|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
80-654 |
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: 805.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASY 159
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 LITSvellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskPVPTDLALIMYTSG 239
Cdd:cd17639 81 IFTD--------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 240 STGRPKGVMMIHKNLIAGMTGQCERIPE-LGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDqssKIKKGS 318
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 319 KGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYKLEQIKRGYDAPLCNILLFKKVKALLGGNVRMM 398
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 399 LSGGAPLSPQTQRFMNIcFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTCrDKPNPRGEI 478
Cdd:cd17639 256 LSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYST-DKPPPRGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 479 IIGGPNVSMGYFKNEEKT-EDFsvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFID 557
Cdd:cd17639 334 LIRGPNVFKGYYKNPEKTkEAF----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 558 NICAYAKSDQSYVISFVVPNQKKLTVLAEQKGVK-GTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKVRLSPEPW 636
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVInSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 1935119612 637 TPETGLVTDAFKLKRKEL 654
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
3-666 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 794.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 3 KRLKAKPISDKPGSPFRSVTHLEslaTIDIP--GADTLDKLFDHAVAKFGKKDCLGTREILSEENEMQPNGKVFKKLILG 80
Cdd:PLN02387 26 KRGVPVDVGGEPGYAIRNARFPE---LVETPweGATTLAALFEQSCKKYSDKRLLGTRKLISREFETSSDGRKFEKLHLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 81 NYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYL 160
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 161 ITSVELLEsKLKPALSEIPGLKHIIYVDKKTINKSEYPEGLE---IHSMQTVEELGakpENLDIPPSKPVPTDLALIMYT 237
Cdd:PLN02387 183 ICDSKQLK-KLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSnwtVSSFSEVEKLG---KENPVDPDLPSPNDIAVIMYT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 238 SGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDQSSKIKKG 317
Cdd:PLN02387 259 SGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 318 SKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYKLEQIK------RGYDAPLCNILLFKKVKALL 391
Cdd:PLN02387 339 TKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEgswfgaWGLEKLLWDALVFKKIRAVL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 392 GGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTCRDK 471
Cdd:PLN02387 419 GGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDK 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 472 PNPRGEIIIGGPNVSMGYFKNEEKT-EDFSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETAL 550
Cdd:PLN02387 499 PMPRGEIVIGGPSVTLGYFKNQEKTdEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAAL 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 551 KNCPFIDNICAYAKSDQSYVISFVVPNQKKLTVLAEQKGVK-GTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKV 629
Cdd:PLN02387 579 SVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKI 658
|
650 660 670
....*....|....*....|....*....|....*..
gi 1935119612 630 RLSPEPWTPETGLVTDAFKLKRKELKNHYLNDIERMY 666
Cdd:PLN02387 659 KLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
80-666 |
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: 528.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLK--PKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGA 157
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 158 SylitsvellesklkpalseipglkhIIYVDKktinkseypeGLEIHSMQTVEELGAKPEnldIPPSKPVPTDLALIMYT 237
Cdd:cd05927 81 S-------------------------IVFCDA----------GVKVYSLEEFEKLGKKNK---VPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 238 SGSTGRPKGVMMIHKNLIAGMTGQC---ERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSS--PLTLSDqss 312
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 313 kikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYKLEQIKRG--YDAPLCNILLFKKVKAL 390
Cdd:cd05927 200 --------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 391 LGGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTCRD 470
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 471 kPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETAL 550
Cdd:cd05927 352 -PNPRGEVCIRGPNVFSGYYKDPEKTAE-ALDEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIY 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 551 KNCPFIDNICAYAKSDQSYVISFVVPNQKKLTVLAEQK-GVKGTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKV 629
Cdd:cd05927 428 ARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAI 507
|
570 580 590
....*....|....*....|....*....|....*..
gi 1935119612 630 RLSPEPWTPETGLVTDAFKLKRKELKNHYLNDIERMY 666
Cdd:cd05927 508 HLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
31-669 |
4.78e-162 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 478.83 E-value: 4.78e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 31 DIPGADTLDKLFDHAVAKFGKKDCLGTREilseenemqpngkvfkkliLGNYRWLNYEDINQRVNHFGRGLAAQGLKPKS 110
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKE-------------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 111 AIAIFCETRAEWMIA--------AQTcfkynfplVTLYATLGEEAVTYGLNESGASYLITSVELLESKLKPALSEIPGLK 182
Cdd:COG1022 67 RVAILSDNRPEWVIAdlailaagAVT--------VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 183 HIIYVDKKTInkseyPEGLEIHSMQTVEELGAK---PENLDIPPSKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMT 259
Cdd:COG1022 139 HIVVLDPRGL-----RDDPRLLSLDELLALGREvadPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 260 GQCERIPeLGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYS-SPLTLSDqsskikkgskgDCTVLKPTLMAAVPEIMD 338
Cdd:COG1022 214 ALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------DLREVKPTFMLAVPRVWE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 339 RIYKNVMSKVQEMNYIQRTLF----KIGYDYKlEQIKRGYDAP--------LCNILLFKKVKALLGGNVRMMLSGGAPLS 406
Cdd:COG1022 282 KVYAGIQAKAEEAGGLKRKLFrwalAVGRRYA-RARLAGKSPSlllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 407 PQTQRF---MNIcfccPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDwqeggytcrdkpnpRGEIIIGGP 483
Cdd:COG1022 361 PELARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKIAE--------------DGEILVRGP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 484 NVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDNICAYA 563
Cdd:COG1022 423 NVMKGYYKNPEATAE-AFDADG--WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 564 kSDQSYVISFVVPNQKKLTVLAEQKGVK-GTWVEICNNPIMEAEILKEIKEVADkmKLERFETPIKVRLSPEPWTPETGL 642
Cdd:COG1022 500 -DGRPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGE 576
|
650 660
....*....|....*....|....*..
gi 1935119612 643 VTDAFKLKRKELKNHYLNDIERMYGGK 669
Cdd:COG1022 577 LTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
15-666 |
6.61e-161 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 477.67 E-value: 6.61e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 15 GSPFRSVTHLEslatiDIPGADTLDKLFDHAVAKFGKKDCLGTReilseeneMQPNGKVfkklilGNYRWLNYEDINQRV 94
Cdd:PLN02736 28 RSPLKLVSRFP-----DHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 95 NHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVELLESKLKpA 174
Cdd:PLN02736 89 TAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLS-C 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 175 LSEIPGLKHIIYVDKKTINKSEYPE--GLEIHSMQTVEELG-AKPEnldiPPSKPVPTDLALIMYTSGSTGRPKGVMMIH 251
Cdd:PLN02736 168 LSEIPSVRLIVVVGGADEPLPSLPSgtGVEIVTYSKLLAQGrSSPQ----PFRPPKPEDVATICYTSGTTGTPKGVVLTH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 252 KNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSP--LTLSDqsskikkgskgDCTVLKPTL 329
Cdd:PLN02736 244 GNLIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGdnLKLMD-----------DLAALRPTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 330 MAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYKLEQIKRGYD-APLCNILLFKKVKALLGGNVRMMLSGGAPLSPQ 408
Cdd:PLN02736 312 FCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 409 TQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTCRDKPNPRGEIIIGGPNVSMG 488
Cdd:PLN02736 392 VMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 489 YFKNEEKTEDFsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQS 568
Cdd:PLN02736 472 YYKDEVQTREV-IDEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 569 YVISFVVPNQKKLTVLAEQKGVK-GTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKVRLSPEPWTPETGLVTDAF 647
Cdd:PLN02736 549 SLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTF 628
|
650
....*....|....*....
gi 1935119612 648 KLKRKELKNHYLNDIERMY 666
Cdd:PLN02736 629 KVKRPQAKAYFAKAISDMY 647
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
50-666 |
3.09e-150 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 451.74 E-value: 3.09e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 50 GKKDCLGTREILSEENEM--QPNG--KVFKKLILGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIA 125
Cdd:PTZ00216 83 GDRRALAYRPVERVEKEVvkDADGkeRTMEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLAS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 126 AQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITS---VELLESKLKpaLSEIPGLKhIIYVDkktinksEYPEGLE 202
Cdd:PTZ00216 163 IYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNgknVPNLLRLMK--SGGMPNTT-IIYLD-------SLPASVD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 203 IHSMQ-----TVEELGAKP---ENLDIPPSKpvpTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPEL-GPK-- 271
Cdd:PTZ00216 233 TEGCRlvawtDVVAKGHSAgshHPLNIPENN---DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGPPee 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 272 -DTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDQSSKikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQE 350
Cdd:PTZ00216 310 dETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPP 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 351 MNYIQRTLFKIGYDYKLEQIKRGYDAPLCNILLFKKVKALLGGNVRMMLSGGAPLSPQTQRFMNICFcCPVGQGYGLTET 430
Cdd:PTZ00216 386 VGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTET 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 431 CGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTcrDKPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFC 510
Cdd:PTZ00216 465 VCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHT--DTPEPRGEILLRGPFLFKGYYKQEELTRE-VLDEDG--WFH 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 511 TGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDN--ICAYAKSDQSYVISFVVPNQKKLTVLAEQK 588
Cdd:PTZ00216 540 TGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEH 619
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935119612 589 GVKGTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLNDIERMY 666
Cdd:PTZ00216 620 GIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
80-654 |
3.92e-138 |
|
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: 411.99 E-value: 3.92e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASY 159
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 LITSVellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvPTDLALIMYTSG 239
Cdd:cd05907 81 LFVED---------------------------------------------------------------PDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 240 STGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVLE-LTAEISCVTYGCRIGYSSPL-TLSDQSSKIKkg 317
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAeTLLDDLSEVR-- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 318 skgdctvlkPTLMAAVPEIMDRIYKNVmsKVQEMNYIQRTLFKIGYdykleqikrgydaplcnillfkkvkallGGNVRM 397
Cdd:cd05907 175 ---------PTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAV----------------------------GGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 398 MLSGGAPLSPQTQRFMNIcFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDwqeggytcrdkpnpRGE 477
Cdd:cd05907 216 AASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--------------DGE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 478 IIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFID 557
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAE-ALDADG--WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLIS 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 558 NICAYAkSDQSYVISFVVPNQKKLTVLAEQKGVKGTWV-EICNNPIMEAEILKEIKEVadKMKLERFETPIKVRLSPEPW 636
Cdd:cd05907 358 QAVVIG-DGRPFLVALIVPDPEALEAWAEEHGIAYTDVaELAANPAVRAEIEAAVEAA--NARLSRYEQIKKFLLLPEPF 434
|
570
....*....|....*...
gi 1935119612 637 TPETGLVTDAFKLKRKEL 654
Cdd:cd05907 435 TIENGELTPTLKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
13-666 |
1.02e-125 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 387.25 E-value: 1.02e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 13 KP--GSPFRSVTHLESLATIDiPGADTLDKLFDHAVAKFGKKDCLGTREILseenemqpNGKVfkklilGNYRWLNYEDI 90
Cdd:PLN02430 18 KPsvGPVYRNLLSKKGFPPID-SDITTAWDIFSKSVEKYPDNKMLGWRRIV--------DGKV------GPYMWKTYKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 91 NQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVELLESK 170
Cdd:PLN02430 83 YEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 171 LKPALSEIPGLKHIIYVDKKTINKSEYPEGLEIHSMQTVEELGAKPENLDiPPSKPVPTDLALIMYTSGSTGRPKGVMMI 250
Cdd:PLN02430 163 LEPDCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPS-ETNPPKPLDICTIMYTSGTSGDPKGVVLT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 251 HKNLIAGMTG------QCEriPELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSpltlSDQSSkikkgSKGDCTV 324
Cdd:PLN02430 242 HEAVATFVRGvdlfmeQFE--DKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYH----GDLNA-----LRDDLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 325 LKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYKLEQIKRGYD----APLCNILLFKKVKALLGGNVRMMLS 400
Cdd:PLN02430 311 LKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLAFRKVKAKLGGRLRLLIS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 401 GGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYST-GRVGAPLICCEIKLRDWQEGGYTCRDKPnPRGEII 479
Cdd:PLN02430 391 GGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYDPLGEP-PRGEIC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 480 IGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDNI 559
Cdd:PLN02430 470 VRGKCLFSGYYKNPELTEEVMKDG----WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDI 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 560 CAYAKSDQSYVISFVVPNQKKLTVLAEQKGVKGTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKVRLSPEPWTPE 639
Cdd:PLN02430 546 WVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVE 625
|
650 660
....*....|....*....|....*..
