkgydaplc 379
Cdd:cd17649 160 -------------------GACVVLRPdELWASADELAEMVRELGVTVLD---------LPPAYLQQL------------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 380 nLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLicc 454
Cdd:cd17649 200 -AEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLF-NAYGPTEATVTPLVWKCEAGAARAgasmpIGRPL--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 455 eiklkdwqeGGYT--INDK------PNPRGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGC 523
Cdd:cd17649 275 ---------GGRSayILDAdlnpvpVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgAPGSRLYRTGDLARWRDDGV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 524 LQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS--YVISFVVPNQkrltllaqqkgvegtwvdicnn 601
Cdd:cd17649 346 IEYLGRVDHQVKIR-GFRIELGEIEAALLEHPGVREAAVVALDGAGgkQLVAYVVLRA---------------------- 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 602 PAMEAEILKEIReAANAMKLERFEIPIK-VRLSPEPWTPETglvtdafKLKRKELR 656
Cdd:cd17649 403 AAAQPELRAQLR-TALRASLPDYMVPAHlVFLARLPLTPNG-------KLDRKALP 450
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
228-534 |
1.23e-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: 80.22 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcriGYSSPLTl 307
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE-WKTKDRILSWMPLTHDMGLIA-----------FHLAPLI- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 308 sdqsskikkgsKGDCTVLKPTLMAAVPEImdriykNVMSKVQEMNYIQKTLFKIGYDYKLEQIK--KGYDAPLcnlllfk 385
Cdd:cd05908 172 -----------AGMNQYLMPTRLFIRRPI------LWLKKASEHKATIVSSPNFGYKYFLKTLKpeKANDWDL------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 386 kvkallgGNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQG-----YGLTE-SCGA---------------------GTVT 437
Cdd:cd05908 228 -------SSIRMILNGAEPIDYElCHEFLDHMSKYGLKRNailpvYGLAEaSVGAslpkaqspfktitlgrrhvthGEPE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 438 EVTD------YTTGRVGAPLICCEIKLKDWQ----EGGYTindkpnprGEIVIGGQNISMGYFKNEEKTAEDYSVDEngq 507
Cdd:cd05908 301 PEVDkkdsecLTFVEVGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEATAKVFTDDG--- 369
|
330 340
....*....|....*....|....*..
gi 4758332 508 rWFCTGDIGeFHPDGCLQIIDRKKDLV 534
Cdd:cd05908 370 -WLKTGDLG-FIRNGRLVITGREKDII 394
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
236-656 |
3.72e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 78.73 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 236 YTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHvleltAEISCFTYGCRIGYSSPLTLSDQSSKIK 315
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYL-MALSNALIWGMNEGAVYLWTLPMFH-----CNGWCFTWTLAALCGTNICLRQVTAKAI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 316 KGSKGDCTVlkpTLMAAVPEIMDRIyknVMSKVQEmnyiqkTLFkigydykleqikkgydaPLCNLllfkkvkallggnV 395
Cdd:PLN02479 276 YSAIANYGV---THFCAAPVVLNTI---VNAPKSE------TIL-----------------PLPRV-------------V 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 396 RMMLSGGAP-------LSPQTHRfmnvcfccpIGQGYGLTESCGAGTV-----------TEVTDYTTGRVGAPLICCE-I 456
Cdd:PLN02479 314 HVMTAGAAPppsvlfaMSEKGFR---------VTHTYGLSETYGPSTVcawkpewdslpPEEQARLNARQGVRYIGLEgL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 457 KLKDWQEGgytindKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKK 531
Cdd:PLN02479 385 DVVDTKTM------KPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF---ANG--WFHSGDLGVKHPDGYIEIKDRSK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 532 DLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS---FVVPNQKrltllaqqkgvegtwVDICNNPAMEAEI 608
Cdd:PLN02479 454 DII-ISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESpcaFVTLKPG---------------VDKSDEAALAEDI 517
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 4758332 609 LKEIREaanamKLERFEIPIKVRLSPEPWTPeTGlvtdafKLKRKELR 656
Cdd:PLN02479 518 MKFCRE-----RLPAYWVPKSVVFGPLPKTA-TG------KIQKHVLR 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-578 |
3.94e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.82 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLESklktalLDISCVKHIIYVDNKAINKAEYPEgfeihsmqsveelgSNPENlgippsRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12467 1680 HLQAR------LPLPDGLRSLVLDQEDDWLEGYSD--------------SNPAV------NLAPQNLAYVIYTSGSTGRP 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaEISCFtygcriGYSSPLTlsdqsskikkgsKGDCTV 324
Cdd:PRK12467 1734 KGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAF------DVSVW------ELFWPLI------------NGARLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LKPTLMAAVPE-IMDRIYKN-VMSKVQEMNYIQktlfkigydyKLEQIKKGYDAPLcnlllfkkvkallggNVRMMLSGG 402
Cdd:PRK12467 1789 IAPPGAHRDPEqLIQLIERQqVTTLHFVPSMLQ----------QLLQMDEQVEHPL---------------SLRRVVCGG 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 403 APLSPQTHR-FMNVCFCCPIGQGYGLTEscgagTVTEVTDYT------TGRVGAPLiccEIKLKDWqeGGYTINDKPNPR 475
Cdd:PRK12467 1844 EALEVEALRpWLERLPDTGLFNLYGPTE-----TAVDVTHWTcrrkdlEGRDSVPI---GQPIANL--STYILDASLNPV 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 476 -----GEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 547
Cdd:PRK12467 1914 pigvaGELYLGGVGLARGYLNRPALTAERFVADpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEI 1992
|
490 500 510
....*....|....*....|....*....|...
gi 4758332 548 EAALKNCPLIDNICAFAK--SDQSYVISFVVPN 578
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQdgANGKQLVAYVVPT 2025
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
222-551 |
2.38e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.80 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltaeiscftYGCRIGY 301
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW-QWTADDVLVHGLPLFHV-----------HGLVLGV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 302 SSPLTLSDQSSKIKKGSK---GDCTVLKPTLMAAVPEIMDRIYKNVmskvqemnyiqktlfkigydykleqikkgyDAPl 378
Cdd:PRK07787 189 LGPLRIGNRFVHTGRPTPeayAQALSEGGTLYFGVPTVWSRIAADP------------------------------EAA- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 379 cnlllfkkvKALlgGNVRMMLSGGAPLS-PQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIK 457
Cdd:PRK07787 238 ---------RAL--RGARLLVSGSAALPvPVFDRLAALTGHRPV-ERYGMTETLITLSTRADGERRPGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 458 LKDwqEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKK-DLVKl 536
Cdd:PRK07787 306 LVD--EDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAA--AFTADG--WFRTGDVAVVDPDGMHRIVGREStDLIK- 378
|
330
....*....|....*.
gi 4758332 537 qAGEY-VSLGKVEAAL 551
Cdd:PRK07787 379 -SGGYrIGAGEIETAL 393
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
228-569 |
2.46e-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: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTaeISCFT---YGCRIG-YSS 303
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFGLT--VGLFTpllTGAEVFlYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 304 PL-------TLSDQsskikkgskgDCTVL--KPTLMAavpeimdriyknvmskvqemNYIQktlFKIGYDYkleqikkgy 374
Cdd:PRK08043 441 PLhyrivpeLVYDR----------NCTVLfgTSTFLG--------------------NYAR---FANPYDF--------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 375 daplcnlllfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-----------SCGAGTVTEVTDYT 443
Cdd:PRK08043 479 ------------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEcapvvsinvpmAAKPGTVGRILPGM 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 444 TGRVgaplicceIKLKDWQEGgytindkpnprGEIVIGGQNISMGYFKNEE------KTAEdysvDENGQR---WFCTGD 514
Cdd:PRK08043 541 DARL--------LSVPGIEQG-----------GRLQLKGPNIMNGYLRVEKpgvlevPTAE----NARGEMergWYDTGD 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 515 IGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEA-ALKNCPLIDNiCAFAKSDQS 569
Cdd:PRK08043 598 IVRFDEQGFVQIQGRAKRFAKI-AGEMVSLEMVEQlALGVSPDKQH-ATAIKSDAS 651
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-589 |
2.59e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLEsklktallDISCvkhiiyvdnkainkaeyPEGFEIHSMQSVEELGSNPEnlGIPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 2109 HLLE--------RLPL-----------------PAGVARLPLDRDAEWADYPD--TAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTlsdqsskikkgsKGDCTV 324
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS--FDGAHE-QWFH---------PLL------------NGARVL 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LKPTLMAAVPEIMDRIYKNVMSKVqemnyiqktlfkigydykleqikkgyDAPLCNLLLFKKVKALLGG--NVRMMLSGG 402
Cdd:PRK12316 2217 IRDDELWDPEQLYDEMERHGVTIL--------------------------DFPPVYLQQLAEHAERDGRppAVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 403 ----APLSPQTHRFMNVCFccpIGQGYGLTEscgagTVTEVTDYTTGRV---GAPLICCEIKLKDwqEGGYTINDKPNP- 474
Cdd:PRK12316 2271 eavpAASLRLAWEALRPVY---LFNGYGPTE-----AVVTPLLWKCRPQdpcGAAYVPIGRALGN--RRAYILDADLNLl 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 475 ----RGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 547
Cdd:PRK12316 2341 apgmAGELYLGGEGLARGYLNRPGLTAERFVPDpfsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR-GFRIELGEI 2419
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 4758332 548 EAALKNCPLIDNICAFAKSDQS--YVISFVVPNQKRLTLLAQQK 589
Cdd:PRK12316 2420 EARLQAHPAVREAVVVAQDGASgkQLVAYVVPDDAAEDLLAELR 2463
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-656 |
2.87e-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: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 89 EVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVelle 168
Cdd:cd05971 11 ELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 169 sklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptPSDMAIVMYTSGSTGRPKGVM 248
Cdd:cd05971 87 -----------------------------------------------------------SDDPALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 249 MHHSNLIaGMTGQCERIPGLGPKDTYIGYLPlahvleltAEISCftygcrIGysspltlsdqsskikkgskGDCTVLKPT 328
Cdd:cd05971 108 HAHRVLL-GHLPGVQFPFNLFPRDGDLYWTP--------ADWAW------IG-------------------GLLDVLLPS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 329 LMAAVPEIMDRIYKnvmskvqemnYIQKTLFKIGYDYKLEQIKkgydAPLCNLLLFKKVKALL---GGNVRMMLSGGAPL 405
Cdd:cd05971 154 LYFGVPVLAHRMTK----------FDPKAALDLMSRYGVTTAF----LPPTALKMMRQQGEQLkhaQVKLRAIATGGESL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 406 SPQTHRFMNVCFCCPIGQGYGLTEsCGA--GTVTEVTDYTTGRVGAPLICCEIKLkdwqeggytINDK-----PNPRGEI 478
Cdd:cd05971 220 GEELLGWAREQFGVEVNEFYGQTE-CNLviGNCSALFPIKPGSMGKPIPGHRVAI---------VDDNgtplpPGEVGEI 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 479 VIGGQNISM--GYFKNEEKTAEDYSVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPL 556
Cdd:cd05971 290 AVELPDPVAflGYWNNPSATEKKMAGD-----WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPA 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 557 IDNICAFAKSDQ---SYVISFVVPNQkrltllaqqkGVEGTwvdicnnpameAEILKEIREAANAmKLERFEIPIKVRLS 633
Cdd:cd05971 364 VLMAAVVGIPDPirgEIVKAFVVLNP----------GETPS-----------DALAREIQELVKT-RLAAHEYPREIEFV 421
|
570 580
....*....|....*....|...
gi 4758332 634 PEPWTPETGlvtdafKLKRKELR 656
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) ... |
85-577 |
3.37e-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: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 164
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ellesklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsrpTPSDMAIVMYTSGSTGRP 244
Cdd:cd17652 91 --------------------------------------------------------------TPDNLAYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAeisCFTYGCR--IGYSSPLTLSDQSSKIKKGSK 319
Cdd:cd17652 109 KGVVVTHRGLANLAAAQIAAF-DVGPGSRVLQFASPsfdASVWELLM---ALLAGATlvLAPAEELLPGEPLADLLREHR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 320 GDCTVLKPTLMAAVPEimdriyknvmskvqemnyiqktlfkigydykleqikkgydaplcnlllfkkvKALLGGnvRMML 399
Cdd:cd17652 185 ITHVTLPPAALAALPP----------------------------------------------------DDLPDL--RTLV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 400 SGGAPLSPQ-------THRFMNvcfccpigqGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIK-LKDWQEggytind 470
Cdd:cd17652 211 VAGEACPAElvdrwapGRRMIN---------AYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYvLDARLR------- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 471 kPNP---RGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 544
Cdd:cd17652 275 -PVPpgvPGELYIAGAGLARGYLNRPGLTAERFVADpfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIR-GFRIEL 352
|
490 500 510
....*....|....*....|....*....|....*.
gi 4758332 545 GKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP 577
Cdd:cd17652 353 GEVEAALTEHPGVAEAVVVVRDDRPGDkrlVAYVVP 388
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
87-567 |
3.58e-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: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 166
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 LEsklktalldiscvkhiiyvdnkainkaeypegfeihsmqsveelgsnpenlgippsRPTPSDMAIVMYTSGSTGRPKG 246
Cdd:cd05969 83 YE--------------------------------------------------------RTDPEDPTLLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VMMHHSNLIA-GMTGQceRIPGLGPKDTYIgylplahvleLTAEISCFTyGCRIGYSSPLTLSdqsskikkgskgdCTVL 325
Cdd:cd05969 107 VLHVHDAMIFyYFTGK--YVLDLHPDDIYW----------CTADPGWVT-GTVYGIWAPWLNG-------------VTNV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 326 kptlmaavpeimdriyknvmskVQEMNYIQKTLFKIGYDYKleqIKKGYDAPLCNLLLFKKVKALLG----GNVRMMLSG 401
Cdd:cd05969 161 ----------------------VYEGRFDAESWYGIIERVK---VTVWYTAPTAIRMLMKEGDELARkydlSSLRFIHSV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 402 GAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIKLKDwQEGGYTindKPNPRGEIVI 480
Cdd:cd05969 216 GEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVD-ENGNEL---PPGTKGILAL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 481 GGQNISM--GYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLID 558
Cdd:cd05969 292 KPGWPSMfrGIWNDEERYKNSF---IDG--WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAVA 365
|
....*....
gi 4758332 559 NICAFAKSD 567
Cdd:cd05969 366 EAGVIGKPD 374
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-590 |
5.61e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.97 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLESklktalLDISCVKHIIYVDNKAINKaeYPEgfeihsmqsveelgSNPENlgippsRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12467 3201 HLLEQ------LPAPAGDTALTLDRLDLNG--YSE--------------NNPST------RVMGENLAYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 245 KGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAhvLELTAEISCFTYGCrigysspltlsdqsskikkgskGDCTV 324
Cdd:PRK12467 3253 KGVGVRHGAL-ANHLCWIAEAYELDANDRVLLFMSFS--FDGAQERFLWTLIC----------------------GGCLV 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 325 LKPTLMAAvPEimdriyknvmSKVQEMNYiqktlfkigydyklEQIKKGYDAP--LCNLLLFKKVKAllGGNVRMMLSGG 402
Cdd:PRK12467 3308 VRDNDLWD-PE----------ELWQAIHA--------------HRISIACFPPayLQQFAEDAGGAD--CASLDIYVFGG 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 403 APLSPQT-----HRFMNVCfccpIGQGYGLTEscgagTVTEVTDYTTGRVGAP-LICCEIKLKDWQEGGYTINDKPNP-- 474
Cdd:PRK12467 3361 EAVPPAAfeqvkRKLKPRG----LTNGYGPTE-----AVVTVTLWKCGGDAVCeAPYAPIGRPVAGRSIYVLDGQLNPvp 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 475 ---RGEIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 548
Cdd:PRK12467 3432 vgvAGELYIGGVGLARGYHQRPSLTAERFVADpfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIE 3510
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 4758332 549 AALKNCPLIDNICAFAKSDQS--YVISFVVPNQKRLTLLAQQKG 590
Cdd:PRK12467 3511 ARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQGDWRETLRD 3554
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
228-577 |
6.04e-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: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIagmtGQCEripglgpkdtyigylplahvleltAEISCFTygcrigysspLTL 307
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCE------------------------WHRPYFG----------VTP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 308 SDQSSKIKkGSKGDCTVLK--PTLMA-AVPEIMDRIYKNVMSKVQEmnYIQKTLFKIGYdykleqikkgYDAPLCnlllf 384
Cdd:cd17645 145 ADKSLVYA-SFSFDASAWEifPHLTAgAALHVVPSERRLDLDALND--YFNQEGITISF----------LPTGAA----- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 385 KKVKALLGGNVRMMLSGGAPLSpqthRFMNVCFccPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIklkdwqe 463
Cdd:cd17645 207 EQFMQLDNQSLRVLLTGGDKLK----KIERKGY--KLVNNYGPTENTVVATSFEIdKPYANIPIGKPIDNTRV------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 464 ggYTIND----KP-NPRGEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 536
Cdd:cd17645 274 --YILDEalqlQPiGVAGELCIAGEGLARGYLNRPELTAEKFIVHpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 4758332 537 QaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVP 577
Cdd:cd17645 352 R-GYRIEPGEIEPFLMNHPLIELAAVLAKEDadgRKYLVAYVTA 394
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
209-570 |
9.82e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 74.43 E-value: 9.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 209 VEELGSNPENLGIPPSRPtpsdmAIVMYTSGSTGRPKGVMMHHSNLiAGMTGQCERIPGLGPKDTyIGYL--PLAHVLEL 286
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSP-----ALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADINSD-VGFVgvPLFHIAGI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 287 TAEISCFTYGCRigysspltlsdqsskikkgskgdcTVLKPTLMAAVPEIMDriyknvmskVQEMNYIQkTLFKIGYDYK 366
Cdd:PRK07786 232 GSMLPGLLLGAP------------------------TVIYPLGAFDPGQLLD---------VLEAEKVT-GIFLVPAQWQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 367 L---EQIKKGYDAPLcnlllfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFccPIGQ---GYGLTEscgAGTVTEVT 440
Cdd:PRK07786 278 AvcaEQQARPRDLAL-----------------RVLSWGAAPASDTLLRQMAATF--PEAQilaAFGQTE---MSPVTCML 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 441 D-----YTTGRVGAPLICCEIKLKDwqeggYTIND-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGD 514
Cdd:PRK07786 336 LgedaiRKLGSVGKVIPTVAARVVD-----ENMNDvPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---AGG--WFHSGD 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 515 IGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY 570
Cdd:PRK07786 406 LVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW 460
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
221-551 |
2.82e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 72.74 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 221 IPPSRPTPSDMAIVM------------YTSGSTGRPKGVMMHH--------SNLIAGMTGQCEripglgpkdTYIGYLPL 280
Cdd:PLN03102 166 IQRGEPTPSLVARMFriqdehdpislnYTSGTTADPKGVVISHrgaylstlSAIIGWEMGTCP---------VYLWTLPM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 281 AHVLELTaeiscFTYGCrigysspltlsdqsskikkGSKGDCTVLKPTLMAavPEImdriYKNV-MSKVQEMNYIqKTLF 359
Cdd:PLN03102 237 FHCNGWT-----FTWGT-------------------AARGGTSVCMRHVTA--PEI----YKNIeMHNVTHMCCV-PTVF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 360 KIgydykleqIKKGYDAPLCNLllfkkvkallGGNVRMMLSGGAPLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEV 439
Cdd:PLN03102 286 NI--------LLKGNSLDLSPR----------SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEW 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 440 TD-----------YTTGRVGAP-LICCEIKLKDwqeggyTINDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYSv 502
Cdd:PLN03102 346 QDewnrlpenqqmELKARQGVSiLGLADVDVKN------KETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAFK- 418
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 4758332 503 dengQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAAL 551
Cdd:PLN03102 419 ----HGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVL 462
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
229-576 |
5.92e-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: 70.75 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLE-------LTAEISCFTYGCRIGY 301
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiltcLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 302 SSPLtlsdqssKIKKGSKGDCTVLKPTLMAAVPEImdriYKNVMSKVQEMNYIQktlfkIGYDYKLEQikkgydaplcnl 381
Cdd:cd17635 81 KSLF-------KILTTNAVTTTCLVPTLLSKLVSE----LKSANATVPSLRLIG-----YGGSRAIAA------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 382 llfKKVKALLGGNVRmmlsggaplspqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKD 460
Cdd:cd17635 133 ---DVRFIEATGLTN------------------------TAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 461 wQEGGYTINDKpnpRGEIVIGGQNISMGYFKNEEKTAEDYsVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 540
Cdd:cd17635 186 -TDGIAGPSAS---FGTIWIKSPANMLGYWNNPERTAEVL-IDG----WVNTGDLGERREDGFLFITGRSSESI-NCGGV 255
|
330 340 350
....*....|....*....|....*....|....*....
gi 4758332 541 YVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 576
Cdd:cd17635 256 KIAPDEVERIAEGVSGVQECACYEISDEEFgelVGLAVV 294
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
227-618 |
9.09e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 71.23 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNL---IAGMTGQCERIPGLGPKDtYIGYLPLAHvleltaeiscfTYGCRIGYSs 303
Cdd:PRK12582 218 TPDTVAKYLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPV-SLDWMPWNH-----------TMGGNANFN- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 304 PLTLSDQSSKIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyiqktlfKIGYDYKLEQIKKgyDAP 377
Cdd:PRK12582 285 GLLWGGGTLYIDDG--------KPlpgmfeETIRNLREISPTVYGNV---------------PAGYAMLAEAMEK--DDA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 378 LCNLLlFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQ------GYGLTEScgAGTVTEVTDYT--TGRVGA 449
Cdd:PRK12582 340 LRRSF-FK--------NLRLMAYGGATLSDDLYERMQALAVRTTGHripfytGYGATET--APTTTGTHWDTerVGLIGL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 450 PLICCEIKLKdwqeggytindkpnPRG---EIVIGGQNISMGYFKNEEKTAEDYsvDENGqrWFCTGDIGEF-HPDGCLQ 525
Cdd:PRK12582 409 PLPGVELKLA--------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAF--DEEG--FYRLGDAARFvDPDDPEK 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 526 --IID-RKKDLVKLQAGEYVSLGKVEA-ALKNC-PLIDNIcAFAKSDQSYVISFVVPNQKRLTLLAqqKGVEGTWVDICN 600
Cdd:PRK12582 471 glIFDgRVAEDFKLSTGTWVSVGTLRPdAVAACsPVIHDA-VVAGQDRAFIGLLAWPNPAACRQLA--GDPDAAPEDVVK 547
|
410
....*....|....*...