gi 1935119612 640 TGLVTDAFKLKRKELKNHYLNDIERMY 666
Cdd:PLN02430 626 RDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
6-666 |
2.15e-117 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 365.70 E-value: 2.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 6 KAKPISD-KP--GSPFRSVTHLESLatIDIP-GADTLDKLFDHAVAKFGKKDCLGTREILseenemqpNGKVfkklilGN 81
Cdd:PLN02861 11 ESRPATGgKPsaGPVYRSIYAKDGL--LDLPaDIDSPWQFFSDAVKKYPNNQMLGRRQVT--------DSKV------GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 82 YRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASylI 161
Cdd:PLN02861 75 YVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 162 TSVEllESKLKPALSEIPG----LKHII-YVDKKTINKSEYPE-GLEIHSMQTVEELGAkpENLDIPPSKPvpTDLALIM 235
Cdd:PLN02861 153 AFVQ--ESKISSILSCLPKcssnLKTIVsFGDVSSEQKEEAEElGVSCFSWEEFSLMGS--LDCELPPKQK--TDICTIM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 236 YTSGSTGRPKGVMMIHKNLIAGMTgQCERIPELGPK-----DTYVGYLPLAHVLELTAEISCVTYGCRIGYSSpltlSDQ 310
Cdd:PLN02861 227 YTSGTTGEPKGVILTNRAIIAEVL-STDHLLKVTDRvateeDSYFSYLPLAHVYDQVIETYCISKGASIGFWQ----GDI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 311 SSKIKkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYKLEQIKRGYD----APLCNILLFKK 386
Cdd:PLN02861 302 RYLME-----DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRLVFDK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 387 VKALLGGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGaGTITEVSD-YS-TGRVGAPLICCEIKLRDWQEG 464
Cdd:PLN02861 377 IKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANvFSmVGTVGVPMTTIEARLESVPEM 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 465 GYTCRDKPnPRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLG 544
Cdd:PLN02861 456 GYDALSDV-PRGEICLRGNTLFSGYHKRQDLTEEVLIDG----WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 545 KVETALKNCPFIDNICAYAKSDQSYVISFVVPNQKKLTVLAEQKGVKGTWVEICNNPIMEAEILKEIKEVADKMKLERFE 624
Cdd:PLN02861 531 NLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFE 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1935119612 625 TPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLNDIERMY 666
Cdd:PLN02861 611 MLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
32-666 |
3.58e-113 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 354.71 E-value: 3.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 32 IPGADTLDKLFDHAVAKFGKKDCLGTREILseenemqpNGKVfkklilGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSA 111
Cdd:PLN02614 41 IEGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 112 IAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVELLESKLKPALSEIPGLKHIIYVDKKT 191
Cdd:PLN02614 107 CGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 192 INKSEYPE--GLEIHSMQTVEELGaKPENLDIPPSKPvpTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERI---- 265
Cdd:PLN02614 187 REQKEEAEtfGLVIYAWDEFLKLG-EGKQYDLPIKKK--SDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksan 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 266 PELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSpltlSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIYKNVM 345
Cdd:PLN02614 264 AALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR----GDVKLLIE-----DLGELKPTIFCAVPRVLDRVYSGLQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 346 SKVQEMNYIQRTLFKIGYDYKLEQIKRGYD----APLCNILLFKKVKALLGGNVRMMLSGGAPLSPQTQRFMNICFCCPV 421
Cdd:PLN02614 335 KKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 422 GQGYGLTETCgAGTITEVSDY--STGRVGAPLICCEIKLRDWQEGGYTCRDKpNPRGEIIIGGPNVSMGYFKNEEKTEDF 499
Cdd:PLN02614 415 LQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVDIRLESVPEMEYDALAS-TPRGEICIRGKTLFSGYYKREDLTKEV 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 500 SVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSYVISFVVPNQK 579
Cdd:PLN02614 493 LIDG----WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQ 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 580 KLTVLAEQKGVKGTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYL 659
Cdd:PLN02614 569 ILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQ 648
|
....*..
gi 1935119612 660 NDIERMY 666
Cdd:PLN02614 649 SVIDEMY 655
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
77-536 |
9.85e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 345.45 E-value: 9.85e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESG 156
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLESKLKPALSEIPGLKHIIYVDKKTINKSEypegleihsmqTVEELGAKPENLDIPPSKPVPTDLALIMY 236
Cdd:pfam00501 94 AKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 237 TSGSTGRPKGVMMIHKNLIAGMTGQ---CERIPELGPKDTYVGYLPLAHVLELTAEI-SCVTYGCRIGYSSPLTLSDQss 312
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALDP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 313 kikKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmskvqemnyiqrtlfkigydykleqikrgydaplcnillfKKVKALLG 392
Cdd:pfam00501 241 ---AALLELIERYKVTVLYGVPTLLNMLLEA-----------------------------------------GAPKRALL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 393 GNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTIT---EVSDYSTGRVGAPLICCEIKLRDWQEGGYTcr 469
Cdd:pfam00501 277 SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPlplDEDLRSLGSVGRPLPGTEVKIVDDETGEPV-- 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1935119612 470 dKPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDEngQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQ 536
Cdd:pfam00501 355 -PPGEPGELCVRGPGVMKGYLNDPELTAE-AFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
80-651 |
8.22e-69 |
|
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: 232.25 E-value: 8.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQtcfkynfplvtlyatlgeeavtyGLNESGASY 159
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQ-----------------------GIMALGAVD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 LITSVEllesklkpalSEIPGLKHIIyvdkktiNKSEyPEGLEIhsmqtveelgakpENldippskpVPTDLALIMYTSG 239
Cdd:cd17640 58 VVRGSD----------SSVEELLYIL-------NHSE-SVALVV-------------EN--------DSDDLATIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 240 STGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDqsskikkgsk 319
Cdd:cd17640 99 TTGNPKGVMLTHANLLHQIRSLSDIVP-PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKD---------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 320 gDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIgydykleqikrgydaplcnillfkkvkALLGGNVRMML 399
Cdd:cd17640 168 -DLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF---------------------------FLSGGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 400 SGGAPLSPQTQRFMNIcFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTcrdKPNPRGEII 479
Cdd:cd17640 220 SGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVL---PPGEKGIVW 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 480 IGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDNI 559
Cdd:cd17640 296 VRGPQVMKGYYKNPEATSK-VLDSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQI 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 560 CAYAKsDQSYVISFVVPNQKKLTVLAEQKGVK---GTWVEICNNPIMEAEILKEIKEVADKMKLERFETPIKVRLSPEPW 636
Cdd:cd17640 373 MVVGQ-DQKRLGALIVPNFEELEKWAKESGVKlanDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF 451
|
570
....*....|....*
gi 1935119612 637 TpETGLVTDAFKLKR 651
Cdd:cd17640 452 I-ENGEMTQTMKIKR 465
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
84-623 |
2.69e-65 |
|
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: 225.38 E-value: 2.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 84 WLNYEDinqRVNHFGRGLAAQGLKPKSAIAIFCETRAEW---MIAAQTCFKYNFPLvtlYATLGEEAVTYGLNESGASYL 160
Cdd:cd17641 14 WADYAD---RVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALSLGI---YQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 161 ITSVELLESKLKPALSEIPGLKHIIYVDKKTINKSEYPEgleIHSMQTVEELG-----AKPENLDIPPSKPVPTDLALIM 235
Cdd:cd17641 88 IAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPR---LISFEDVVALGraldrRDPGLYEREVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 236 YTSGSTGRPKGVMMIHKNLIaGMTGQCERIPELGPKDTYVGYLPLAHVLE--LTAEISCVTYGCRIGYSSPLTLsdqssk 313
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFL-GHCAAYLAADPLGPGDEYVSVLPLPWIGEqmYSVGQALVCGFIVNFPEEPETM------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 314 ikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYD--YK-LEQIKRGYDAP--------LCNIL 382
Cdd:cd17641 238 -----MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKlgLRaLDRGKRGRPVSlwlrlaswLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 LFKKVKALLG-GNVRMMLSGGAPLSPQTQRF---MNIcfccPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKL 458
Cdd:cd17641 313 LFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 459 RDwqeggytcrdkpnpRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 538
Cdd:cd17641 389 DE--------------VGEILVRSPGVFVGYYKNPEATAE-DFDEDG--WLHTGDAGYFKENGHLVVIDRAKDVGTTSDG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 539 EYVSLGKVETALKNCPFIDNICAYAKsDQSYVISFVVPNQKKLTVLAEQKGVK-GTWVEICNNPIMEAEILKEIKEV--- 614
Cdd:cd17641 452 TRFSPQFIENKLKFSPYIAEAVVLGA-GRPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVnas 530
|
570
....*....|
gi 1935119612 615 -ADKMKLERF 623
Cdd:cd17641 531 lPEAQRIRRF 540
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
83-661 |
1.68e-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: 220.07 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:COG0318 23 RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 svellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvptdlALIMYTSGSTG 242
Cdd:COG0318 103 ---------------------------------------------------------------------ALILYTSGTTG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 243 RPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVLELTAEI-SCVTYGCRI---GYSSPLTLSDQsskIKKGs 318
Cdd:COG0318 114 RPKGVMLTHRNLLANAAAIAAALG-LTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLvllPRFDPERVLEL---IERE- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 319 kgdctvlKPTLMAAVPEIMDRIyknvmskvqeMNYIQRtlfkigydykleqikRGYDAPlcnillfkkvkallggNVRMM 398
Cdd:COG0318 189 -------RVTVLFGVPTMLARL----------LRHPEF---------------ARYDLS----------------SLRLV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 399 LSGGAPLSPQT-QRFMNiCFCCPVGQGYGLTETCGAGTIT--EVSDYSTGRVGAPLICCEIKLRDwqEGGYTCrdKPNPR 475
Cdd:COG0318 221 VSGGAPLPPELlERFEE-RFGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVD--EDGREL--PPGEV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 476 GEIIIGGPNVSMGYFKNEEKTEDfsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVETALKNCPF 555
Cdd:COG0318 296 GEIVVRGPNVMKGYWNDPEATAE--AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAHPG 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 556 IDNICAYAKSDQSY---VISFVVPNqkkltvlaeqKGVKGTwveicnnpimEAEILKEIKEvadkmKLERFETPIKVRLS 632
Cdd:COG0318 371 VAEAAVVGVPDEKWgerVVAFVVLR----------PGAELD----------AEELRAFLRE-----RLARYKVPRRVEFV 425
|
570 580 590
....*....|....*....|....*....|
gi 1935119612 633 PE-PWTPeTGlvtdafKLKRKELKNHYLND 661
Cdd:COG0318 426 DElPRTA-SG------KIDRRALRERYAAG 448
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
85-560 |
1.03e-59 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 208.22 E-value: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLEsKLKPALSEIPGLKHIIYVDkktiNKSEYPEGLEihsmQTVEELGAKPENLDIPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:cd05911 91 DGLE-KVKEAAKELGPKDKIIVLD----DKPDGVLSIE----DLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIPE-LGPKDTYVGYLPLAHVLELTAEISCVTYGCrigysspltlsdqsskikkgskgdcT 323
Cdd:cd05911 162 KGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLNGA-------------------------T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 324 VLkptlmaavpeIMDRIYKNVMskvqeMNYIQRtlfkigydYKleqIKRGYDAPLCNILLFK---KVKALLGgNVRMMLS 400
Cdd:cd05911 217 VI----------IMPKFDSELF-----LDLIEK--------YK---ITFLYLVPPIAAALAKsplLDKYDLS-SLRVILS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 401 GGAPLSPQTQRFMNICFC-CPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTcrdKPNPRGEII 479
Cdd:cd05911 270 GGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSL---GPNEPGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 480 IGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNI 559
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKE-TFDEDG--WLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHPGVADA 422
|
.
gi 1935119612 560 C 560
Cdd:cd05911 423 A 423
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
230-587 |
4.46e-55 |
|
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: 191.34 E-value: 4.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAgMTGQCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCRI---GYSSPLT 306
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 307 LSDqssKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmskvqemnyiqrtlfkigydykLEQIK-RGYDAPlcnillfk 385
Cdd:cd04433 80 ALE---LIER--------EKVTILLGVPTLLARL--------------------------LKAPEsAGYDLS-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 386 kvkallggNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGR--VGAPLICCEIKLRDwQE 463
Cdd:cd04433 115 --------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPVPGVEVRIVD-PD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 464 GGytcRDKPNPRGEIIIGGPNVSMGYFKNEEKTEDFsvDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 543
Cdd:cd04433 186 GG---ELPPGEIGELVVRGPSVMKGYWNNPEATAAV--DEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVYP 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1935119612 544 GKVETALKNCPFIDNICAYAKSDQSY---VISFVVPNQKKlTVLAEQ 587
Cdd:cd04433 258 AEVEAVLLGHPGVAEAAVVGVPDPEWgerVVAVVVLRPGA-DLDAEE 303
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
80-658 |
3.04e-54 |
|
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: 193.84 E-value: 3.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASY 159
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 LITSvellesKLKPALSEIPGLkhiiyvdkktinkseyPEGLEIHSMQTVEELGAKPENLDI----PPSK----PVPTDL 231
Cdd:cd05932 82 LFVG------KLDDWKAMAPGV----------------PEGLISISLPPPSAANCQYQWDDLiaqhPPLEerptRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 232 ALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTA-EISCVTYGCRIGYSSPLTLSDQ 310
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 311 sskikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKV--QEMNyiqrTLFKIgydykleqikrgydaPLCNILLFKKVK 388
Cdd:cd05932 219 ----------DVQRARPTLFFSVPRLWTKFQQGVQDKIpqQKLN----LLLKI---------------PVVNSLVKRKVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 389 ALLGGN-VRMMLSGGAPLSPQTQRF-----MNICfccpvgQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLrdwq 462
Cdd:cd05932 270 KGLGLDqCRLAGCGSAPVPPALLEWyrslgLNIL------EAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 463 eggytcrdkpNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVS 542
Cdd:cd05932 340 ----------SEDGEILVRSPALMMGYYKDPEATAE-AFTADG--FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 543 LGKVETALKNCPFIDNICAYAkSDQSYVISFVVPNQKkltvlAEQKGVKGTWVEIcnnpimEAEILKEIKEVadKMKLER 622
Cdd:cd05932 407 PAPIENKLAEHDRVEMVCVIG-SGLPAPLALVVLSEE-----ARLRADAFARAEL------EASLRAHLARV--NSTLDS 472
|
570 580 590
....*....|....*....|....*....|....*.
gi 1935119612 623 FETPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHY 658
Cdd:cd05932 473 HEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
85-585 |
3.82e-54 |
|
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: 192.27 E-value: 3.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSv 164
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgaKPEnldippskpvptDLALIMYTSGSTGRP 244
Cdd:cd05914 87 --------------------------------------------------DED------------DVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGqCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYgcrigYSSPLTLSDQ--SSKIKKGSKGDc 322
Cdd:cd05914 105 KGVMLTYRNIVSNVDG-VKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLL-----NGAHVVFLDKipSAKIIALAFAQ- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 323 tvLKPTLMAAVPEIMDRIYKNVmskVQEMNYIQRTLFKIGYDYKLEQIKRgydaplcniLLFKKVKALLGGNVRMMLSGG 402
Cdd:cd05914 178 --VTPTLGVPVPLVIEKIFKMD---IIPKLTLKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 403 APLSPQTQRF---MNICFCcpvgQGYGLTET----CGAGTITEVSDySTGRVgapLICCEIKLrdwqeggytcrDKPNPR 475
Cdd:cd05914 244 AKINPDVEEFlrtIGFPYT----IGYGMTETapiiSYSPPNRIRLG-SAGKV---IDGVEVRI-----------DSPDPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 476 ---GEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKN 552
Cdd:cd05914 305 tgeGEIIVRGPNVMKGYYKNPEATAE-AFDKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINN 381
|
490 500 510
....*....|....*....|....*....|...
gi 1935119612 553 CPFIdnicayaksdqsyVISFVVPNQKKLTVLA 585
Cdd:cd05914 382 MPFV-------------LESLVVVQEKKLVALA 401
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
37-554 |
1.58e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 191.94 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 37 TLDKLFDHAVAKFGKKdclgtrEILSEEnemqpnGKVFkklilgnyrwlNYEDINQRVNHFGRGLAAQGLKPKSAIAIFC 116
Cdd:PRK06187 7 TIGRILRHGARKHPDK------EAVYFD------GRRT-----------TYAELDERVNRLANALRALGVKKGDRVAVFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 117 ETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVELLESkLKPALSEIPGLKHIIYVDKKTiNKSE 196
Cdd:PRK06187 64 WNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPL-LAAILPQLPTVRTVIVEGDGP-AAPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 197 YPEGLEIHSMqtveeLGAKPENLDIPPSKPvpTDLALIMYTSGSTGRPKGVMMIHKNLIAgMTGQCERIPELGPKDTYVG 276
Cdd:PRK06187 142 APEVGEYEEL-----LAAASDTFDFPDIDE--NDAAAMLYTSGTTGHPKGVVLSHRNLFL-HSLAVCAWLKLSRDDVYLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 277 YLPLAHVLELTAEISCVTYGCRIGYS---SPLTLSDQsskIKKgskgdctvLKPTLMAAVPEIMdriyknvmskvqemNY 353
Cdd:PRK06187 214 IVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPTIW--------------QM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 354 IQRTLFKIGYDYkleqikrgydaplcnillfkkvkallgGNVRMMLSGGAPLSPQT-QRFMNIcFCCPVGQGYGLTETCG 432
Cdd:PRK06187 269 LLKAPRAYFVDF---------------------------SSLRLVIYGGAALPPALlREFKEK-FGIDLVQGYGMTETSP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 433 AGTIT----EVSDYST--GRVGAPLICCEIKLRDwQEGgytcRDKPNPR---GEIIIGGPNVSMGYFKNEEKTEDFSVDE 503
Cdd:PRK06187 321 VVSVLppedQLPGQWTkrRSAGRPLPGVEARIVD-DDG----DELPPDGgevGEIIVRGPWLMQGYWNRPEATAETIDGG 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1935119612 504 ngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCP 554
Cdd:PRK06187 396 ----WLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELEDALYGHP 441
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
83-533 |
2.20e-49 |
|
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: 179.30 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 SVELlesklkpalseipglkhiiyvdkktinkseypegleihsmqtvEELGAKPENLDIPPSkPVPTDLALIMYTSGSTG 242
Cdd:cd05936 103 AVSF-------------------------------------------TDLLAAGAPLGERVA-LTPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 243 RPKGVMMIHKNLIAGMTgQCERIPE--LGPKDTYVGYLPLAHVLELTAeisCVTYGCRIGYS-------SPLTLSDQssk 313
Cdd:cd05936 139 VPKGAMLTHRNLVANAL-QIKAWLEdlLEGDDVVLAALPLFHVFGLTV---ALLLPLALGATivliprfRPIGVLKE--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 314 IKKGskgdctvlKPTLMAAVPeimdriyknvmskvqemnyiqrTLFkIGydykleqikrgydaplcnILLFKKVKALLGG 393
Cdd:cd05936 212 IRKH--------RVTIFPGVP----------------------TMY-IA------------------LLNAPEFKKRDFS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 394 NVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYS-TGRVGAPLICCEIKLRDWQeggytcrDKP 472
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVDDD-------GEE 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 473 NPR---GEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:cd05936 316 LPPgevGELWVRGPQVMKGYWNRPEETAEAFVDG----WLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
80-558 |
2.60e-48 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 179.09 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRW--LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAA-QTCFKYNFpLVTLYATLGEEAVTYGLNESG 156
Cdd:cd05933 2 RGDKWhtLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAvGAIFAGGI-AVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLESKLKPALSEIPGLKHIIyvdkktINKSEYPEGL-EIHSMQTVEELG--AKPENLDIPPSKPVPTDLAL 233
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAII------QYKEPLKEKEpNLYSWDEFMELGrsIPDEQLDAIISSQKPNQCCT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 234 IMYTSGSTGRPKGVMMIHKNL--IAGMTGQCERI--PELGpKDTYVGYLPLAHVLELTAEI-SCVTYGCRIGYSSPLTLs 308
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNItwTAKAASQHMDLrpATVG-QESVVSYLPLSHIAAQILDIwLPIKVGGQVYFAQPDAL- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 309 dqsskikKGSKGDcTV--LKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLF----KIGYDYKLEQIKRGYDAPLC--- 379
Cdd:cd05933 233 -------KGTLVK-TLreVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLMGGESPSPLFyrl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 380 -NILLFKKVKALLG-GNVRMMLSGGAPLSPQTQRF---MNIcfccPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICC 454
Cdd:cd05933 305 aKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAYRLLSCGKALPGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 455 EIKLrdwqeggytcrDKPNPR--GEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDL 532
Cdd:cd05933 381 KTKI-----------HNPDADgiGEICFWGRHVFMGYLNMEDKTEE-AIDEDG--WLHSGDLGKLDEDGFLYITGRIKEL 446
|
490 500
....*....|....*....|....*..