gi 4758332 601 NPAMeAEILKEIREAANA 618
Cdd:PRK12582 548 HPAV-LAILREGLSAHNA 564
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
87-256 |
9.11e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 71.08 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKyNFPLVT-LYATLGKEAVVHGLNESEASYLITSVE 165
Cdd:PRK04319 76 YKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALK-NGAIVGpLFEAFMEEAVRDRLEDSEAKVLITTPA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 166 LLESKLKTallDISCVKHIIYVDNKAinkaEYPEGFeihsMQSVEELGSNPENLGIPPSrpTPSDMAIVMYTSGSTGRPK 245
Cdd:PRK04319 155 LLERKPAD---DLPSLKHVLLVGEDV----EEGPGT----LDFNALMEQASDEFDIEWT--DREDGAILHYTSGSTGKPK 221
|
170
....*....|.
gi 4758332 246 GVMMHHSNLIA 256
Cdd:PRK04319 222 GVLHVHNAMLQ 232
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-567 |
1.29e-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: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVL-ELTAEISCFTYGCRIGYSSPLT 306
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVY-NAWMLALNSLFDPDDVLLCGLPLFHVNgSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LSDqsskikKGSKGDCTVL----KPTLMAAVPEIMDriyknvmskvqemnyiqktlfkigydyKLEQIKKGYDAplcnll 382
Cdd:cd05944 80 YRN------PGLFDNFWKLveryRITSLSTVPTVYA---------------------------ALLQVPVNADI------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 383 lfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-SCGAGTVTEVTDYTTGRVGAPLICCEIKLKDW 461
Cdd:cd05944 121 ----------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 462 QEGGYTIND-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 540
Cdd:cd05944 191 DGVGRLLRDcAPDEVGEICVAGPGVFGGYLYTEGNKNAFV-----ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGH 264
|
330 340
....*....|....*....|....*..
gi 4758332 541 YVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:cd05944 265 NIDPALIEEALLRHPAVAFAGAVGQPD 291
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
103-567 |
1.71e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 70.37 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 103 ALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGKEAVV-------------HGLNESEASYLITSVELLEs 169
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAY-------------YAILRANAVVvpvnpmnreeelaHYVTDSGARVAIVGSELAP- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 170 KLKTALLDIScVKHII------YVDNKAINKAeyPEGFEI-HSMQSVEELGSNP------ENLGIPPSRPTPSDMAIVMY 236
Cdd:PRK08314 121 KVAPAVGNLR-LRHVIvaqysdYLPAEPEIAV--PAWLRAePPLQALAPGGVVAwkealaAGLAPPPHTAGPDDLAVLPY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 237 TSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLeltaeiscftyGCRIGYSSPLTLsdqsskikk 316
Cdd:PRK08314 198 TSGTTGVPKGCMHTHRTVMANAVGSV-LWSNSTPESVVLAVLPLFHVT-----------GMVHSMNAPIYA--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 317 gskGDCTVLKPTL-MAAVPEIMDRiyknvmSKVQEMNYIQKTLFKIGYDYKLEQikkgYDapLCNLllfkkvkALLGGnv 395
Cdd:PRK08314 257 ---GATVVLMPRWdREAAARLIER------YRVTHWTNIPTMVVDFLASPGLAE----RD--LSSL-------RYIGG-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 396 rmmlsGGAPLsPQT-----HRFMNVCFCcpigQGYGLTEScGAGTVTEVTDYTTGR-VGAPLICCEIKLKDWQEGgytIN 469
Cdd:PRK08314 313 -----GGAAM-PEAvaerlKELTGLDYV----EGYGLTET-MAQTHSNPPDRPKLQcLGIPTFGVDARVIDPETL---EE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 470 DKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEA 549
Cdd:PRK08314 379 LPPGEVGEIVVHGPQVFKGYWNRPEATAEAF-IEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVEN 456
|
490
....*....|....*...
gi 4758332 550 ALKNCPLIDNICAFAKSD 567
Cdd:PRK08314 457 LLYKHPAIQEACVIATPD 474
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
85-586 |
2.05e-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: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYN-FPLVTLYatlgkeavvhGLNESEASYLITS 163
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGaVPVLALP----------SHRRSELSAFCAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 164 VELlesklktalldiscvkhiiyvdnKAINKAEYPEGFEiHSMQSVEELGSNPenlgippsrptpsDMAIVMYTSGSTGR 243
Cdd:cd05920 111 AEA-----------------------VAYIVPDRHAGFD-HRALARELAESIP-------------EVALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 244 PKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTAE--ISCFTYGCRIGYSSPltlsdqsskikkGSKGD 321
Cdd:cd05920 154 PKLIPRTHNDYAYNVR-ASAEVCGLDQDTVYLAVLPAAHNFPLACPgvLGTLLAGGRVVLAPD------------PSPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 322 CTVL----KPTLMAAVPEImdriyknVMSKVQEmnyiqktlfkigydykleqiKKGYDAPLCNLllfkkvkallggnvRM 397
Cdd:cd05920 221 AFPLiereGVTVTALVPAL-------VSLWLDA--------------------AASRRADLSSL--------------RL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 398 MLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTVT--------EVTDYTTGRVGAPLIccEIKLKDwQEGgytiN 469
Cdd:cd05920 260 LQVGGARLSPALARRVPPVLGCTLQQVFGMAE----GLLNytrlddpdEVIIHTQGRPMSPDD--EIRVVD-EEG----N 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 470 D-KPNPRGEIVIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 548
Cdd:cd05920 329 PvPPGEEGELLTRGPYTIRGYYRAPEHNAR--AFTPDG--FYRTGDLVRRTPDGYLVVEGRIKDQIN-RGGEKIAAEEVE 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 4758332 549 AALKNCPLIDNICAFAKSDQSY---VISFVVPNQKRLTLLA 586
Cdd:cd05920 404 NLLLRHPAVHDAAVVAMPDELLgerSCAFVVLRDPPPSAAQ 444
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
425-579 |
5.78e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.38 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 425 YGLTESCGAGTVTEVTD-----YTTGRVGAPLICCEIKLKDwqEGGytiNDKPNP-RGEIVIGGQNISMGYFKNEEKTAE 498
Cdd:PRK04813 293 YGPTEATVAVTSIEITDemldqYKRLPIGYAKPDSPLLIID--EEG---TKLPDGeQGEIVISGPSVSKGYLNNPEKTAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 499 DYsVDENGQRWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFV 575
Cdd:PRK04813 368 AF-FTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVESAVVVPYNKDHkvqYLIAYV 444
|
....
gi 4758332 576 VPNQ 579
Cdd:PRK04813 445 VPKE 448
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
230-577 |
6.01e-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: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAhvleltaeiscFTYGCRIGYSSPLtlsd 309
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLA-----------FTFGLGGVLLFPF---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 310 qsskikkgSKGDCTVLKPtlmAAVPEimdriykNVMSKVQEmnYIQKTLFKIGYDYKLEQIKKGYDAPLcnlllfkkvka 389
Cdd:cd05958 163 --------GVGASGVLLE---EATPD-------LLLSAIAR--YKPTVLFTAPTAYRAMLAHPDAAGPD----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 390 llGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytin 469
Cdd:cd05958 212 --LSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEG----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 470 dKPNPRGEI---VIGGQNismGYFKNEEKTAEDYSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGK 546
Cdd:cd05958 284 -NPVPDGTIgrlAVRGPT---GCRYLADKRQRTYVQGG----WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPE 354
|
330 340 350
....*....|....*....|....*....|....
gi 4758332 547 VEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESrgvVVKAFVVL 388
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
220-592 |
6.13e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.22 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 220 GIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcri 299
Cdd:PRK06814 784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLTG----------- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 300 GYSSPLtlsdqSSKIKkgskgdcTVLKPTLM--AAVPEImdrIYKnvmskvqemnyIQKTLFkIGYDYKLeqikKGYdAP 377
Cdd:PRK06814 852 GLVLPL-----LSGVK-------VFLYPSPLhyRIIPEL---IYD-----------TNATIL-FGTDTFL----NGY-AR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 378 LCNLLLFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTES-----------CGAGTVtevtdyttGR 446
Cdd:PRK06814 900 YAHPYDFR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapvialntpmhNKAGTV--------GR 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 447 VgAPLIccEIKLKDwQEGgytINDKpnprGEIVIGGQNISMGYFKNEEKTAedYSVDENGqrWFCTGDIGEFHPDGCLQI 526
Cdd:PRK06814 964 L-LPGI--EYRLEP-VPG---IDEG----GRLFVRGPNVMLGYLRAENPGV--LEPPADG--WYDTGDIVTIDEEGFITI 1028
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758332 527 IDRKKDLVKLqAGEYVSLGKVEAAlkncplidnICAFAKSDQSYVISfvVPNQK---RLTLLAQQKGVE 592
Cdd:PRK06814 1029 KGRAKRFAKI-AGEMISLAAVEEL---------AAELWPDALHAAVS--IPDARkgeRIILLTTASDAT 1085
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
31-578 |
1.07e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 67.79 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 31 DIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMqpngkvfkklilgNYKWMNYlEVNRRVNNFGSgltaLGLKPKN 110
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVYGHKTALIFESSGGVVRRY-------------SYLELNE-EINRTANLFYS----LGIRKGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 111 TIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDnk 190
Cdd:PRK08008 64 KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 191 ainkAEYPEGFEIHSMQsvEELGSNPENLG-IPPSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-AGMTG--QCerip 266
Cdd:PRK08008 142 ----VALPADDGVSSFT--QLKAQQPATLCyAPPL--STDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSawQC---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 267 GLGPKDTYIGYLPLAHV-LELTAEISCFTYGCRI----GYSSPlTLSDQSSKIKkgskgdctvlkptlmAAVPEIMDRIY 341
Cdd:PRK08008 210 ALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFvlleKYSAR-AFWGQVCKYR---------------ATITECIPMMI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 342 KNVMSKVQEMNYIQKTLFKIGYDYKL-EQIKKGYDAPLcnlllfkkvkallggNVRMMLSggaplspqthrfmnvcfccp 420
Cdd:PRK08008 274 RTLMVQPPSANDRQHCLREVMFYLNLsDQEKDAFEERF---------------GVRLLTS-------------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 421 igqgYGLTEScgagTVTEVTDYTTGR-----VGAPLICCEIKLKDwqEGGYTIndKPNPRGEIVIG---GQNISMGYFKN 492
Cdd:PRK08008 319 ----YGMTET----IVGIIGDRPGDKrrwpsIGRPGFCYEAEIRD--DHNRPL--PAGEIGEICIKgvpGKTIFKEYYLD 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 493 EEKTAEdySVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QS 569
Cdd:PRK08008 387 PKATAK--VLEADG--WLHTGDTGYVDEEGFFYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVGIKDsirDE 461
|
....*....