gi 1935119612 533 VKLQAGEYVSLGKVETALKN-CPFIDN 558
Cdd:cd05933 447 IITAGGENVPPVPIEDAVKKeLPIISN 473
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
196-644 |
2.65e-45 |
|
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: 170.33 E-value: 2.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 196 EYPEGLEIHSMQTVEELGAKPENLDIPPSKPVPtdLALIMYTSGSTGRPKGVMMIHKNLI-AGMTGQCERIPELGPKDTy 274
Cdd:cd17632 192 AVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDP--LALLIYTSGSTGTPKGAMYTERLVAtFWLKVSSIQDIRPPASIT- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 275 VGYLPLAHVLELTAEISCVTYGcRIGYSSPLtlSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIYknvmskvqemnyi 354
Cdd:cd17632 269 LNFMPMSHIAGRISLYGTLARG-GTAYFAAA--SDMSTLFD-----DLALVRPTELFLVPRVCDMLF------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 355 QRtlfkigydYKLEQIKR---GYDAplcnILLFKKVKA-----LLGGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYG 426
Cdd:cd17632 328 QR--------YQAELDRRsvaGADA----ETLAERVKAelrerVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 427 LTEtcgAGTITevsdySTGRVGAPLICcEIKLRDWQEGGYTCRDKPNPRGEIIIGGPNVSMGYFKNEEKTEDFsVDENGq 506
Cdd:cd17632 396 STE---AGAVI-----LDGVIVRPPVL-DYKLVDVPELGYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAEV-FDEDG- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 507 rWFCTGDI-GEFHPDGcLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSYVISFVVPNQKKLTVLA 585
Cdd:cd17632 465 -FYRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGED 542
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1935119612 586 EQKgvkgtwveicnnpiMEAEILKEIKEVADKMKLERFETPIKVRLSPEPWTPETGLVT 644
Cdd:cd17632 543 TAR--------------LRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
188-669 |
3.08e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 166.43 E-value: 3.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 188 DKKTINK----SEYPEGLEIHSMQTVEELGAKPENLDIPPSKPvpTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCE 263
Cdd:PTZ00342 261 DKEKLEKikdlKEKAKKLGISIILFDDMTKNKTTNYKIQNEDP--DFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 264 R--IPELGPKdTYVGYLPLAHVLELTAEISCVTYGCRIgysspltlsDQSSK-IKKGSKgDCTVLKPTLMAAVPEIMDRI 340
Cdd:PTZ00342 339 HsiFKKYNPK-THLSYLPISHIYERVIAYLSFMLGGTI---------NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 341 YKNVMSKVQEMNYIQRTLFKigydyKLEQIKRG-YDAPLCNIL-----LFKKVKALLGGNVRMMLSGGAPLSPQTQR--- 411
Cdd:PTZ00342 408 YTNIMTEINNLPPLKRFLVK-----KILSLRKSnNNGGFSKFLegithISSKIKDKVNPNLEVILNGGGKLSPKIAEels 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 412 -FMNICFCcpvgQGYGLTETCGAGTITEVSDYSTGRVGAPlIC--CEIKLRDWQEggYTCRDKPnPRGEIIIGGPNVSMG 488
Cdd:PTZ00342 483 vLLNVNYY----QGYGLTETTGPIFVQHADDNNTESIGGP-ISpnTKYKVRTWET--YKATDTL-PKGELLIKSDSIFSG 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 489 YFKNEEKTED-FSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVETALKNCPFIDNICAYAksDQ 567
Cdd:PTZ00342 555 YFLEKEQTKNaFTED----GYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYG--DD 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 568 SY-----VISfvVPNQKKLTVLAEQKGVKGTWV-----------EICNNPIMEAEILKEIKEVADKMKLERFETPIKVRL 631
Cdd:PTZ00342 629 SMdgplaIIS--VDKYLLFKCLKDDNMLESTGIneknylekltdETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDIYL 706
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1935119612 632 SPEPWTpETGLVTDAFKLKRKELKNHY---LNDIERMYGGK 669
Cdd:PTZ00342 707 TSKVWD-TNNYLTPTFKVKRFYVFKDYaffIDQVKKIYKNK 746
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
84-656 |
1.52e-41 |
|
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: 157.86 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 84 WLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMI---AAQTCFKYNFPLVTLYAtlgEEAVTYGLNESGASYL 160
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVaflAAARAGAVVAPLNPAYK---KAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 161 ITSVELLESKLKPALSEIPGLKHIiYVDKKTinKSEYPEGleihsmqtvEELGAKPENLDIPPSKPVPT--DLALIMYTS 238
Cdd:cd05926 91 LTPKGELGPASRAASKLGLAILEL-ALDVGV--LIRAPSA---------ESLSNLLADKKNAKSEGVPLpdDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 239 GSTGRPKGVMMIHKNLIAGMTGQCeRIPELGPKDTYVGYLPLAHVLELTAEI--SCVTYGCrigysspLTLSDQSSkikk 316
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNIT-NTYKLTPDDRTLVVMPLFHVHGLVASLlsTLAAGGS-------VVLPPRFS---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 317 GSK--GDCTVLKPTLMAAVPEIMDRIYKNVMSKvqemnyiqrtlfkigydykleqiKRGYDAPLcnillfkkvkallggn 394
Cdd:cd05926 227 ASTfwPDVRDYNATWYTAVPTIHQILLNRPEPN-----------------------PESPPPKL---------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 395 vRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTIT--EVSDYSTGRVGAPLiccEIKLRDWQEGGYTCrdKP 472
Cdd:cd05926 268 -RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPV---GVEVRILDEDGEIL--PP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 473 NPRGEIIIGGPNVSMGYFKNEEKT-EDFSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALK 551
Cdd:cd05926 342 GVVGEICLRGPNVTRGYLNNPEANaEAAFKD----GWFRTGDLGYLDADGYLFLTGRIKELIN-RGGEKISPLEVDGVLL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 552 NCPFIDNICAYAKSDQSY---VISFVVPNQKKltvlaeqkgvkgtwveicnnPIMEAEILKEIKEvadkmKLERFETPIK 628
Cdd:cd05926 417 SHPAVLEAVAFGVPDEKYgeeVAAAVVLREGA--------------------SVTEEELRAFCRK-----HLAAFKVPKK 471
|
570 580
....*....|....*....|....*....
gi 1935119612 629 VRLSPE-PWTPeTGlvtdafKLKRKELKN 656
Cdd:cd05926 472 VYFVDElPKTA-TG------KIQRRKVAE 493
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
85-534 |
2.03e-40 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 155.09 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEwmiaaqtcfkynFPLVTLYAT-LGeeAVTYGLN---------- 153
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIE------------FPVAFLAVLsLG--AVVTTANplstpaeiak 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 154 ---ESGASYLITSVELLEsKLKPALSEIpglkhiIYVDkktinksEYPEGLEIHSMQTVEELGAKPENLDIPPSkpvptD 230
Cdd:cd05904 99 qvkDSGAKLAFTTAELAE-KLASLALPV------VLLD-------SAEFDSLSFSDLLFEADEAEPPVVVIKQD-----D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 231 LALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERI-PELGPKDTYVGYLPLAHVLELTaeiSCVTYGCRIG--------Y 301
Cdd:cd05904 160 VAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLS---SFALGLLRLGatvvvmprF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 302 SSPLTLSdqssKIKKgskgdctvLKPTLMAAVPEIMDRIYKNVMSKvqemnyiqrtlfkigydykleqikrGYDaplcni 381
Cdd:cd05904 237 DLEELLA----AIER--------YKVTHLPVVPPIVLALVKSPIVD-------------------------KYD------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 382 llfkkVKALlggnvRMMLSGGAPLSPQT-----QRFMNicfcCPVGQGYGLTETCGAGTITEVSDYSTGRVG-----APL 451
Cdd:cd05904 274 -----LSSL-----RQIMSGAAPLGKELieafrAKFPN----VDLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 452 IccEIKLRDWQEGGYTcrdKPNPRGEIIIGGPNVSMGYFKNEEKTEdFSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 531
Cdd:cd05904 340 V--EAKIVDPETGESL---PPNQTGELWIRGPSIMKGYLNNPEATA-ATIDKEG--WLHTGDLCYIDEDGYLFIVDRLKE 411
|
...
gi 1935119612 532 LVK 534
Cdd:cd05904 412 LIK 414
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
87-575 |
5.11e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 153.19 E-value: 5.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 87 YEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSvel 166
Cdd:PRK03640 30 FMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 167 lesklkpalseipglkhiiyvdkktinkSEYPEGLEIHSMQTVEELGAKPENlDIPPSKPVP-TDLALIMYTSGSTGRPK 245
Cdd:PRK03640 107 ----------------------------DDFEAKLIPGISVKFAELMNGPKE-EAEIQEEFDlDEVATIMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 246 GVMMIHKNLIAGMTGQCEripELG--PKDTYVGYLPLAHVLELTAEISCVTYGCRIgyssplTLSDQ--SSKIKKGSKGD 321
Cdd:PRK03640 158 GVIQTYGNHWWSAVGSAL---NLGltEDDCWLAAVPIFHISGLSILMRSVIYGMRV------VLVEKfdAEKINKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 322 ctvlKPTLMAAVPeimdriyknVMskvqemnyIQRTLFKIGydykleqiKRGYDAplcnillfkkvkallggNVRMMLSG 401
Cdd:PRK03640 229 ----GVTIISVVS---------TM--------LQRLLERLG--------EGTYPS-----------------SFRCMLLG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 402 GAPLSPQT-----QRfmNIcfccPVGQGYGLTETCgAGTITEVSDYST---GRVGAPLICCEIKLRDwqeGGYTCrdKPN 473
Cdd:PRK03640 263 GGPAPKPLleqckEK--GI----PVYQSYGMTETA-SQIVTLSPEDALtklGSAGKPLFPCELKIEK---DGVVV--PPF 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 474 PRGEIIIGGPNVSMGYFKNEEKTEDfsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVETALKNC 553
Cdd:PRK03640 331 EEGEIVVKGPNVTKGYLNREDATRE--TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSH 405
|
490 500
....*....|....*....|....*
gi 1935119612 554 PFIDNICAYAKSDQSY---VISFVV 575
Cdd:PRK03640 406 PGVAEAGVVGVPDDKWgqvPVAFVV 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
85-533 |
9.52e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 150.44 E-value: 9.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAqtcfkynFPLVTLYATL--------GEEAvTYGLNESG 156
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAA-------LGALKAGAVVvplntrytADEA-AYILARGD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLESkLKPALSEIPGLKHIIYVdkktinksEYPEGLEIHS-MQTVEELGAKPENLDIPPSKpVPTDLALIM 235
Cdd:PRK07656 103 AKALFVLGLFLGV-DYSATTRLPALEHVVIC--------ETEEDDPHTEkMKTFTDFLAAGDPAERAPEV-DPDDVADIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 236 YTSGSTGRPKGVMMIHKNLIAGMTGQCErIPELGPKDTYVGYLPLAHVLELTAeiscvtygcriGYSSPLtlsdqsskik 315
Cdd:PRK07656 173 FTSGTTGRPKGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKA-----------GVNAPL---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 316 kgSKGdCTVLkPTLMAAVPEIMDRIYK---NVMSKVQEMnyiqrtlfkigYDYKLEQIKRGYDAplcnillFKkvkallg 392
Cdd:PRK07656 231 --MRG-ATIL-PLPVFDPDEVFRLIETeriTVLPGPPTM-----------YNSLLQHPDRSAED-------LS------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 393 gNVRMMLSGGAPLSPQ-TQRFMNICFCCPVGQGYGLTETCGAGTITEVSD---YSTGRVGAPLICCEIKLRDwqEGGYTC 468
Cdd:PRK07656 282 -SLRLAVTGAASMPVAlLERFESELGVDIVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEV 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1935119612 469 rdKPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:PRK07656 359 --PVGEVGELLVRGPNVMKGYYDDPEATAA-AIDADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
77-550 |
3.34e-34 |
|
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: 135.43 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWLnYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESG 156
Cdd:cd17631 14 LVFGGRSLT-YAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITsvellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvptDLALIMY 236
Cdd:cd17631 93 AKVLFD-------------------------------------------------------------------DLALLMY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 237 TSGSTGRPKGVMMIHKNL-----IAGMTGqceripELGPKDTYVGYLPLAHVLELtaeiscvtyGCrigYSSPLTLSDQS 311
Cdd:cd17631 106 TSGTTGRPKGAMLTHRNLlwnavNALAAL------DLGPDDVLLVVAPLFHIGGL---------GV---FTLPTLLRGGT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 312 SKIKKGSKGDcTVL------KPTLMAAVPEIMDRIyknvmskvqemnyIQRTLFkigydykleqikRGYDAPlcnillfk 385
Cdd:cd17631 168 VVILRKFDPE-TVLdlierhRVTSFFLVPTMIQAL-------------LQHPRF------------ATTDLS-------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 386 kvkallggNVRMMLSGGAPLSPQTQRFMnICFCCPVGQGYGLTETCGAGTITEVSDYST--GRVGAPLICCEIKLRDwqE 463
Cdd:cd17631 214 --------SLRAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD--P 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 464 GGYTCrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDenGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSL 543
Cdd:cd17631 283 DGREV--PPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD--G--WFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYP 355
|
....*..