gi 4758332 570 YVISFVVPN 578
Cdd:PRK08008 462 AIKAFVVLN 470
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
87-665 |
1.32e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 67.24 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 166
Cdd:PRK08276 14 YGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 LESkLKTALLDISCVKHIIYVDnkainkAEYPEGFEIHSmqsvEELGSNPENLgiPPSRPTPSDMAivmYTSGSTGRPKG 246
Cdd:PRK08276 94 ADT-AAELAAELPAGVPLLLVV------AGPVPGFRSYE----EALAAQPDTP--IADETAGADML---YSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VM-----MHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrigySSPLTLSDQSSKIkkgskGD 321
Cdd:PRK08276 158 IKrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH-------------------TAPLRFGMSALAL-----GG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 322 CTVLkptlmaavpeiMDRiyknvMSKVQEMNYIQKtlFKIGYDY----------KL-EQIKKGYDaplcnlllfkkVKAL 390
Cdd:PRK08276 214 TVVV-----------MEK-----FDAEEALALIER--YRVTHSQlvptmfvrmlKLpEEVRARYD-----------VSSL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 391 lggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDYTT--GRVGAPLIcCEIKLKDwqeggytI 468
Cdd:PRK08276 265 -----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGV-TVITSEDWLAhpGSVGKAVL-GEVRILD-------E 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 469 NDKPNPRGEI-----VIGGQNISmgYFKNEEKTAEDYsvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVklqageyVS 543
Cdd:PRK08276 331 DGNELPPGEIgtvyfEMDGYPFE--YHNDPEKTAAAR----NPHGWVTVGDVGYLDEDGYLYLTDRKSDMI-------IS 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 544 LG------KVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQkrltllaqqkGVEGTwvdicnnPAMEAEILKEIRE 614
Cdd:PRK08276 398 GGvniypqEIENLLVTHPKVADVAVFGVPDEEMgerVKAVVQPAD----------GADAG-------DALAAELIAWLRG 460
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 4758332 615 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHYLKDIER 665
Cdd:PRK08276 461 -----RLAHYKCPRSIDFEDElPRTP-TG------KLYKRRLRDRYWEGRQR 500
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
86-661 |
2.07e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.56 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 86 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRA---EWMIAAQTCFKYnFPLVTLYATLGKEAVVhgLNESEASYLIT 162
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAAYI--VDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 163 SVELLESkLKTALLDISCVKHIIYVDNKAINkaeypEGFEIHSmQSVEELGSNPEnlgipPSRPTPSDMaivMYTSGSTG 242
Cdd:PRK13391 103 SAAKLDV-ARALLKQCPGVRHRLVLDGDGEL-----EGFVGYA-EAVAGLPATPI-----ADESLGTDM---LYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 243 RPKGVM--MHHSNLIA--GMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrigySSPLTLSdqSSKIKKGS 318
Cdd:PRK13391 168 RPKGIKrpLPEQPPDTplPLTAFLQRLWGFRSDMVYLSPAPLYH-------------------SAPQRAV--MLVIRLGG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 319 kgdcTVLkptlmaavpeIMDRiyknvMSKVQEMNYIQKtlFKIGYD----------YKL-EQIKKGYDaplcnlllfkkV 387
Cdd:PRK13391 227 ----TVI----------VMEH-----FDAEQYLALIEE--YGVTHTqlvptmfsrmLKLpEEVRDKYD-----------L 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 388 KALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDY-----TTGRV--GAPLICceiklkd 460
Cdd:PRK13391 275 SSL-----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGF-TACDSEEWlahpgTVGRAmfGDLHIL------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 461 wQEGGytindKPNPRGEIvigGQ-----NISMGYFKNEEKTAEDYSVDENgqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 535
Cdd:PRK13391 342 -DDDG-----AELPPGEP---GTiwfegGRPFEYLNDPAKTAEARHPDGT---WSTVGDIGYVDEDGYLYLTDRAAFMI- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 536 LQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKrltlLAQQ-KGVEGTWVDICNNPAMEAEILKEIRE 614
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNED----LGEEvKAVVQPVDGVDPGPALAAELIAFCRQ 473
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 4758332 615 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELRNHYLK 661
Cdd:PRK13391 474 -----RLSRQKCPRSIDFEDElPRLP-TG------KLYKRLLRDRYWG 509
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
87-282 |
3.22e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.97 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynFPLVTLYATLG-------KEAVVHGLNESEASY 159
Cdd:PRK08279 65 YAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAW-------LGLAKLGAVVAllntqqrGAVLAHSLNLVDAKH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 LITSVELLESkLKTALLDIScVKHIIYVDNKAINKAeyPEGF-EIHSMQSveelGSNPENlgiPPSRP--TPSDMAIVMY 236
Cdd:PRK08279 138 LIVGEELVEA-FEEARADLA-RPPRLWVAGGDTLDD--PEGYeDLAAAAA----GAPTTN---PASRSgvTAKDTAFYIY 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 4758332 237 TSGSTGRPKGVMMHHSNLI---AGMTGQCeripGLGPKDTYIGYLPLAH 282
Cdd:PRK08279 207 TSGTTGLPKAAVMSHMRWLkamGGFGGLL----RLTPDDVLYCCLPLYH 251
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
77-665 |
6.70e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 62.02 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 77 LILGNyKWMNYLEVNRRVNNFGSGLTALGLKP--------KNTIAIFCETRAEWMIAAqtcfkYNFPlVTLYATlgKEAV 148
Cdd:PRK12406 5 IISGD-RRRSFDELAQRAARAAGGLAALGVRPgdcvallmRNDFAFFEAAYAAMRLGA-----YAVP-VNWHFK--PEEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 149 VHGLNESEASYLITSVELLESkLKTALldiscvkhiiyvdnkainkaeyPEGFEIHSMQSVEELGSN----PENLGIP-- 222
Cdd:PRK12406 76 AYILEDSGARVLIAHADLLHG-LASAL----------------------PAGVTVLSVPTPPEIAAAyrisPALLTPPag 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 223 ----------------PSRPTPSDMaivMYTSGSTGRPKGVmmhhsnliagmtgqcERIPGLgPKDTyigylplAHVLEL 286
Cdd:PRK12406 133 aidwegwlaqqepydgPPVPQPQSM---IYTSGTTGHPKGV---------------RRAAPT-PEQA-------AAAEQM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 287 TAEISCFTYGCRIGYSSPLTLSDQSS-KIKKGSKGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYIQKTLFKIgydY 365
Cdd:PRK12406 187 RALIYGLKPGIRALLTGPLYHSAPNAyGLRAGRLGGVLVLQPRFDPE--ELLQLIERH---RITHMHMVPTMFIRL---L 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 366 KL-EQIKKGYDaplcnlllfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT--DY 442
Cdd:PRK12406 259 KLpEEVRAKYD-----------VSSL-----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTES---GAVTFATseDA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 443 TT--GRVGAPLICCEIKLKDwqeggytINDKPNPRGEI-----VIGGqNISMGYFKNEEKTAEdysVDENGqrWFCTGDI 515
Cdd:PRK12406 320 LShpGTVGKAAPGAELRFVD-------EDGRPLPQGEIgeiysRIAG-NPDFTYHNKPEKRAE---IDRGG--FITSGDV 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 516 GEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkrltllaqQKGVE 592
Cdd:PRK12406 387 GYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFgeaLMAVVEP----------QPGAT 455
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758332 593 gtwVDicnnpamEAEILKEIREAanamkLERFEIPIKVRLSPEpwTPEtglvTDAFKLKRKELRNHYLKDIER 665
Cdd:PRK12406 456 ---LD-------EADIRAQLKAR-----LAGYKVPKHIEIMAE--LPR----EDSGKIFKRRLRDPYWANAGR 507
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
236-543 |
7.00e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 236 YTSGSTGRPKGVMM-HHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVleltaeiscFTYGcrIGYSSPltlSDQSSKI 314
Cdd:PRK06018 184 YTSGTTGDPKGVLYsHRSNVLHALMANNGDALGTSAADTMLPVVPLFHA---------NSWG--IAFSAP---SMGTKLV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 315 KKGSKGDCTVL-------KPTLMAAVPEIMDRIyknvmskvqeMNYIQKTlfkigyDYKLEQIKK----GYDAPLCNLLL 383
Cdd:PRK06018 250 MPGAKLDGASVyelldteKVTFTAGVPTVWLML----------LQYMEKE------GLKLPHLKMvvcgGSAMPRSMIKA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 384 FKKvkalLGGNVRmmlsggaplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVT---DYTTG--------RVGAPLI 452
Cdd:PRK06018 314 FED----MGVEVR--------------------------HAWGMTEMSPLGTLAALKppfSKLPGdarldvlqKQGYPPF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 453 CCEIKLKDwQEGgytiNDKP---NPRGEIVIGGQNISMGYFKneektAEDYSVDENGqrWFCTGDIGEFHPDGCLQIIDR 529
Cdd:PRK06018 364 GVEMKITD-DAG----KELPwdgKTFGRLKVRGPAVAAAYYR-----VDGEILDDDG--FFDTGDVATIDAYGYMRITDR 431
|
330
....*....|....
gi 4758332 530 KKDLVKlQAGEYVS 543
Cdd:PRK06018 432 SKDVIK-SGGEWIS 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
206-541 |
7.62e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.84 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 206 MQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIpglgpKDTYigylplahvle 285
Cdd:PRK09274 151 GTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA----QIEAL-----REDY----------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 286 ltaeiscftygcrigysspltlsdqssKIKKGSKGDCT-----VLKPTL-MAAV-PEiMDriyknvMSKVQEMN--YIQK 356
Cdd:PRK09274 211 ---------------------------GIEPGEIDLPTfplfaLFGPALgMTSViPD-MD------PTRPATVDpaKLFA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 357 TLFKigydyklEQIKKGYDAP--LCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTH-RFMNVcfccpIGQG------YGL 427
Cdd:PRK09274 257 AIER-------YGVTNLFGSPalLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIeRFRAM-----LPPDaeiltpYGA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 428 TESCGAGTVT--EVTDYTTGR--------VGAPLICCEIKLKDwqeggytINDKPNPR------------GEIVIGGQNI 485
Cdd:PRK09274 325 TEALPISSIEsrEILFATRAAtdngagicVGRPVDGVEVRIIA-------ISDAPIPEwddalrlatgeiGEIVVAGPMV 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 486 SMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEY 541
Cdd:PRK09274 398 TRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
77-534 |
9.30e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 61.54 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 77 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAE-W--MIAAQTC-FKYnfplVTLYATLGKEAVVHGL 152
Cdd:PRK06188 31 LVLGDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLmaIGAAQLAgLRR----TALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 153 NESEASYLIT-SVELLESKLktALLD-ISCVKHIIYVDnkainkaEYPEGfeihsmqsvEELGSNPENLGIPPSRP--TP 228
Cdd:PRK06188 106 EDAGISTLIVdPAPFVERAL--ALLArVPSLKHVLTLG-------PVPDG---------VDLLAAAAKFGPAPLVAaaLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 229 SDMAIVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKDTYIGYLPLAHVleltaeiscftygcrigysspltls 308
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRS-IATMAQIQLAEWEWPADPRFLMCTPLSHA------------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 309 dqsskikkgskGDCTVLkPTLMAAVPEIMDRIYK--NVMSKVQEMNyIQKTLFKIGYDYKLEQIKKGYDAPLCNLllfkk 386
Cdd:PRK06188 222 -----------GGAFFL-PTLLRGGTVIVLAKFDpaEVLRAIEEQR-ITATFLVPTMIYALLDHPDLRTRDLSSL----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 387 vkallggnvRMMLSGGAPLSPQ-----THRFMNVcfccpIGQGYGLTESCGAGTVTEVTDYTTGRV------GAPLICCE 455
Cdd:PRK06188 284 ---------ETVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 456 IKLKDwqeggytINDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PRK06188 350 VALLD-------EDGREVAQgevGEICVRGPLVMDGYWNRPEETAEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKD 417
|
..