gi 1935119612 544 GKVETAL 550
Cdd:cd17631 356 AEVEDVL 362
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
224-579 |
1.69e-32 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 130.16 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 224 SKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCEripELG--PKDTYVGYLPLAHVLELTAEISCVTYGCRIgy 301
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSAL---NLGltEDDNWLCALPLFHISGLSILMRSVIYGMTV-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 302 ssplTLSDQ--SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvmskvqemnyiqrtlfkigydykLEQIKRGYDAplc 379
Cdd:cd05912 147 ----YLVDKfdAEQVLHLINSG----KVTIISVVPTMLQRL--------------------------LEILGEGYPN--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 380 nillfkkvkallggNVRMMLSGGAPLSP---QTQRFMNIcfccPVGQGYGLTETCG-AGTIT-EVSDYSTGRVGAPLICC 454
Cdd:cd05912 190 --------------NLRCILLGGGPAPKpllEQCKEKGI----PVYQSYGMTETCSqIVTLSpEDALNKIGSAGKPLFPV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 455 EIKLRDwqEGGytcrdKPNPRGEIIIGGPNVSMGYFKNEEKTEdfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 534
Cdd:cd05912 252 ELKIED--DGQ-----PPYEVGEILLKGPNVTKGYLNRPDATE--ESFENG--WFKTGDIGYLDEEGFLYVLDRRSDLI- 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1935119612 535 LQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSY---VISFVVPNQK 579
Cdd:cd05912 320 ISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvPVAFVVSERP 367
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
226-576 |
2.94e-32 |
|
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: 129.81 E-value: 2.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 226 PVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVleltaeiscvtygcrIGYSSPL 305
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG-LGPGDVFLVASPMAHQ---------------TGFVYGF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 TLSdqsskikkgskgdctvlkptLMAAVPEIMDRIYkNVMSKVQEMNYiQRTLFKIGYDYKLEQIKRGYD---APLCNIl 382
Cdd:cd05903 154 TLP--------------------LLLGAPVVLQDIW-DPDKALALMRE-HGVTFMMGATPFLTDLLNAVEeagEPLSRL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 lfkkvkallggnvRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSD-----YSTGRVGAPLiccEIK 457
Cdd:cd05903 211 -------------RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrlYTDGRPLPGV---EIK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 458 LRDwqegGYTCRDKPNPRGEIIIGGPNVSMGYFKNEEKTEDFsvDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQA 537
Cdd:cd05903 275 VVD----DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADA--APEG--WFRTGDLARLDEDGYLRITGRSKDII-IRG 345
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1935119612 538 GEYVSLGKVETALKNCPFIDNICAYAKSDQ---SYVISFVVP 576
Cdd:cd05903 346 GENIPVLEVEDLLLGHPGVIEAAVVALPDErlgERACAVVVT 387
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
77-566 |
6.63e-32 |
|
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: 130.29 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNyRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIA------AQTCFKYNFPLvtlyatLGEEAVTY 150
Cdd:TIGR03098 19 LVHHD-RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAmfgaalAGGVFVPINPL------LKAEQVAH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 151 GLNESGASYLITSVELLEsKLKPALSEIPGLKHIIYVDKKTiNKSEYPEGLEIHSMQTVEELGAKpenldIPPSKPVPTD 230
Cdd:TIGR03098 92 ILADCNVRLLVTSSERLD-LLHPALPGCHDLRTLIIVGDPA-HASEGHPGEEPASWPKLLALGDA-----DPPHPVIDSD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 231 LALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDQ 310
Cdd:TIGR03098 165 MAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYL-ENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 311 SSKIKKGskgdctvlKPTLMAAVPEImdriyknvmskvqemnYIQrtLFKIgyDYKLEqikrgyDAPLCNILlfkkvkAL 390
Cdd:TIGR03098 244 LKALEKH--------GITGLAAVPPL----------------WAQ--LAQL--DWPES------AAPSLRYL------TN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 391 LGGNV-RMMLSGGAPLSPQTQRFMNicfccpvgqgYGLTETCGAGTI-TEVSDYSTGRVGAPLICCEIKLrdWQEGGYTC 468
Cdd:TIGR03098 284 SGGAMpRATLSRLRSFLPNARLFLM----------YGLTEAFRSTYLpPEEVDRRPDSIGKAIPNAEVLV--LREDGSEC 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 469 rdKPNPRGEIIIGGPNVSMGYFKNEEKT-EDFSVDENGQR---------WfcTGDIGEFHPDGCLQIIDRKKDLVKlQAG 538
Cdd:TIGR03098 352 --APGEEGELVHRGALVAMGYWNDPEKTaERFRPLPPFPGelhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIK-TSG 426
|
490 500
....*....|....*....|....*...
gi 1935119612 539 EYVSLGKVETALKNCPFIDNICAYAKSD 566
Cdd:TIGR03098 427 YRVSPTEVEEVAYATGLVAEAVAFGVPD 454
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
221-558 |
6.13e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 127.81 E-value: 6.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 221 IPPSKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIA-GMTGQCeRIPELGPKD-TYVGYLPLAHVLELTAeisCVTYGCR 298
Cdd:PRK05605 211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKA-WVPGLGDGPeRVLAALPMFHAYGLTL---CLTLAVS 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 299 IG--------YSSPLTLsdqsSKIKKGskgdctvlKPTLMAAVPEimdrIYKNVMSKVQEmnyiqrtlfkigydykleqi 370
Cdd:PRK05605 287 IGgelvllpaPDIDLIL----DAMKKH--------PPTWLPGVPP----LYEKIAEAAEE-------------------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 371 kRGYDaplcnillfkkvkalLGGnVRMMLSGGAPLSPQTqrfmnicfccpVGQ-----------GYGLTETCGAGTITEV 439
Cdd:PRK05605 331 -RGVD---------------LSG-VRNAFSGAMALPVST-----------VELwekltggllveGYGLTETSPIIVGNPM 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 440 SDYS-TGRVGAPLICCEIKLRDWQEGGytcRDKPN-PRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEF 517
Cdd:PRK05605 383 SDDRrPGYVGVPFPDTEVRIVDPEDPD---ETMPDgEEGELLVRGPQVFKGYWNRPEETAKSFLDG----WFRTGDVVVM 455
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1935119612 518 HPDGCLQIIDRKKDLVkLQAGEYVSLGKVETALKNCPFIDN 558
Cdd:PRK05605 456 EEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
85-577 |
8.60e-31 |
|
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: 126.67 E-value: 8.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITsv 164
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellESKLKPalsEIPGLKHIIYVDKKTInkSEYPEgleihsmqtveelgakpENLDiPPSKPvpTDLALIMYTSGSTGRP 244
Cdd:cd17655 101 ---QSHLQP---PIAFIGLIDLLDEDTI--YHEES-----------------ENLE-PVSKS--DDLAYVIYTSGSTGKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPL---AHVLELTAeiscvtygcrigyssPLTLSDQSSKIKKGSKGD 321
Cdd:cd17655 153 KGVMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIsfdASVTEIFA---------------SLLSGNTLYIVRKETVLD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 322 CTVLkptlmaavpeimdriyknvmskvqeMNYIQrtlfkigyDYKLEQIkrgyDAPLCNILLFKKVKALLGGNVRMMLSG 401
Cdd:cd17655 217 GQAL-------------------------TQYIR--------QNRITII----DLTPAHLKLLDAADDSEGLSLKHLIVG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 402 GAPLSPQTQRFMNICFC--CPVGQGYGLTETCGAGTI--TEVSDYSTGRV--GAPLICCEIKLRDwQEGgytcrdKPNP- 474
Cdd:cd17655 260 GEALSTELAKKIIELFGtnPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYG------RPQPv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 475 --RGEIIIGGPNVSMGYFKNEEKT-EDFSVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETA 549
Cdd:cd17655 333 gvAGELYIGGEGVARGYLNRPELTaEKFVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR-GYRIELGEIEAR 411
|
490 500 510
....*....|....*....|....*....|.
gi 1935119612 550 LKNCPFIDNICAYAKSDQS---YVISFVVPN 577
Cdd:cd17655 412 LLQHPDIKEAVVIARKDEQgqnYLCAYIVSE 442
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
87-561 |
8.43e-30 |
|
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: 122.37 E-value: 8.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 87 YEDINQRVNHFGRGL-AAQGLKPKSAIAIFCEtRAEWMIAAQ-TCFK----YnFPLVTLYAtlgEEAVTYGLNESGASYL 160
Cdd:TIGR01733 2 YRELDERANRLARHLrAAGGVGPGDRVAVLLE-RSAELVVAIlAVLKagaaY-VPLDPAYP---AERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 161 ITSVELLESKLKPALSEIPglkhiiyVDkktinkseypegleihsmQTVEELGAKPENLDIPPSKPVPTDLALIMYTSGS 240
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVIL-------LD------------------PLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 241 TGRPKGVMMIHKNLIAgMTGQCERIPELGPKDTYVGYLPLAH---VLELTAeiscvtygcrigyssPLTLsdqsskikkg 317
Cdd:TIGR01733 132 TGRPKGVVVTHRSLVN-LLAWLARRYGLDPDDRVLQFASLSFdasVEEIFG---------------ALLA---------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 318 skGDCTVLKPT----LMAAVPEIMDRIYK-NVMSKVqemnyiqRTLFKigydykleqikrgydaplcnilLFKKVKALLG 392
Cdd:TIGR01733 186 --GATLVVPPEdeerDDAALLAALIAEHPvTVLNLT-------PSLLA----------------------LLAAALPPAL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 393 GNVRMMLSGGAPLSPQT-----QRFMNICFCcpvgQGYGLTETCGAGTITEVSDYSTGR-----VGAPLICCEIKLRDwQ 462
Cdd:TIGR01733 235 ASLRLVILGGEALTPALvdrwrARGPGARLI----NLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRLYVLD-D 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 463 EGgytcrdKPNPR---GEIIIGGPNVSMGYFKNEEKT-----EDFSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVK 534
Cdd:TIGR01733 310 DL------RPVPVgvvGELYIGGPGVARGYLNRPELTaerfvPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVK 383
|
490 500
....*....|....*....|....*..