gi 4758332 533 LV 534
Cdd:PRK06188 418 MI 419
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
143-658 |
1.55e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.95 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 143 LGKEAVVHGLNESEASYLITSVELLEsKLKTALLDISCVKHIIYVDNKAINKAE--YPEGFEIHSMQSveELGSNPENLG 220
Cdd:PRK05620 98 LMNDQIVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIGPSDADSAAahMPEGIKVYSYEA--LLDGRSTVYD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 221 IPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcri 299
Cdd:PRK05620 175 WPELDET--TAAAICYSTGTTGAPKGVVYSHRSLyLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSG--- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 300 gysSPLTLSDQSskikkgskgdctVLKPTLMAAVPEIMDRIYKNVMSK-VQEMNYIQKTLFKigydykleqikkgydapl 378
Cdd:PRK05620 250 ---TPLVFPGPD------------LSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPPE------------------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 379 cnlllfkkvkallggnvRMML----SGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--------EVTD---YT 443
Cdd:PRK05620 297 -----------------RMSLqeiyVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVArppsgvsgEARWayrVS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 444 TGRVGAPLiccEIKLKDwqeGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTA-------EDYSVDENGQR-----WFC 511
Cdd:PRK05620 360 QGRFPASL---EYRIVN---DGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaastfRGEDVEDANDRftadgWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 512 TGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVslgkVEAALKNcplidNICAFAKSDQSYVISFvvPNQK------RLTLL 585
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIR-SGGEWI----YSAQLEN-----YIMAAPEVVECAVIGY--PDDKwgerplAVTVL 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758332 586 AQqkGVEGTwvdicnnpameAEILKEIREAAnamkleRFEIPikVRLSPEPWT-PETGLVTDAFKLKRKELRNH 658
Cdd:PRK05620 502 AP--GIEPT-----------RETAERLRDQL------RDRLP--NWMLPEYWTfVDEIDKTSVGKFDKKDLRQH 554
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
85-551 |
1.61e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 164
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 165 ELLEsklktallDISCVKHIIYVDNKAINKAEYPE---GFEIHsmqsveelGSNpenlgippsrptpsdMAIVMYTSGST 241
Cdd:PRK05691 1237 HLLE--------RLPQAEGVSAIALDSLHLDSWPSqapGLHLH--------GDN---------------LAYVIYTSGST 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 242 GRPKGVMMHHSNLIagmtgqcERIPGLgpKDTYIgyLPLAHVLELTAEIS-------CF---TYGCRIgysspltlsdqs 311
Cdd:PRK05691 1286 GQPKGVGNTHAALA-------ERLQWM--QATYA--LDDSDVLMQKAPISfdvsvweCFwplITGCRL------------ 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 312 skikkgskgdctvlkptLMAAVPEIMD--RIYKNVMSK-VQEMNYIQKTLfkigydyklEQIKKGYDAPLCNLLlfkkvk 388
Cdd:PRK05691 1343 -----------------VLAGPGEHRDpqRIAELVQQYgVTTLHFVPPLL---------QLFIDEPLAAACTSL------ 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 389 allggnvRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTEScgAGTVT----EVTDYTTGRVGAPL--ICCEIKLKDW 461
Cdd:PRK05691 1391 -------RRLFSGGEALPAElRNRVLQRLPQVQLHNRYGPTET--AINVThwqcQAEDGERSPIGRPLgnVLCRVLDAEL 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 462 QeggytindkPNPRG---EIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVK 535
Cdd:PRK05691 1462 N---------LLPPGvagELCIGGAGLARGYLGRPALTAERFVPDplgEDGARLYRTGDRARWNADGALEYLGRLDQQVK 1532
|
490
....*....|....*.
gi 4758332 536 LQaGEYVSLGKVEAAL 551
Cdd:PRK05691 1533 LR-GFRVEPEEIQARL 1547
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
228-534 |
2.06e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPgLGPKDTYIGYLPLAHVLELtaeiscftygcrIGysspl 305
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGID-LNPDDVIVSWLPLYHDMGL------------IG----- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 306 tlsdqsskikkgskgdcTVLKPtLMAAVPEIMdriyknvMSKVQEMNYIQKTLFKIG-----------YDYKL--EQIKk 372
Cdd:PRK05691 227 -----------------GLLQP-IFSGVPCVL-------MSPAYFLERPLRWLEAISeyggtisggpdFAYRLcsERVS- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 373 gyDAPLCNLLLfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQ-----GYGLTESC--------GAG-TVT 437
Cdd:PRK05691 281 --ESALERLDL---------SRWRVAYSGSEPIRQDSlERFAEKFAACGFDPdsffaSYGLAEATlfvsggrrGQGiPAL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 438 EVTDYTTGR------VGAPLICC-------EIKLKDWQEGGyTINDkpNPRGEIVIGGQNISMGYFKNEEKTAEDYsVDE 504
Cdd:PRK05691 350 ELDAEALARnraepgTGSVLMSCgrsqpghAVLIVDPQSLE-VLGD--NRVGEIWASGPSIAHGYWRNPEASAKTF-VEH 425
|
330 340 350
....*....|....*....|....*....|
gi 4758332 505 NGQRWFCTGDIGeFHPDGCLQIIDRKKDLV 534
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 ... |
80-281 |
3.40e-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: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 159
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 LITSVELLE----SKLKT----ALLDISC-VKHIIYVDNKAINKAEYPEGFEIHSMQSVEelGSNPEnlgIPPSRPTPSD 230
Cdd:TIGR02188 164 VITADEGLRggkvIPLKAivdeALEKCPVsVEHVLVVRRTGNPVVPWVEGRDVWWHDLMA--KASAY---CEPEPMDSED 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758332 231 MAIVMYTSGSTGRPKGVMmhHS----NLIAGMTgqCERIPGLGPKD--------------TYIGYLPLA 281
Cdd:TIGR02188 239 PLFILYTSGSTGKPKGVL--HTtggyLLYAAMT--MKYVFDIKDGDifwctadvgwitghSYIVYGPLA 303
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
217-534 |
3.60e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 59.62 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 217 ENLGIPPSRP---TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscf 293
Cdd:PRK07768 137 DLLAADPIDPvetGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGM------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 294 tygcrIGY-SSPLTLSdqsskikkgskgdCTVLKPTLMAAV------PEIMDRiYKNVMSKVQEMNY--IQKTLFKigyd 364
Cdd:PRK07768 210 -----VGFlTVPMYFG-------------AELVKVTPMDFLrdpllwAELISK-YRGTMTAAPNFAYalLARRLRR---- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 365 ykleQIKKG-YDAplcnlllfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTES--- 430
Cdd:PRK07768 267 ----QAKPGaFDL----------------SSLRFALNGAEPIDPADvEDLLDAgarfglrpeAILP----AYGMAEAtla 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 431 -----CGAGTVTEVTD------------YTTGRV------GAPLICCEIKLKDwqEGGYTIndkpNPR--GEIVIGGQNI 485
Cdd:PRK07768 323 vsfspCGAGLVVDEVDadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD--EDGQVL----PPRgvGVIELRGESV 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 4758332 486 SMGYFkneekTAEDY--SVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
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 ... |
87-274 |
3.73e-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: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT---- 162
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadgg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 163 -----SVELLESKLKTALLDISCVKHIIYVDNKAINkAEYPEGFEIHSMQSVEElgSNPENlgiPPSRPTPSDMAIVMYT 237
Cdd:cd17634 167 vragrSVPLKKNVDDALNPNVTSVEHVIVLKRTGSD-IDWQEGRDLWWRDLIAK--ASPEH---QPEAMNAEDPLFILYT 240
|
170 180 190
....*....|....*....|....*....|....*..
gi 4758332 238 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY 274
Cdd:cd17634 241 SGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIY 277
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
22-396 |
4.02e-09 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 60.25 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 22 THFDSLAvidipGADTLDKLFDHAVSKFGKKDSLGtreilsEENEmqpngkvfkkliLGNYKWMNYLEVNRRVNNFGSGL 101
Cdd:PTZ00297 418 REYNPLA-----GVRSLGEMWERSVTRHSTFRCLG------QTSE------------SGESEWLTYGTVDARARELGSGL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 102 TALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLyatLGKEAVVHGLneseasylitsveLLESKLKTALLDISCV 181
Cdd:PTZ00297 475 LALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPL---VGKGSTMRTL-------------IDEHKIKVVFADRNSV 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 182 KHIIYVDNKAINKAEYPEGFEIHSMQSV-----------EELGSNPENLGIPPSRPTPSDMAIVMY----TSGSTGRPKG 246
Cdd:PTZ00297 539 AAILTCRSRKLETVVYTHSFYDEDDHAVardlnitlipyEFVEQKGRLCPVPLKEHVTTDTVFTYVvdntTSASGDGLAV 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VMMHHSNLIAG-----MTGQcerIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIkkgskgd 321
Cdd:PTZ00297 619 VRVTHADVLRDistlvMTGV---LPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVKF------- 688
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758332 322 ctvlKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIK-KGYDAPLCNLLLFKKVKALLGGNVR 396
Cdd:PTZ00297 689 ----QPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRSRLINiHRRDSSLLRFIFFRATQELLGGCVE 760
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
87-583 |
5.04e-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: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplvtlyatLGkeAVVHGLN----ESEASYLIT 162
Cdd:cd05923 31 YSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHR-----------LG--AVPALINprlkAAELAELIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 163 SVELlesklktalldiscvKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGSnPENLG--IPPSRPTPSDMAIVMYTSGS 240
Cdd:cd05923 98 RGEM---------------TAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGE-PESAGplIEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 241 TGRPKGVMM---HHSNLIAGMTGQCeripGL--GPKDTYIGYLPLAHVleltaeiscftygcrIGYSSPLTLSdqsskik 315
Cdd:cd05923 162 TGLPKGAVIpqrAAESRVLFMSTQA----GLrhGRHNVVLGLMPLYHV---------------IGFFAVLVAA------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 316 kgSKGDCTVLkptlmaaVPEIMDRiyknvmskVQEMNYIQKtlfkigydyklEQIKKGYDAP-----LCNLLLFKKVKAl 390
Cdd:cd05923 216 --LALDGTYV-------VVEEFDP--------ADALKLIEQ-----------ERVTSLFATPthldaLAAAAEFAGLKL- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 391 lgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgAGTVTEVTDYTTGRVGAPLICCEIKLKdwQEGGYTIND 470
Cdd:cd05923 267 --SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE---AMNSLYMRDARTGTEMRPGFFSEVRIV--RIGGSPDEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 471 KPN-PRGEIVI--GGQNISMGYFKNEEKTAEDYSvdengQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKV 547
Cdd:cd05923 340 LANgEEGELIVaaAADAAFTGYLNQPEATAKKLQ-----DGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEI 413
|
490 500 510
....*....|....*....|....*....|....*....
gi 4758332 548 EAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKRLT 583
Cdd:cd05923 414 ERVLSRHPGVTEVVVIGVADERWgqsVTACVVPREGTLS 452
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
87-252 |
7.05e-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: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVEL 166
Cdd:cd05966 87 YRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 --------LESKLKTALLDISCVKHIIYVDNKAiNKAEYPEGFEI--HsmqsvEELGSNPENlgIPPSRPTPSDMAIVMY 236
Cdd:cd05966 167 yrggkvipLKEIVDEALEKCPSVEKVLVVKRTG-GEVPMTEGRDLwwH-----DLMAKQSPE--CEPEWMDSEDPLFILY 238
|
170
....*....|....*.
gi 4758332 237 TSGSTGRPKGVMmhHS 252
Cdd:cd05966 239 TSGSTGKPKGVV--HT 252
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
80-251 |
7.62e-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: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 80 GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 159
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 160 LITS---------VELLESKLKTALLDIScVKHIIYVDNKAINKAEYPEGFeihsMQSVEELGSNPENLgippSRPTPSD 230
Cdd:cd05968 167 LITAdgftrrgreVNLKEEADKACAQCPT-VEKVVVVRHLGNDFTPAKGRD----LSYDEEKETAGDGA----ERTESED 237
|
170 180
....*....|....*....|.
gi 4758332 231 MAIVMYTSGSTGRPKGVMMHH 251
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
393-579 |
1.10e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 58.08 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 393 GNVRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTEScgAGTVTEVT--DYTTGR--VGAPLICCEIKLKdwqegg 465
Cdd:PRK07445 230 AQFRTILLGGAPAWPsllEQARQLQL----RLAPTYGMTET--ASQIATLKpdDFLAGNnsSGQVLPHAQITIP------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 466 ytindkPNPRGEIVIGGQNISMGYfkneektaedYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLG 545
Cdd:PRK07445 298 ------ANQTGNITIQAQSLALGY----------YPQILDSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPA 360
|
170 180 190
....*....|....*....|....*....|....*..
gi 4758332 546 KVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 579
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLGLPDPHWgevVTAIYVPKD 397
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
101-662 |
1.88e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.32 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 101 LTALGLKPKNTIAIFCETRAEWMIAAQTCfKYN----FPLVTLYATLGKEAVVHGLN----ESEASYLITSVELLEsklk 172
Cdd:PRK09192 66 LLALGLKPGDRVALIAETDGDFVEAFFAC-QYAglvpVPLPLPMGFGGRESYIAQLRgmlaSAQPAAIITPDELLP---- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 173 taLLdiscvkhiiyvdNKAINKAEYPEGFeihsmqSVEELGSNPENlGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 252
Cdd:PRK09192 141 --WV------------NEATHGNPLLHVL------SHAWFKALPEA-DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 253 NLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeISCFTygcrigysSPLTlsDQSSkikkgskgdcTVLKPTLMAA 332
Cdd:PRK09192 200 ALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGL---VGFLL--------TPVA--TQLS----------VDYLPTRDFA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 333 VPEI--MDRIYKNVMSkvqeMNYIQktlfKIGYDykleqikkgydapLCNLLLFKKVKALL-------GGNvrmmlsGGA 403
Cdd:PRK09192 257 RRPLqwLDLISRNRGT----ISYSP----PFGYE-------------LCARRVNSKDLAELdlscwrvAGI------GAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 404 PLSPQT-HRFMNvCFcCPIG-------QGYGLTESC--------GAGTVTEVTDYT--------------TGRV------ 447
Cdd:PRK09192 310 MIRPDVlHQFAE-AF-APAGfddkafmPSYGLAEATlavsfsplGSGIVVEEVDRDrleyqgkavapgaeTRRVrtfvnc 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 448 GAPLICCEIKLKDwqEGGYTINDKpnPRGEIVIGGQNISMGYFKNEEkTAEDYSVDEngqrWFCTGDIGeFHPDGCLQII 527
Cdd:PRK09192 388 GKALPGHEIEIRN--EAGMPLPER--VVGHICVRGPSLMSGYFRDEE-SQDVLAADG----WLDTGDLG-YLLDGYLYIT 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 528 DRKKDLVKLQaGEYVSLGKVEAALKNCPLID--NICAFAKSDqsyvisfvvPNQKRLTLLAQqkgvegtwvdiCNnpAME 605
Cdd:PRK09192 458 GRAKDLIIIN-GRNIWPQDIEWIAEQEPELRsgDAAAFSIAQ---------ENGEKIVLLVQ-----------CR--ISD 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 4758332 606 AEILKEIREAANAMKLERFEIPIKVRLSPepwtPETGLVTDAFKLKRKELRNHYLKD 662
Cdd:PRK09192 515 EERRGQLIHALAALVRSEFGVEAAVELVP----PHSLPRTSSGKLSRAKAKKRYLSG 567
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
77-591 |
1.98e-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: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 77 LILGNYKWmNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYN-FPLVTLYAtlgkeavvHGLNE- 154
Cdd:COG1021 44 VVDGERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGaIPVFALPA--------HRRAEi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 155 ------SEASYLITS--------VELLESkLKTALldiSCVKHIIYVDNkainkaeyPEGFeihsmQSVEELGSNPENLG 220
Cdd:COG1021 115 shfaeqSEAVAYIIPdrhrgfdyRALARE-LQAEV---PSLRHVLVVGD--------AGEF-----TSLDALLAAPADLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 221 IPpsRPTPSDMAIVMYTSGSTGRPKgvmmhhsnLI-------AGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscf 293
Cdd:COG1021 178 EP--RPDPDDVAFFQLSGGTTGLPK--------LIprthddyLYSVRASAEICGLDADTVYLAALPAAHNFPL------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 294 tygcrigySSPLTLsdqsskikkG--SKGDCTVLKP----------------TLMAAVPEIMDRIyknvmskvqeMNYIQ 355
Cdd:COG1021 241 --------SSPGVL---------GvlYAGGTVVLAPdpspdtafplierervTVTALVPPLALLW----------LDAAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 356 KtlfkigYDYKLeqikkgydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGT 435
Cdd:COG1021 294 R------SRYDL-------------------------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE----GL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 436 VT--------EVTDYTTGRvgaPlICC--EIKLKDwqeggytINDKPNPRGE----IVIGGQNISmGYFKNEEKTAEdyS 501
Cdd:COG1021 339 VNytrlddpeEVILTTQGR---P-ISPddEVRIVD-------EDGNPVPPGEvgelLTRGPYTIR-GYYRAPEHNAR--A 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 502 VDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPN 578
Cdd:COG1021 405 FTPDG--FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgerSCAFVVPR 481
|
570
....*....|....*...
gi 4758332 579 QKRLTLLA-----QQKGV 591
Cdd:COG1021 482 GEPLTLAElrrflRERGL 499
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
87-657 |
3.18e-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: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWmiaaqtcfkynfpLVTLYATLGKEAVVHGLNeseasYLITSVEL 166
Cdd:cd05940 6 YAELDAMANRYARWLKSLGLKPGDVVALFMENRPEY-------------VLLWLGLVKIGAVAALIN-----YNLRGESL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 167 LESklktalLDISCVKHIIYvdnkainkaeypegfeihsmqsveelgsnpenlgippsrptpsDMAIVMYTSGSTGRPKG 246
Cdd:cd05940 68 AHC------LNVSSAKHLVV-------------------------------------------DAALYIYTSGTTGLPKA 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 247 VMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVlelTAEISCFTYGCRIGYSspltlsdqsskikkgskgdcTVLK 326
Cdd:cd05940 99 AIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYHS---TALIVGWSACLASGAT--------------------LVIR 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 327 PTLMAAvpEIMDRIYKNvmskvqemnyiQKTLFkigydykleqikkGYDAPLCNLLLFKKVKAL-LGGNVRMMLSGGapL 405
Cdd:cd05940 155 KKFSAS--NFWDDIRKY-----------QATIF-------------QYIGELCRYLLNQPPKPTeRKHKVRMIFGNG--L 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 406 SPQTHRFMNVCFCCP-IGQGYGLTE-SCG-------AGTVTEVTDYTTGRVGAPLICCEIK----LKDwqEGGYTINDKP 472
Cdd:cd05940 207 RPDIWEEFKERFGVPrIAEFYAATEgNSGfinffgkPGAIGRNPSLLRKVAPLALVKYDLEsgepIRD--AEGRCIKVPR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 473 NPRGEIV--IGGQNISMGYFKN---EEKTAEDysVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 547
Cdd:cd05940 285 GEPGLLIsrINPLEPFDGYTDPaatEKKILRD--VFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK-GENVSTTEV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 548 EAALKncplidnicAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDIcnnPAMEAEILKEireaanamkLERFEIP 627
Cdd:cd05940 362 AAVLG---------AFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDL---SALAAHLEKN---------LPGYARP 420
|
570 580 590
....*....|....*....|....*....|
gi 4758332 628 IKVRLSPEPWTPETglvtdaFKLKRKELRN 657
Cdd:cd05940 421 LFLRLQPEMEITGT------FKQQKVDLRN 444
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
223-568 |
3.98e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.82 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 223 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGpkdTYIGYLPLAHVLELTAEISCFTYGcrigyS 302
Cdd:PRK07824 29 VGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG---QWLLALPAHHIAGLQVLVRSVIAG-----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 303 SPLTLsDQSSKIKkgskgdctvlKPTLMAAVPEI-MDRIYKNVMSKvqemnyiqktlfkigydykleQIKKGYDAPlcnl 381
Cdd:PRK07824 101 EPVEL-DVSAGFD----------PTALPRAVAELgGGRRYTSLVPM---------------------QLAKALDDP---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 382 llfKKVKALLGGNVrmMLSGGAPLSPQTHRfMNVCFCCPIGQGYGLTESCGaGTVTEvtdyttgrvGAPLICCEIKLKDw 461
Cdd:PRK07824 145 ---AATAALAELDA--VLVGGGPAPAPVLD-AAAAAGINVVRTYGMSETSG-GCVYD---------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 462 qeggytindkpnprGEIVIGGQNISMGYfKNEEktaEDYSVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVKlQAGEY 541
Cdd:PRK07824 208 --------------GRIALGGPTLAKGY-RNPV---DPDPFAEPG--WFRTDDLGALD-DGVLTVLGRADDAIS-TGGLT 265
|
330 340
....*....|....*....|....*..
gi 4758332 542 VSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGLPDD 292
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
416-577 |
1.31e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.49 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 416 CFCcpigqGYGLTEScgAGTVTEV-TDYTTGrVGAPLICCEIKLKDwqeggytindkpnprGEIVIGGQNISMGYFKNEE 494
Cdd:PRK09029 267 CWC-----GYGLTEM--ASTVCAKrADGLAG-VGSPLPGREVKLVD---------------GEIWLRGASLALGYWRQGQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 495 KTAedySVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNicafaksdqsyviSF 574
Cdd:PRK09029 324 LVP---LVNDEG--WFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQ-------------VF 383
|
...