gi 1935119612 535 LQaGEYVSLGKVETALKNCPFIDNICA 561
Cdd:TIGR01733 384 IR-GYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
83-578 |
2.74e-29 |
|
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: 124.97 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCEtRAEWMIAAqtcfkynfplvtLYATL--G-----------EEAVT 149
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLE-RSLEMVVA------------LLAVLkaGaayvpldpaypAERLA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 150 YGLNESGASYLITsvellESKLKPALSEIPGlkHIIYVDKKTInkSEYPEGLeihsmqtveelgakpenldiPPSKPVPT 229
Cdd:COG1020 567 YMLEDAGARLVLT-----QSALAARLPELGV--PVLALDALAL--AAEPATN--------------------PPVPVTPD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAH---VLELtaeISCVTYGCRIGYSSPLT 306
Cdd:COG1020 618 DLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG-LGPGDRVLQFASLSFdasVWEI---FGALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 307 LSD--------QSSKIkkgskgdcTVLK--PTLMAAVPEimdriyknvmskvqemnyiqrtlfkigydykleqikrgYDA 376
Cdd:COG1020 694 RRDpaalaellARHRV--------TVLNltPSLLRALLD--------------------------------------AAP 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 377 PLCnillfkkvkallgGNVRMMLSGGAPLSPQT-QRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGR----VGAPL 451
Cdd:COG1020 728 EAL-------------PSLRLVLVGGEALPPELvRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsvpIGRPI 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 452 ICCEIKLRDwqEGGytcrdKPNP---RGEIIIGGPNVSMGYFKNEEKTED-FSVD---ENGQRWFCTGDIGEFHPDGCLQ 524
Cdd:COG1020 795 ANTRVYVLD--AHL-----QPVPvgvPGELYIGGAGLARGYLNRPELTAErFVADpfgFPGARLYRTGDLARWLPDGNLE 867
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1935119612 525 IIDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICAYAKSDQS---YVISFVVPNQ 578
Cdd:COG1020 868 FLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAREDAPgdkRLVAYVVPEA 923
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
142-568 |
4.35e-29 |
|
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: 121.28 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 142 TLGEEAVTYGLNESGASYLITSVELLEsKLK-PALSEIPGLKHIIYVD--KKTINKSEYPEGLeIHSMQTVEELgakpen 218
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQFIE-KLKlHHLFDVEYDARIVYLEdlRAKISKADKCKAF-LAGKFPPKWL------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 219 LDIPPSKPV-PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTgQCERIPELGPKDTYVGYLPLAHVLELTaeiSCVTYGC 297
Cdd:cd05909 136 LRIFGVAPVqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFGLT---GCLWLPL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 298 RIG-----YSSPLTLSDQSSKIKKGSkgdCTVL--KPTLMaavpeimdRIYknvmskvqeMNYIQRTLFKigydykleqi 370
Cdd:cd05909 212 LSGikvvfHPNPLDYKKIPELIYDKK---ATILlgTPTFL--------RGY---------ARAAHPEDFS---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 371 krgydaplcnillfkkvkallggNVRMMLSGGAPLSPQT-QRFMNIcFCCPVGQGYGLTETCGAGTI-TEVSDYSTGRVG 448
Cdd:cd05909 262 -----------------------SLRLVVAGAEKLKDTLrQEFQEK-FGIRILEGYGTTECSPVISVnTPQSPNKEGTVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 449 APLICCEIKLRDwQEGGytcrdKPNPRGE---IIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQI 525
Cdd:cd05909 318 RPLPGMEVKIVS-VETH-----EEVPIGEgglLLVRGPNVMLGYLNEPELTSFAFGDG----WYDTGDIGKIDGEGFLTI 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1935119612 526 IDRKKDLVKLqAGEYVSLGKVETAL-KNCPFIDNICAYAKSDQS 568
Cdd:cd05909 388 TGRLSRFAKI-AGEMVSLEAIEDILsEILPEDNEVAVVSVPDGR 430
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
230-587 |
1.11e-28 |
|
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: 119.32 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAgmtgQCERIPEL---GPKDTYVGYLPLAHVLELTAEISCVTYgCRigySSPLT 306
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAA----NVRALVDAwrwTEDDVLLHVLPLHHVHGLVNALLCPLF-AG---ASVEF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 307 LSDQSSKIKKGSKGDCTVlkpTLMAAVPEIMDRIyknvmskvqemnyIQrtlfkigydykleqikrGYDAPLCNILLFKK 386
Cdd:cd05941 162 LPKFDPKEVAISRLMPSI---TVFMGVPTIYTRL-------------LQ-----------------YYEAHFTDPQFARA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 387 VKAllgGNVRMMLSGGAPLSPQT-QRFMNIcfccpVGQG----YGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDw 461
Cdd:cd05941 209 AAA---ERLRLMVSGSAALPVPTlEEWEAI-----TGHTllerYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVD- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 462 QEGGytcrdKPNPR---GEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 538
Cdd:cd05941 280 EETG-----EPLPRgevGEIQVRGPSVFKEYWNKPEATKE-EFTDDG--WFKTGDLGVVDEDGYYWILGRSSVDIIKSGG 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1935119612 539 EYVSLGKVETALKNCPFIDNICAYAKSDQSY---VISFVVPNQKKLTVLAEQ 587
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLRAGAAALSLEE 403
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
227-577 |
1.86e-28 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 118.89 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 227 VPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPkdtyvgylplahvleltaeiscvtyGCRIGYSSPLT 306
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGP-------------------------GDVFLNQAPFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 307 LsdqsskikkgskgDCTV--LKPTLMA-----AVPEIMDRIYKNVMSKVQEMnyiqrtlfkigydykleQIKRGYDAP-- 377
Cdd:cd05945 149 F-------------DLSVmdLYPALASgatlvPVPRDATADPKQLFRFLAEH-----------------GITVWVSTPsf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 378 --LCniLLFKKVKALLGGNVRMMLSGGAPLSPQT-----QRFMNicfcCPVGQGYGLTETCGAGTITEVSDYSTGR---- 446
Cdd:cd05945 199 aaMC--LLSPTFTPESLPSLRHFLFCGEVLPHKTaralqQRFPD----ARIYNTYGPTEATVAVTYIEVTPEVLDGydrl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 447 -VGAPLICCEIKLRDwQEGGYTcrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDENGQRWFCTGDIGEFHPDGCLQI 525
Cdd:cd05945 273 pIGYAKPGAKLVILD-EDGRPV---PPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEADGLLFY 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1935119612 526 IDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICA---YAKSDQSYVISFVVPN 577
Cdd:cd05945 349 RGRLDFQVKLN-GYRIELEEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVPK 402
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
85-578 |
5.26e-28 |
|
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: 117.63 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFK----YnfplVTLYATLGEEAVTYGLNESGASYL 160
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKagaaY----VPLDPSYPAERLAYILEDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 161 ITSvellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvPTDLALIMYTSGS 240
Cdd:cd05930 89 LTD----------------------------------------------------------------PDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 241 TGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLA---HVLELT------AEISCVTYGCRigySSPLTLSD-- 309
Cdd:cd05930 105 TGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSfdvSVWEIFgallagATLVVLPEEVR---KDPEALADll 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 QSSKIkkgskgdcTVLK--PTLMAAVpeimdriyknvmskvqeMNYIQRTLFKigydykleqikrgydaplcnillfkkv 387
Cdd:cd05930 181 AEEGI--------TVLHltPSLLRLL-----------------LQELELAALP--------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 388 kallggNVRMMLSGGAPLSPQT-QRFMNICFCCPVGQGYGLTETCGAGTITEVS--DYSTGRV--GAPLICCEIKLRDwq 462
Cdd:cd05930 209 ------SLRLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATYYRVPpdDEEDGRVpiGRPIPNTRVYVLD-- 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 463 eggytCRDKPNPR---GEIIIGGPNVSMGYFKNEEKTEDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLq 536
Cdd:cd05930 281 -----ENLRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPnpfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKI- 354
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1935119612 537 AGEYVSLGKVETALKNCPFIDNICAYAKSD---QSYVISFVVPNQ 578
Cdd:cd05930 355 RGYRIELGEIEAALLAHPGVREAAVVAREDgdgEKRLVAYVVPDE 399
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
101-639 |
1.19e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.93 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 101 LAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVEL----LESKLKPALS 176
Cdd:PRK06087 66 LLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtrPVDLILPLQN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 177 EIPGLKHIIYVDKktinksEYPEgleiHSMQTVEELGAKPENLDIPPskPVPTD-LALIMYTSGSTGRPKGVMMIHKNLI 255
Cdd:PRK06087 146 QLPQLQQIVGVDK------LAPA----TSSLSLSQIIADYEPLTTAI--TTHGDeLAAVLFTSGTEGLPKGVMLTHNNIL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 256 AGMTGQCERIpELGPKDTYVGYLPLAHVlelTAEISCVTYGCRIGYSSPLTLSDQSSK-IKKGSKGDCTvlkpTLMAAVP 334
Cdd:PRK06087 214 ASERAYCARL-NLTWQDVFMMPAPLGHA---TGFLHGVTAPFLIGARSVLLDIFTPDAcLALLEQQRCT----CMLGATP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 335 EIMDrIYKNVMskvqemnyiqrtlfkigydykleqiKRGYDAPlcnillfkkvkallggNVRMMLSGGAPLSPQT----- 409
Cdd:PRK06087 286 FIYD-LLNLLE-------------------------KQPADLS----------------ALRFFLCGGTTIPKKVarecq 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 410 QRFMNICFCcpvgqgYGLTETCGAGTITevSDYSTGRVGA----PLICCEIKLRDWQEggytcrdKPNPR---GEIIIGG 482
Cdd:PRK06087 324 QRGIKLLSV------YGSTESSPHAVVN--LDDPLSRFMHtdgyAAAGVEIKVVDEAR-------KTLPPgceGEEASRG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 483 PNVSMGYFKNEEKTeDFSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVETALKNCPFIDNICAY 562
Cdd:PRK06087 389 PNVFMGYLDEPELT-ARALDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 563 AKSDQSY---VISFVVP--NQKKLTV------LAEQKGVKGTWVEicnnpimEAEILKEI-KEVADKMKLERFETPIKVR 630
Cdd:PRK06087 465 AMPDERLgerSCAYVVLkaPHHSLTLeevvafFSRKRVAKYKYPE-------HIVVIDKLpRTASGKIQKFLLRKDIMRR 537
|
....*....
gi 1935119612 631 LSPEPWTPE 639
Cdd:PRK06087 538 LTQDVCEEI 546
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
36-533 |
2.16e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 117.22 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 36 DTLDKLFDHAVAKFGKKDCLGTREilseenemqpngkvfkklilGNYRWlNYEDINQRVNHFGRGLAAQGLKPKSAIAIF 115
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRD--------------------QGLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 116 CETRAEWmiaaqtcfkynfpLVTLYAT--LGEEAVT-----------YGLNESGASYLITS--------VELLESkLKPA 174
Cdd:PRK08315 75 APNVPEW-------------VLTQFATakIGAILVTinpayrlseleYALNQSGCKALIAAdgfkdsdyVAMLYE-LAPE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 175 L----------SEIPGLKHIIYV-DKKTINKSEYPEGLEIHSMQTVEELGAKPENLDippskpvPTDLALIMYTSGSTGR 243
Cdd:PRK08315 141 LatcepgqlqsARLPELRRVIFLgDEKHPGMLNFDELLALGRAVDDAELAARQATLD-------PDDPINIQYTSGTTGF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 244 PKGVMMIHKNLI--AGMTGQCERipeLGPKDTYVGYLPLAH----VLeltAEISCVTYGCRIGYssPLTLSDQSSKIKKG 317
Cdd:PRK08315 214 PKGATLTHRNILnnGYFIGEAMK---LTEEDRLCIPVPLYHcfgmVL---GNLACVTHGATMVY--PGEGFDPLATLAAV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 318 SKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIQRTLFkigyDykLEQIKRGYDA-PLCNILLFKKVKAllggn 394
Cdd:PRK08315 286 EEERCTALYgvPTMFIA-----------------ELDHPDFARF----D--LSSLRTGIMAgSPCPIEVMKRVID----- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 395 vRMMLSGgaplspqtqrfMNICfccpvgqgYGLTETCGAGTITEVSD-----YSTgrVGAPLICCEIKLRDwQEGGYTCr 469
Cdd:PRK08315 338 -KMHMSE-----------VTIA--------YGMTETSPVSTQTRTDDplekrVTT--VGRALPHLEVKIVD-PETGETV- 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 470 dKPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:PRK08315 394 -PRGEQGELCTRGYSVMKGYWNDPEKTAE-AIDADG--WMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
87-556 |
2.55e-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: 116.47 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 87 YEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVEL 166
Cdd:cd17642 47 YAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 167 LESKLKPAlSEIPGLKHIIYVDKKTinksEYPEGLEIHSMQTVEELGAKPENLDIPPSKPVPTDLALIMYTSGSTGRPKG 246
Cdd:cd17642 127 LQKVLNVQ-KKLKIIKTIIILDSKE----DYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 247 VMMIHKNLIAGMTGQceRIPELG----PKDTYVGYLPLAHVLELTAEISCVTYGCRIGY----SSPLTLSD-QSSKIKKg 317
Cdd:cd17642 202 VQLTHKNIVARFSHA--RDPIFGnqiiPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykfEEELFLRSlQDYKVQS- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 318 skgdcTVLKPTLMAAVP--EIMDRiyknvmskvqemnyiqrtlfkigYDYKleqikrgydaplcnillfkkvkallggNV 395
Cdd:cd17642 279 -----ALLVPTLFAFFAksTLVDK-----------------------YDLS---------------------------NL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 396 RMMLSGGAPLSPQTQRFMNICFCCP-VGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTcrdKPNP 474
Cdd:cd17642 304 HEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTL---GPNE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 475 RGEIIIGGPNVSMGYFKNEEKTEDFsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCP 554
Cdd:cd17642 381 RGELCVKGPMIMKGYVNNPEATKAL-IDKDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GYQVPPAELESILLQHP 456
|
..
gi 1935119612 555 FI 556
Cdd:cd17642 457 KI 458
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
137-550 |
9.54e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.56 E-value: 9.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 137 VTLYATLGEEAVTYGLNESGASYLITSVELLES-KLKPALSEIPGLKHIIYVD--KKTINKSEypeglEIHSMQTVEELG 213
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKFLEKlKNKGFDLELPENVKVIYLEdlKAKISKVD-----KLTALLAARLLP 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 214 AKP-ENLDIPPSKPvpTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTgQCERIPELGPKDTYVGYLPLAHVLELTAE--- 289
Cdd:PRK08633 768 ARLlKRLYGPTFKP--DDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSLPFFHSFGLTVTlwl 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 290 -----ISCVTYgcrigySSPLtlsdQSSKIKKgskgdcTVLK--PTLMAAVPEIMdRIYknvmskvqemnyiqrtlfkig 362
Cdd:PRK08633 845 pllegIKVVYH------PDPT----DALGIAK------LVAKhrATILLGTPTFL-RLY--------------------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 363 ydykleqikrgydaplcniLLFKKVKALLGGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTI----TE 438
Cdd:PRK08633 887 -------------------LRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVnlpdVL 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 439 VSDYST------GRVGAPLICCEIKLRDwQEGGYTCrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDENGQRWFCTG 512
Cdd:PRK08633 948 AADFKRqtgskeGSVGMPLPGVAVRIVD-PETFEEL--PPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTG 1024
|
410 420 430
....*....|....*....|....*....|....*...