gi 4758332 575 VVP 577
Cdd:PRK09029 384 VVP 386
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
85-656 |
1.89e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 54.36 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 85 MNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLGkeAVVHGLN----ESEASYL 160
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ITS-----------------VELLESKLKTALLDiscVKHIIYVDNKAinkAEYPEGFEIHSMQSVE-ELGSNPENLGIP 222
Cdd:PRK06164 103 LGRgrarwlvvwpgfkgidfAAILAAVPPDALPP---LRAIAVVDDAA---DATPAPAPGARVQLFAlPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 223 PSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYG----CR 298
Cdd:PRK06164 177 AA--DPDAGALLFTTSGTTSGPKLVLHRQATLLR-HARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGaplvCE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 299 IGYSSPLTLSD-QSSKIKKGSKGDctvlkptlmaavpEIMDRIYKnvmSKVQEMNYIQKTLFKIGyDY-----KLEQIKK 372
Cdd:PRK06164 254 PVFDAARTARAlRRHRVTHTFGND-------------EMLRRILD---TAGERADFPSARLFGFA-SFapalgELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 373 GYDAPLCNLLLFKKVKALLGG-------NVRMmLSGGAPLSPQthrfmnvcfccpigqgygltescgaGTVtEVTDYTTG 445
Cdd:PRK06164 317 ARGVPLTGLYGSSEVQALVALqpatdpvSVRI-EGGGRPASPE-------------------------ARV-RARDPQDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 446 RVGAPlicceiklkdwqeggytindkpNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDEngqrWFCTGDIGEFHPDGCLQ 525
Cdd:PRK06164 370 ALLPD----------------------GESGEIEIRAPSLMRGYLDNPDATARALTDDG----YFRTGDLGYTRGDGQFV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 526 IIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDN--ICAFAKSDQSYVISFVVPNqkrltllaqqkgvEGTWVDicnnpa 603
Cdd:PRK06164 424 YQTRMGDSLRL-GGFLVNPAEIEHALEALPGVAAaqVVGATRDGKTVPVAFVIPT-------------DGASPD------ 483
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 4758332 604 mEAEILKEIREAanamkLERFEIPIKVRLSPEPWTPETGlvtDAFKLKRKELR 656
Cdd:PRK06164 484 -EAGLMAACREA-----LAGFKVPARVQVVEAFPVTESA---NGAKIQKHRLR 527
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
220-534 |
2.00e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 54.18 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 220 GIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA----GMTGQCERIPGLGPKD-TYIGYLPLAH----VLELTAEI 290
Cdd:PRK05850 151 GSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYFGDTGGVPPPDtTVVSWLPFYHdmglVLGVCAPI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 291 SCftyGCRIGYSSPLTLsdqsskikkgskgdctVLKPT----LMAAVPEImdriyknvmskvqemnyiqktlFKIGYDYK 366
Cdd:PRK05850 231 LG---GCPAVLTSPVAF----------------LQRPArwmqLLASNPHA----------------------FSAAPNFA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 367 LE-QIKKGYDAPLCNLLLfkkvkallgGNVRMMLSGGAPLSPQT-HRFMN--VCFCCP---IGQGYGLTE------SCGA 433
Cdd:PRK05850 270 FElAVRKTSDDDMAGLDL---------GGVLGIISGSERVHPATlKRFADrfAPFNLRetaIRPSYGLAEatvyvaTREP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 434 GTVTEVTDY-----TTGRV-------GAPLIcceiklkdwqegGYTINDKPNPR---------------GEIVIGGQNIS 486
Cdd:PRK05850 341 GQPPESVRFdyeklSAGHAkrcetggGTPLV------------SYGSPRSPTVRivdpdtciecpagtvGEIWVHGDNVA 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 4758332 487 MGYFKNEEKTAE-------DYSVDENGQRWFCTGDIGEFHpDGCLQIIDRKKDLV 534
Cdd:PRK05850 409 AGYWQKPEETERtfgatlvDPSPGTPEGPWLRTGDLGFIS-EGELFIVGRIKDLL 462
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
223-534 |
2.79e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.58 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 223 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLiagMTGQCERIPGLGPK--DTYIGYLPLAHVLELTAEISCFTYGCRIG 300
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNL---PTNVLQVIDALEGQegDRGVSWLPFFHDMGLITVLLPALLGHYIT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 301 YSSPLTLsdqsskikkgskgdctVLKP----TLMAAVPEIMDRIyknvmskvqemnyiqktlFKIGYDYKLEQ-----IK 371
Cdd:PRK07769 251 FMSPAAF----------------VRRPgrwiRELARKPGGTGGT------------------FSAAPNFAFEHaaargLP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 372 KGYDAPLcNLllfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCcPIG-------QGYGLTESC------------- 431
Cdd:PRK07769 297 KDGEPPL-DL-----------SNVKGLLNGSEPVSPASMRKFNEAFA-PYGlpptaikPSYGMAEATlfvsttpmdeept 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 432 ---------GAGTVTEVTDYTTGRVgAPLICCEIKLKDWQE--GGYTINDKPNPR-GEIVIGGQNISMGYFKNEEKTAED 499
Cdd:PRK07769 364 viyvdrdelNAGRFVEVPADAPNAV-AQVSAGKVGVSEWAVivDPETASELPDGQiGEIWLHGNNIGTGYWGKPEETAAT 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 4758332 500 Y--------------SVDENGqRWFCTGDIGEFHpDGCLQIIDRKKDLV 534
Cdd:PRK07769 443 FqnilksrlseshaeGAPDDA-LWVRTGDYGVYF-DGELYITGRVKDLV 489
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
222-564 |
4.66e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 53.51 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS---NLIAGMTGQCeripGLGPKDTyigylplahVLELTAeiscftygCR 298
Cdd:PRK10252 591 PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTaivNRLLWMQNHY----PLTADDV---------VLQKTP--------CS 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 299 IGYSS-----PLTLsdqsskikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmSKVQEMNYIQKTLfkigydykleqikKG 373
Cdd:PRK10252 650 FDVSVweffwPFIA------------GAKLVMAEPEAHRDPLAMQQFFAE--YGVTTTHFVPSML-------------AA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 374 YDAPLCNLLLFKKVKALlggnVRMMLSGGA---PLSPQTHRFMNVcfccPIGQGYGLTEScgAGTVT------EVTDYTT 444
Cdd:PRK10252 703 FVASLTPEGARQSCASL----RQVFCSGEAlpaDLCREWQQLTGA----PLHNLYGPTEA--AVDVSwypafgEELAAVR 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 445 GR---VGAPLicceiklkdWQEGGYTINDKPNP-----RGEIVIGGQNISMGYFKNEEKTAEDYSVD--ENGQRWFCTGD 514
Cdd:PRK10252 773 GSsvpIGYPV---------WNTGLRILDARMRPvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADpfAPGERMYRTGD 843
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 4758332 515 IGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 564
Cdd:PRK10252 844 VARWLDDGAVEYLGRSDDQLKIR-GQRIELGEIDRAMQALPDVEQAVTHA 892
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
484-555 |
4.82e-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: 4.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758332 484 NISMGYFKNEEKTAEDYsVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCP 555
Cdd:cd05924 222 HIPLGYYGDEAKTAETF-PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-TGGEKVFPEEVEEALKSHP 291
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
425-557 |
4.98e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 52.74 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 425 YGLTESCGAGTVT---EVTDYT-TGR---VGAPLICCEIKLKDWQEGgytindKPNP---RGEIVIGGQNISMGYFKNEE 494
Cdd:PRK06178 360 WGMTETHTCDTFTagfQDDDFDlLSQpvfVGLPVPGTEFKICDFETG------ELLPlgaEGEIVVRTPSLLKGYWNKPE 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758332 495 KTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLI 557
Cdd:PRK06178 434 ATAE---ALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAV 490
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
228-584 |
7.98e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.13 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCrigysspltl 307
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRA-CLKFFSPKEDDVMMSFLPPFH-----------AYGF---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 308 sdqsskikkgskgDCTVLKPtLMAAVPEIMDriYKNVMSK--VQEMNYIQKTLF---KIGYDYKLEQIKKGyDAPLCNLL 382
Cdd:PRK06334 240 -------------NSCTLFP-LLSGVPVVFA--YNPLYPKkiVEMIDEAKVTFLgstPVFFDYILKTAKKQ-ESCLPSLR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 383 LfkkvkALLGGNV--RMMLSGGAPLSPQTHrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTTGR-VGAPLICCEIKLK 459
Cdd:PRK06334 303 F-----VVIGGDAfkDSLYQEALKTFPHIQ----------LRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 460 dwQEGGYTindkPNPRGE---IVIGGQNISMGYFKNEEKTAedySVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 536
Cdd:PRK06334 368 --SEETKV----PVSSGEtglVLTRGTSLFSGYLGEDFGQG---FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 4758332 537 qAGEYVSLGKVEAALkncplidnICAFAKSDQSYVISFVV---PNQK-RLTL 584
Cdd:PRK06334 439 -GAEMVSLEALESIL--------MEGFGQNAADHAGPLVVcglPGEKvRLCL 481
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
227-656 |
1.90e-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: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNliagmtgqceripglgpkdTYIGYLPLAHVLELTAEIScfTYGCRIGYSSPLT 306
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRR-------------------TLVTSNLLSHDLNLKNGDR--TYTCMPLYHGTAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 307 LSDQSSKIKKGSkgdCTVLKPTLMAAvpeimdRIYKNVMSkvQEMNYIQktlfkigydykleqikkgYDAPLCNLLLF-- 384
Cdd:cd05937 144 FLGACNCLMSGG---TLALSRKFSAS------QFWKDVRD--SGATIIQ------------------YVGELCRYLLStp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 385 --KKVKAllgGNVRMMLSGGapLSPQT-HRFMNVcFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 460
Cdd:cd05937 195 psPYDRD---HKVRVAWGNG--LRPDIwERFRER-FNVPeIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFEN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 461 WQ-------EGGYTINDKPN------PRGEiviGGQNIS----------MGYFKNEEKTAEDYSVD--ENGQRWFCTGDI 515
Cdd:cd05937 269 QVvlvkmdpETDDPIRDPKTgfcvraPVGE---PGEMLGrvpfknreafQGYLHNEDATESKLVRDvfRKGDIYFRTGDL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 516 GEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEaalkncpliDNICAFAKSDQSYVISFVVPNQKrltllaQQKGVEGtw 595
Cdd:cd05937 346 LRQDADGRWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHPDIAEANVYGVKVPGHD------GRAGCAA-- 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758332 596 VDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEpwtpetGLVTDAFKLKRKELR 656
Cdd:cd05937 408 ITLEESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VATTDNHKQQKGVLR 462
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
236-545 |
2.36e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 50.81 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 236 YTSGSTGRPKGVMMHHSNLIAGMTGQ-CERIPGLGPKDTYIGYLPLAHvleltaeiscftyGCRIgysspltlsDQSSKI 314
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFVITNHlADLMPGTTEQDASLVVAPLSH-------------GAGI---------HQLCQV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 315 KKGSKgdcTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKigyDYKLEQikkgYDAplcnlllfkkvkallgGN 394
Cdd:PRK07470 228 ARGAA---TVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVE---HPAVDR----YDH----------------SS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 395 VRMMLSGGAPL--SPQTH---RFMNVcfccpIGQGYGLTESCGAGTVT-----EVTDYTTGRVGapliCC-------EIK 457
Cdd:PRK07470 282 LRYVIYAGAPMyrADQKRalaKLGKV-----LVQYFGLGEVTGNITVLppalhDAEDGPDARIG----TCgfertgmEVQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 458 LKDwqEGGYTIndKPNPRGEIVIGGQNISMGYFKNEEKTAEDYsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLvklq 537
Cdd:PRK07470 353 IQD--DEGREL--PPGETGEICVIGPAVFAGYYNNPEANAKAF---RDG--WFRTGDLGHLDARGFLYITGRASDM---- 419
|
....*...
gi 4758332 538 ageYVSLG 545
Cdd:PRK07470 420 ---YISGG 424
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
209-539 |
2.39e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.53 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 209 VEELGSNPENLGIPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTA 288
Cdd:PRK05851 134 LATAAHTNRSASLTP--PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 289 EISCFTYGcrigysSPLTLSDQSSkikkgskgdctvlkptlMAAVPeimdriyknvMSKVQEMNYIQKTLFK---IGYDY 365
Cdd:PRK05851 212 LLTAALAG------APLWLAPTTA-----------------FSASP----------FRWLSWLSDSRATLTAapnFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 366 kleqIKKgYDaplcnlllfKKVKALLGGNVRMMLSGGAPLSPQ-THRFMNVcfCCPIG-------QGYGLTES------- 430
Cdd:PRK05851 259 ----IGK-YA---------RRVSDVDLGALRVALNGGEPVDCDgFERFATA--MAPFGfdagaaaPSYGLAEStcavtvp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 431 -CGAG-TVTEVTDYTTG------RVGAPLICCEIKLKDwQEGGYTINDKpnPRGEIVIGGQNISMGYFKNEEKTAEDysv 502
Cdd:PRK05851 323 vPGIGlRVDEVTTDDGSgarrhaVLGNPIPGMEVRISP-GDGAAGVAGR--EIGEIEIRGASMMSGYLGQAPIDPDD--- 396
|
330 340 350
....*....|....*....|....*....|....*..