gi 1935119612 513 DIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVETAL 550
Cdd:PRK08633 1025 DKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
87-550 |
2.37e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 114.05 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 87 YEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVEL 166
Cdd:COG0365 42 YAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 167 LE--------SKLKPALSEIPGLKHIIYVDKkTINKSEYPEGLEIHsmqtvEELGAKPENLDippskPVPT---DLALIM 235
Cdd:COG0365 122 LRggkvidlkEKVDEALEELPSLEHVIVVGR-TGADVPMEGDLDWD-----ELLAAASAEFE-----PEPTdadDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 236 YTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTY-----VG---------YLPLAHvleltaEISCVTYGCRIGY 301
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFwctadIGwatghsyivYGPLLN------GATVVLYEGRPDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 302 SSPLTLSDQSSKikkgskgdctvLKPTLMAAVPeimdriyknvmskvqemNYIqRTLFKIGydyklEQIKRGYDaplcni 381
Cdd:COG0365 265 PDPGRLWELIEK-----------YGVTVFFTAP-----------------TAI-RALMKAG-----DEPLKKYD------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 382 llfkkVKALlggnvRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGA-GTITEVSDYSTGRVGAPLICCEIKLRD 460
Cdd:COG0365 305 -----LSSL-----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVVD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 461 wqEGGYTCRdkPNPRGEIIIGGPNVSM--GYFKNEEKTED--FSVDENgqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLq 536
Cdd:COG0365 375 --EDGNPVP--PGEEGELVIKGPWPGMfrGYWNDPERYREtyFGRFPG---WYRTGDGARRDEDGYFWILGRSDDVINV- 446
|
490
....*....|....
gi 1935119612 537 AGEYVSLGKVETAL 550
Cdd:COG0365 447 SGHRIGTAEIESAL 460
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
85-567 |
3.05e-26 |
|
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: 112.19 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELlesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvpTDLALIMYTSGSTGRP 244
Cdd:cd05935 82 EL--------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCeRIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCriGYSSPLTLSDQSSKIKKGSKGDCTV 324
Cdd:cd05935 100 KGCMHTHFSAAANALQSA-VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG--GTYVLMARWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 325 LkptlMAAVPEIMDriyknVMSKVQemnyiqrtlfkigydykleqiKRGYDaplcnillFKKVKALLGGnvrmmlsgGAP 404
Cdd:cd05935 177 W----TNIPTMLVD-----LLATPE---------------------FKTRD--------LSSLKVLTGG--------GAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 405 LSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEGGYTcrdKPNPRGEIIIGGPN 484
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGREL---PPNEVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 485 VSMGYFKNEEKTEDFSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVETALKNCPFIDNICAYAK 564
Cdd:cd05935 288 IFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVCVISV 366
|
...
gi 1935119612 565 SDQ 567
Cdd:cd05935 367 PDE 369
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
83-567 |
7.21e-26 |
|
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: 111.61 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 SVELlesklkpalseipglkhiiyvdkktinkseyPEGLEIHSMQTVEELGAKPENLDIPPSKPVPTDLALIMYTSGSTG 242
Cdd:cd12116 91 DDAL-------------------------------PDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 243 RPKGVMMIHKNLIAGMTGQCERiPELGPKDTYVG-------------YLPL---AHVLELTAEIScvtygcrigySSPLT 306
Cdd:cd12116 140 RPKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAvttyafdisllelLLPLlagARVVIAPRETQ----------RDPEA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 307 LSDQSSKIkkgskgdctvlKPTLMAAVPEIMdriyknvmskvqemnyiqRTLFKIGYdykleQIKRGYDApLCnillfkk 386
Cdd:cd12116 209 LARLIEAH-----------SITVMQATPATW------------------RMLLDAGW-----QGRAGLTA-LC------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 387 vkallggnvrmmlsGGAPLSPQTQRFmnicFCCPVGQG---YGLTETCGAGTITEVSDYSTG-RVGAPLICCEIKLRDwq 462
Cdd:cd12116 247 --------------GGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAAAGPiPIGRPLANTQVYVLD-- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 463 EGGytcrdKPNPR---GEIIIGGPNVSMGYFKNEEKT-EDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 535
Cdd:cd12116 307 AAL-----RPVPPgvpGELYIGGDGVAQGYLGRPALTaERFVPDpfaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKI 381
|
490 500 510
....*....|....*....|....*....|..
gi 1935119612 536 QaGEYVSLGKVETALKNCPFIDNICAYAKSDQ 567
Cdd:cd12116 382 R-GHRIELGEIEAALAAHPGVAQAAVVVREDG 412
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
41-554 |
2.14e-25 |
|
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: 110.41 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 41 LFDHAVAKFGKkdclgtREILSEENEmqpngkvfkklilGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCetra 120
Cdd:cd12119 1 LLEHAARLHGD------REIVSRTHE-------------GEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLA---- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 121 eWmiaaqTCFKYnfpLVTLYAT-------------LGEEAVTYGLNESGASYLITSVELLeSKLKPALSEIPGLKHIIYV 187
Cdd:cd12119 58 -W-----NTHRH---LELYYAVpgmgavlhtinprLFPEQIAYIINHAEDRVVFVDRDFL-PLLEAIAPRLPTVEHVVVM 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 188 DKKtiNKSEYPEGLEIHSMQtvEELGAKPENLDIPPSKPvpTDLALIMYTSGSTGRPKGVMMIHKNLI--AGMTGQCERI 265
Cdd:cd12119 128 TDD--AAMPEPAGVGVLAYE--ELLAAESPEYDWPDFDE--NTAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 266 PeLGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDQSSKIKKGSKgdctvlkPTLMAAVPEImdriYKNVM 345
Cdd:cd12119 202 G-LSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDPASLAELIEREG-------VTFAAGVPTV----WQGLL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 346 skvQEMNYIQRTLFKigydykleqikrgydaplcnillfkkvkallggnVRMMLSGGAPLSPQ-----TQRFMNICfccp 420
Cdd:cd12119 270 ---DHLEANGRDLSS----------------------------------LRRVVIGGSAVPRSlieafEERGVRVI---- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 421 vgQGYGLTETCGAGTI----TEVSD----------YSTGRVgAPLIccEIKLRDwQEGGYTCRDkPNPRGEIIIGGPNVS 486
Cdd:cd12119 309 --HAWGMTETSPLGTVarppSEHSNlsedeqlalrAKQGRP-VPGV--ELRIVD-DDGRELPWD-GKAVGELQVRGPWVT 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935119612 487 MGYFKNEEKTEDFsvDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCP 554
Cdd:cd12119 382 KSYYKNDEESEAL--TEDG--WLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWISSVELENAIMAHP 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
229-567 |
2.32e-25 |
|
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: 109.30 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 229 TDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHvleltaeISCVTYGCRIGYSSPLTLs 308
Cdd:cd05934 81 VDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG-LGEDDVYLTVLPLFH-------INAQAVSVLAALSVGATL- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 309 dqsskikkgskgdctVLKPTLMAAvpeimdriykNVMSKVQE-----MNYIQRTLfkigyDYKLEQIKRGYDAplcnill 383
Cdd:cd05934 152 ---------------VLLPRFSAS----------RFWSDVRRygatvTNYLGAML-----SYLLAQPPSPDDR------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 384 fkkvkallGGNVRmmLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCgAGTITEVSDYS-TGRVGAPLICCEIKLRDWQ 462
Cdd:cd05934 195 --------AHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETI-VGVIGPRDEPRrPGSIGRPAPGYEVRIVDDD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 463 eggytcrDKPNPR---GEIII---GGPNVSMGYFKNEEKTEDfsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQ 536
Cdd:cd05934 264 -------GQELPAgepGELVIrglRGWGFFKGYYNMPEATAE--AMRNG--WFHTGDLGYRDADGFFYFVDRKKDMIR-R 331
|
330 340 350
....*....|....*....|....*....|.
gi 1935119612 537 AGEYVSLGKVETALKNCPFIDNICAYAKSDQ 567
Cdd:cd05934 332 RGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-554 |
1.15e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 108.05 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRA---EWMIAAQTCFKYNFPLvtlYATLGEEAVTYGLNESGASYLI 161
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAaflELAFAASYLGAVFLPI---NYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 162 TSVELlesklkpalSEIPGLKHIIYVdkktinkseypegLEIHSMQTVEELGAKpeNLDIPPSKPV-PTDLALIMYTSGS 240
Cdd:PRK06145 105 VDEEF---------DAIVALETPKIV-------------IDAAAQADSRRLAQG--GLEIPPQAAVaPTDLVRLMYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 241 TGRPKGVMMIHKNL--------IA-GMTGQcERIPELGPkdtyvgylpLAHV--LELTAeISCVTYGCRIGYSSPLTLSD 309
Cdd:PRK06145 161 TDRPKGVMHSYGNLhwksidhvIAlGLTAS-ERLLVVGP---------LYHVgaFDLPG-IAVLWVGGTLRIHREFDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 QSSKIKKgSKGDCTVLKPTLMAAVPEIMDRiyknvmskvqemnyiqrtlfkigYDYKLEQ----IKRGYDAPLCNILLFK 385
Cdd:PRK06145 230 VLAAIER-HRLTCAWMAPVMLSRVLTVPDR-----------------------DRFDLDSlawcIGGGEKTPESRIRDFT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 386 KVkallggnvrmmLSGGaplspqtqRFMNicfccpvgqGYGLTETCGAGTITEVSDY-----STGRVGAPLiccEIKLRD 460
Cdd:PRK06145 286 RV-----------FTRA--------RYID---------AYGLTETCSGDTLMEAGREiekigSTGRALAHV---EIRIAD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 461 wQEGGYTcrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEY 540
Cdd:PRK06145 335 -GAGRWL---PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD----WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGEN 405
|
490
....*....|....
gi 1935119612 541 VSLGKVETALKNCP 554
Cdd:PRK06145 406 IASSEVERVIYELP 419
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
230-658 |
1.39e-24 |
|
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: 105.11 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVLELTAEISCVTYGcrigysSPLTLSD 309
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVGGLAILVRSLLAG------AELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 QSSKIKKgskgDCTVLKPTLMAAVPEimdriyknvmskvqemnyiqrtlfkigydykleQIKRGYDAPLCNILLFkkvka 389
Cdd:cd17630 74 RNQALAE----DLAPPGVTHVSLVPT---------------------------------QLQRLLDSGQGPAALK----- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 390 llggNVRMMLSGGAPLSPQ-TQRFmnICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDwqeggytc 468
Cdd:cd17630 112 ----SLRAVLLGGAPIPPElLERA--ADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 469 rdkpnpRGEIIIGGPNVSMGYFKNEEKTEdfsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVET 548
Cdd:cd17630 178 ------DGEIWVGGASLAMGYLRGQLVPE---FNEDG--WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 549 ALKNCPFIDNICAYAKSDQSY---VISFVVPnqkkltvlaeqkgvkgtwveicNNPIMEAEILKEIKEvadkmKLERFET 625
Cdd:cd17630 246 ALAAHPAVRDAFVVGVPDEELgqrPVAVIVG----------------------RGPADPAELRAWLKD-----KLARFKL 298
|
410 420 430
....*....|....*....|....*....|...