gi 4758332 503 dengqrWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAG 539
Cdd:PRK05851 397 ------WFPTGDLGYL-VDGGLVVCGRAKELITV-AG 425
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
476-548 |
3.04e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 50.48 E-value: 3.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758332 476 GEIVIGGQNISMGYFKNEEKTAEDysvdengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 548
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASPLVD--------GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
233-578 |
1.77e-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: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 233 IVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysspltlsdqss 312
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLA-QALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAG---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 313 kikkgskGDCTVLKPTLMAAVPEIMDRiyknvmSKVQEMNYIQKTLfkigydyklEQIKKGYDAPLCNLLLFKKVKALLG 392
Cdd:cd17636 67 -------GTNVFVRRVDAEEVLELIEA------ERCTHAFLLPPTI---------DQIVELNADGLYDLSSLRSSPAAPE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 393 GNvrMMLSggAPLSPQTHRFMnvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytiNDKP 472
Cdd:cd17636 125 WN--DMAT--VDTSPWGRKPG----------GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDG----REVP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 473 NPR-GEIVIGGQNISMGYFKNEEktaedysvdENGQR----WFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKV 547
Cdd:cd17636 186 DGEvGEIVARGPTVMAGYWNRPE---------VNARRtrggWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEV 255
|
330 340 350
....*....|....*....|....*....|....*
gi 4758332 548 EAALKNCPLIDNICAFAKSD----QSyVISFVVPN 578
Cdd:cd17636 256 ERCLRQHPAVADAAVIGVPDprwaQS-VKAIVVLK 289
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
87-259 |
1.84e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 47.83 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLG-KEAVVHG----------LNES 155
Cdd:PRK00174 101 YRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC-----------ARIGaVHSVVFGgfsaealadrIIDA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 156 EASYLITSVELLE----SKLKT----ALLDISCVKHIIYVdNKAINKAEYPEGFEI--HSMQSveelGSNPEnlgIPPSR 225
Cdd:PRK00174 170 GAKLVITADEGVRggkpIPLKAnvdeALANCPSVEKVIVV-RRTGGDVDWVEGRDLwwHELVA----GASDE---CEPEP 241
|
170 180 190
....*....|....*....|....*....|....*...
gi 4758332 226 PTPSDMAIVMYTSGSTGRPKGVMmhHS----NLIAGMT 259
Cdd:PRK00174 242 MDAEDPLFILYTSGSTGKPKGVL--HTtggyLVYAAMT 277
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
210-282 |
3.25e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.98 E-value: 3.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758332 210 EELGSNPENLgIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTgQCERIpGLGPKDTYIGYLPLAH 282
Cdd:PRK07867 134 DELAAHRDAE-PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVM-LAQRF-GLGPDDVCYVSMPLFH 204
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
86-269 |
4.93e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.09 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 86 NYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEW--MIAAQtcFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 163
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLlgMIVGS--FKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 164 VELLEskLKTALLDiscvkhiiyvdnkAINKAEYPEGFEIHSMQSVEELGSNPenlGIppsRPTPSDMAIVMYTSGSTGR 243
Cdd:PRK05691 3825 AACRE--QARALLD-------------ELGCANRPRLLVWEEVQAGEVASHNP---GI---YSGPDNLAYVIYTSGSTGL 3883
|
170 180
....*....|....*....|....*..
gi 4758332 244 PKGVMMHHsnliAGM-TGQCERIPGLG 269
Cdd:PRK05691 3884 PKGVMVEQ----RGMlNNQLSKVPYLA 3906
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
209-656 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 209 VEELGSNPENLgIPPSRPtPSDMaivMYTSGSTGRPKGVMMHHS------NLIAGMTGQCeripGLGPKDTYIGYLPLAH 282
Cdd:cd05929 110 EAAEGGSPETP-IEDEAA-GWKM---LYSGGTTGRPKGIKRGLPggppdnDTLMAAALGF----GPGADSVYLSPAPLYH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 283 vleltaeiscftygcrigySSPLTLSDQSSKIkkgskGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYIqKTLF-KI 361
Cdd:cd05929 181 -------------------AAPFRWSMTALFM-----GGTLVLMEKFDPE--EFLRLIERY---RVTFAQFV-PTMFvRL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 362 gydYKL-EQIKKGYDaplcnlllfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEsCGAGTVTEVT 440
Cdd:cd05929 231 ---LKLpEAVRNAYD-----------LSSL-----KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE-GQGLTIINGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 441 DYTT--GRVGAPLicceiklkdwqEGGYTI---NDKPNPRGEI--VIGGQNISMGYFKNEEKTAEdySVDENGqrWFCTG 513
Cdd:cd05929 291 EWLThpGSVGRAV-----------LGKVHIldeDGNEVPPGEIgeVYFANGPGFEYTNDPEKTAA--ARNEGG--WSTLG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 514 DIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKrltlLAQQ-KGVE 592
Cdd:cd05929 356 DVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVG-----------VPDEE----LGQRvHAVV 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758332 593 GTWVDICNNPAMEAEILKEIREAanamkLERFEIPIKVRLSPEPwtpetgLVTDAFKLKRKELR 656
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, ... |
236-560 |
1.09e-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: 44.70 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 236 YTSGSTGRPKGVMMHHSNLIAGMTGQcERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIK 315
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 316 KGSKgdctvlkpTLMAAVPEIMDRIYK--NVMSKVQEMNYIQKTLFKIgydyKLEQIKKGydAPLCNLLLFkkvkallgg 393
Cdd:cd17633 86 QYNA--------TVIYLVPTMLQALARtlEPESKIKSIFSSGQKLFES----TKKKLKNI--FPKANLIEF--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 394 nvrmmlSGGAPLSPQTHRFMNvcfccpigqgygltescgagtvtevTDYTTGRVGAPLICCEIKLKDwQEGGYTindkpn 473
Cdd:cd17633 143 ------YGTSELSFITYNFNQ-------------------------ESRPPNSVGRPFPNVEIEIRN-ADGGEI------ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 474 prGEIVIGGQNISMGYFKNEEktaedYSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKN 553
Cdd:cd17633 185 --GKIFVKSEMVFSGYVRGGF-----SNPDG----WMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKA 252
|
....*..
gi 4758332 554 CPLIDNI 560
Cdd:cd17633 253 IPGIEEA 259
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-558 |
1.68e-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: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 219 LGIPPSrptpSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL----AHVLELTAEIScft 294
Cdd:cd05910 79 IGIPKA----DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY-GIRPGEVDLATFPLfalfGPALGLTSVIP--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 295 ygcRIGYSSPLTLSDQS--SKIKKgskgdctvLKPTLMAAVPEIMDRIYKNVMSkvqemnyIQKTLfkigydykleqikk 372
Cdd:cd05910 151 ---DMDPTRPARADPQKlvGAIRQ--------YGVSIVFGSPALLERVARYCAQ-------HGITL-------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 373 gydaplcnlllfkkvkallgGNVRMMLSGGAPLSPQTH-RFMN-VCFCCPIGQGYGLTESC------GAGTVTEVTDYTT 444
Cdd:cd05910 199 --------------------PSLRRVLSAGAPVPIALAaRLRKmLSDEAEILTPYGATEALpvssigSRELLATTTAATS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 445 GR----VGAPLICCEIKL-----KDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDI 515
Cdd:cd05910 259 GGagtcVGRPIPGVRVRIieiddEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 4758332 516 GEFHPDGCLQIIDRKKDLVKLQAGEYVSLgKVEAALKNCPLID 558
Cdd:cd05910 339 GYLDDEGRLWFCGRKAHRVITTGGTLYTE-PVERVFNTHPGVR 380
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
478-569 |
2.45e-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: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 478 IVIGGQNISMGYFKNEEKTaeDYSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 557
Cdd:cd05915 363 VQLKGPWITGGYYGNEEAT--RSALTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLENALMGHPKV 437
|
90
....*....|..
gi 4758332 558 DNICAFAKSDQS 569
Cdd:cd05915 438 KEAAVVAIPHPK 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
222-558 |
2.85e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAEISCftyGCR 298
Cdd:PRK05691 2326 LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF-GMRADDCELHFYSInfdAASERLLVPLLC---GAR 2401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 299 IgysspltlsdqsskikkgskgdctVLKPTLMAAVPEIMDRIyknvmsKVQEMNYIQktlFKIGYDYKLEQIKKGYDAPL 378
Cdd:PRK05691 2402 V------------------------VLRAQGQWGAEEICQLI------REQQVSILG---FTPSYGSQLAQWLAGQGEQL 2448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 379 cnlllfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCcP--IGQGYGLTESC--------------GAGTVTevtdy 442
Cdd:PRK05691 2449 ---------------PVRMCITGGEALTGEHLQRIRQAFA-PqlFFNAYGPTETVvmplaclapeqleeGAASVP----- 2507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 443 tTGR-VGAPLicceiklkdwqegGYTINDK--PNPRG---EIVIGGQNISMGYFKNEEKTAEDYSVD---ENGQRWFCTG 513
Cdd:PRK05691 2508 -IGRvVGARV-------------AYILDADlaLVPQGatgELYVGGAGLAQGYHDRPGLTAERFVADpfaADGGRLYRTG 2573
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 4758332 514 DIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLID 558
Cdd:PRK05691 2574 DLVRLRADGLVEYVGRIDHQVKIR-GFRIELGEIESRLLEHPAVR 2617
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
7-282 |
6.84e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 43.17 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 7 AKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAvskfgkKDSLGtrEILSEENEMQPNGKVFkkliLGNYKWMN 86
Cdd:PRK07868 407 ARGAADAAVAANRSVRTLAVETARTLPRLARLGQINDHT------RISLG--RIIAEQARDAPKGEFL----LFDGRVHT 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAaqtcfkynfplVTLYATLGKEAVV----HGLNES----EAS 158
Cdd:PRK07868 475 YEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVA-----------IAALSRLGAVAVLmppdTDLAAAvrlgGVT 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 159 YLITSVELLESKLKTALldiscvkHIIYVDNKAINKAEYPEGFEIHSMQSVEelgsnPENLGIPP-SRPTPS---DMAIV 234
Cdd:PRK07868 544 EIITDPTNLEAARQLPG-------RVLVLGGGESRDLDLPDDADVIDMEKID-----PDAVELPGwYRPNPGlarDLAFI 611
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 4758332 235 MY-TSGSTGRPKGVMMHHSNLIAGMTGQCERipgLGPKDTYIGYLPLAH 282
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 ... |
402-555 |
7.30e-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: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 402 GAPLSPQT-HRFMNVCfCCPIGQGYGLTEScgagTVTEVT----DYTTGRVGAPLICCEIKLKDwQEGGYTindKPNPRG 476
Cdd:cd05970 310 GEALNPEVfNTFKEKT-GIKLMEGFGQTET----TLTIATfpwmEPKPGSMGKPAPGYEIDLID-REGRSC---EAGEEG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 477 EIVI---GGQNISM--GYFKNEEKTAEdysVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 551
Cdd:cd05970 381 EIVIrtsKGKPVGLfgGYYKDAEKTAE---VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESAL 454
|
....
gi 4758332 552 KNCP 555
Cdd:cd05970 455 IQHP 458
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-283 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 87 YLEVNRRVNNFGSGL-TALGLKPKNTIAIFC--ETRAEWM---IAAQTCfkynfPLVTLYATLGKEAVVHGLNESEASYL 160
Cdd:cd05938 8 YRDVDRRSNQAARALlAHAGLRPGDTVALLLgnEPAFLWIwlgLAKLGC-----PVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758332 161 ITSVELLES------KLKTALLdiscvkHIIYVDNKAInkaeyPEGFeIHSMQSVEELGSNPenlgIPPS---RPTPSDM 231
Cdd:cd05938 83 VVAPELQEAveevlpALRADGV------SVWYLSHTSN-----TEGV-ISLLDKVDAASDEP----VPASlraHVTIKSP 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 4758332 232 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQceRIPGLGPKDTYIGYLPLAHV 283
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISHLRVLQCSGFL--SLCGVTADDVIYITLPLYHS 196
|
|
| |