gi 1935119612 626 PIkvRLSPEPWTPETGLVtdafKLKRKELKNHY 658
Cdd:cd17630 299 PK--RIYPVPELPRTGGG----KVDRRALRAWL 325
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
78-576 |
1.43e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 107.64 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 78 ILGNYRWLNYEDINQRVNHFGRGLAAQ-GLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESG 156
Cdd:PRK06839 21 IITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLESKLkpALSEIPGLKHIIYVdkktinksEYPEGLEIHsmqtveelgaKPENLDiPPSKPVPTdlaLIMY 236
Cdd:PRK06839 101 TTVLFVEKTFQNMAL--SMQKVSYVQRVISI--------TSLKEIEDR----------KIDNFV-EKNESASF---IICY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 237 TSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVleltAEISCVTY-----GCRIGYSSPLTLSDQS 311
Cdd:PRK06839 157 TSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHI----GGIGLFAFptlfaGGVIIVPRKFEPTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 312 SKIKKGskgdctvlKPTLMAAVPEIMDRIyknvmskvqemnyIQRTLFkigydykleqIKRGYDaplcnillfkkvkall 391
Cdd:PRK06839 232 SMIEKH--------KVTVVMGVPTIHQAL-------------INCSKF----------ETTNLQ---------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 392 ggNVRMMLSGGAPLS-PQTQRFMNICFccPVGQGYGLTETCGAGTITEVSDYS--TGRVGAPLICCEIKLRDWQEGgytc 468
Cdd:PRK06839 265 --SVRWFYNGGAPCPeELMREFIDRGF--LFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDENKN---- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 469 RDKPNPRGEIIIGGPNVSMGYFKNEEKTEDfsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVET 548
Cdd:PRK06839 337 KVEVGEVGELLIRGPNVMKEYWNRPDATEE--TIQDG--WLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQ 411
|
490 500 510
....*....|....*....|....*....|.
gi 1935119612 549 ALKNCPFIDNICAYAKSDQSY---VISFVVP 576
Cdd:PRK06839 412 VINKLSDVYEVAVVGRQHVKWgeiPIAFIVK 442
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
80-578 |
3.24e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.06 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFK----YNfPLVTLYAtlgEEAVTYGLNES 155
Cdd:PRK13295 51 GAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRigavLN-PLMPIFR---ERELSFMLKHA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 156 GASYLIT-------SVELLESKLKPALseiPGLKHIIYVDkktinkSEYPEGLEIHSMQTVEELGAkpenlDIPP----S 224
Cdd:PRK13295 127 ESKVLVVpktfrgfDHAAMARRLRPEL---PALRHVVVVG------GDGADSFEALLITPAWEQEP-----DAPAilarL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 225 KPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHvleLTAEIscvtYGCRIgyssP 304
Cdd:PRK13295 193 RPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASPMAH---QTGFM----YGLMM----P 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 305 LTLsdqsskikkgskGDCTVLK----PTL-------------MAAVPEIMDriyknvMSKVQEmnyiqrtlfkigydykl 367
Cdd:PRK13295 261 VML------------GATAVLQdiwdPARaaelirtegvtftMASTPFLTD------LTRAVK----------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 368 eqiKRGYDAPlcnillfkkvkallggNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTEtCGAGTITEVSD---YST 444
Cdd:PRK13295 306 ---ESGRPVS----------------SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE-NGAVTLTKLDDpdeRAS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 445 GRVGAPLICCEIKLRDWQeggytcrDKPNPRGEI---IIGGPNVSMGYFKNEEKTEDfsvDENGqrWFCTGDIGEFHPDG 521
Cdd:PRK13295 366 TTDGCPLPGVEVRVVDAD-------GAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGT---DADG--WFDTGDLARIDADG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 522 CLQIIDRKKDLVkLQAGEYVSLGKVETALKNCPFIDNICAYAKSD---QSYVISFVVPNQ 578
Cdd:PRK13295 434 YIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDerlGERACAFVVPRP 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
223-587 |
6.31e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.39 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 223 PSKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTgQCERI--PELGP-KDTYVGYLPLAHvleltaeISCVTYGCRI 299
Cdd:PRK05677 201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANML-QCRALmgSNLNEgCEILIAPLPLYH-------IYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 300 gysspLTLSdqsskikkgskGDCTVLKPTlmaavPEIMDRIYKnVMSKVQEMNYIQ-RTLFkigydykleqikrgydAPL 378
Cdd:PRK05677 273 -----MMLI-----------GNHNILISN-----PRDLPAMVK-ELGKWKFSGFVGlNTLF----------------VAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 379 CNILLFKKV--KALlggnvRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEI 456
Cdd:PRK05677 315 CNNEAFRKLdfSAL-----KLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLC 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 457 KLRDwQEGGYTCRDKPnprGEIIIGGPNVSMGYFKNEEKTeDFSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQ 536
Cdd:PRK05677 390 KVID-DDGNELPLGEV---GELCVKGPQVMKGYWQRPEAT-DEILDSDG--WLKTGDIALIQEDGYMRIVDRKKDMI-LV 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 537 AGEYVSLGKVETALKNCPFIDNICAYAKSDQS---YVISFVVPnQKKLTVLAEQ 587
Cdd:PRK05677 462 SGFNVYPNELEDVLAALPGVLQCAAIGVPDEKsgeAIKVFVVV-KPGETLTKEQ 514
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
83-569 |
4.37e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 103.70 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWlNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:PRK12583 45 RY-TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 S--------VELLESkLKPALSE----------IPGLKHIIYVDKktinksEYPEG-LEIHSMQTVEElGAKPENLDIPP 223
Cdd:PRK12583 124 AdafktsdyHAMLQE-LLPGLAEgqpgalacerLPELRGVVSLAP------APPPGfLAWHELQARGE-TVSREALAERQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 224 SKPVPTDLALIMYTSGSTGRPKGVMMIHKNLI--AGMTGQCERipeLGPKDTYVGYLPLAHVLELT-AEISCVTYGCRIG 300
Cdd:PRK12583 196 ASLDRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAESLG---LTEHDRLCVPVPLYHCFGMVlANLGCMTVGACLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 301 YssPLTLSDQSSKIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIQRTLFKIgydykleqikrgydapl 378
Cdd:PRK12583 273 Y--PNEAFDPLATLQAVEEERCTALYgvPTMFIA-----------------ELDHPQRGNFDL----------------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 379 cnillfkkvkallgGNVRMMLSGGAPLSPQT-QRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGR---VGAPLICC 454
Cdd:PRK12583 317 --------------SSLRTGIMAGAPCPIEVmRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRvetVGRTQPHL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 455 EIKLRDwQEGGYTCRDKpnpRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 534
Cdd:PRK12583 383 EVKVVD-PDGATVPRGE---IGELCTRGYSVMKGYWNNPEATAE-SIDEDG--WMHTGDLATMDEQGYVRIVGRSKDMI- 454
|
490 500 510
....*....|....*....|....*....|....*
gi 1935119612 535 LQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSY 569
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
85-579 |
4.93e-23 |
|
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: 102.94 E-value: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELlesKLKPALSeipglKHIIYVDKKTINKseypegleihsmqtveELGakpENLDIPPSKpvpTDLALIMYTSGSTGRP 244
Cdd:cd17656 94 HL---KSKLSFN-----KSTILLEDPSISQ----------------EDT---SNIDYINNS---DDLLYIIYTSGTTGKP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMtgQCERipelgpkdTYVGYLPLAHVLELTAEISCVTYgcrigysspltlSDQSSKIKKGskGDCTV 324
Cdd:cd17656 144 KGVQLEHKNMVNLL--HFER--------EKTNINFSDKVLQFATCSFDVCY------------QEIFSTLLSG--GTLYI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 325 LKPTLMAAVPEIMDRIYKNVMSKVqemnYIQRTLFKIGYDykleqiKRGYDAPLcnillFKKVKALLGGNVRMMLSggap 404
Cdd:cd17656 200 IREETKRDVEQLFDLVKRHNIEVV----FLPVAFLKFIFS------EREFINRF-----PTCVKHIITAGEQLVIT---- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 405 lspQTQRFMNICFCCPVGQGYGLTETCGAGTIT-----EVSDYSTgrVGAPLICCEIKLRDWQEggytcrdKPNPRG--- 476
Cdd:cd17656 261 ---NEFKEMLHEHNVHLHNHYGPSETHVVTTYTinpeaEIPELPP--IGKPISNTWIYILDQEQ-------QLQPQGivg 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 477 EIIIGGPNVSMGYFKNEEKT-EDFSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNC 553
Cdd:cd17656 329 ELYISGASVARGYLNRQELTaEKFFPDpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR-GYRIELGEIEAQLLNH 407
|
490 500
....*....|....*....|....*....
gi 1935119612 554 PFIDNICAYAKSD---QSYVISFVVPNQK 579
Cdd:cd17656 408 PGVSEAVVLDKADdkgEKYLCAYFVMEQE 436
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
85-533 |
6.18e-23 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 103.13 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFkynfpLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACV-----LAGFVPAPLTVPPTYDEPNARLRKLRHIW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLES-------KLKPALSEIPGLKHIiyvdkktinkseypEGLEIHSmqtVEELGAKPENLDIPPSKPvpTDLALIMYT 237
Cdd:cd05906 115 QLLGSpvvltdaELVAEFAGLETLSGL--------------PGIRVLS---IEELLDTAADHDLPQSRP--DDLALLMLT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 238 SGSTGRPKGVMMIHKNLIAGMTGQCeRIPELGPKDTYVGYLPLAHVLELT-AEISCVTYGCR-IGYSSPLTLSDqsskik 315
Cdd:cd05906 176 SGSTGFPKAVPLTHRNILARSAGKI-QHNGLTPQDVFLNWVPLDHVGGLVeLHLRAVYLGCQqVHVPTEEILAD------ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 316 kgskgdctvlkPTLMaavpeimdriyknvmskvqeMNYIQRtlFKIGYDYkleqikrgydAP--LCNILL-----FKKVK 388
Cdd:cd05906 249 -----------PLRW--------------------LDLIDR--YRVTITW----------APnfAFALLNdlleeIEDGT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 389 ALLgGNVRMMLSGGAPLSPQT-QRFMNICFCCPVGQ-----GYGLTETCgAGTITEVSDYSTGR--------VGAPLICC 454
Cdd:cd05906 286 WDL-SSLRYLVNAGEAVVAKTiRRLLRLLEPYGLPPdairpAFGMTETC-SGVIYSRSFPTYDHsqalefvsLGRPIPGV 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935119612 455 EIKLRDwQEGGYTCRDKPnprGEIIIGGPNVSMGYFKNEEKTEDFSVDENgqrWFCTGDIGEFHpDGCLQIIDRKKDLV 533
Cdd:cd05906 364 SMRIVD-DEGQLLPEGEV---GRLQVRGPVVTKGYYNNPEANAEAFTEDG---WFRTGDLGFLD-NGNLTITGRTKDTI 434
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
225-583 |
1.14e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 99.51 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 225 KPVPT---DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGP---------KDTYVGYLPLAHVLELTAEISC 292
Cdd:PRK12492 200 KPVPVgldDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplmkegQEVMIAPLPLYHIYAFTANCMC 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 293 --VTYGCRIGYSSPltlSDQSSKIKKGSKGDCTVL--KPTLMAAVpeimdriyknvmskvqeMNYIQrtlfkigydykle 368
Cdd:PRK12492 280 mmVSGNHNVLITNP---RDIPGFIKELGKWRFSALlgLNTLFVAL-----------------MDHPG------------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 369 qikrgydaplcnillFKKVKAllgGNVRMMLSGGAPLSPQT-QRFMNICfCCPVGQGYGLTETCGAGTITEVSDYST-GR 446
Cdd:PRK12492 327 ---------------FKDLDF---SALKLTNSGGTALVKATaERWEQLT-GCTIVEGYGLTETSPVASTNPYGELARlGT 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 447 VGAPLICCEIKLRDwQEGgytcRDKP-NPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQI 525
Cdd:PRK12492 388 VGIPVPGTALKVID-DDG----NELPlGERGELCIKGPQVMKGYWQQPEATAE-ALDAEG--WFKTGDIAVIDPDGFVRI 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935119612 526 IDRKKDLVkLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQ---SYVISFVVPNQKKLTV 583
Cdd:PRK12492 460 VDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDErsgEAVKLFVVARDPGLSV 519
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
75-623 |
1.80e-21 |
|
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: 98.21 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 75 KKLILGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNE 154
Cdd:cd05959 20 KTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 155 SGASYLITSVELLEsKLKPAL-SEIPGLKHIIYVDkktinkseyPEGLEIHSMQTVEELGAKPENLdiPPSKPVPTDLAL 233
Cdd:cd05959 100 SRARVVVVSGELAP-VLAAALtKSEHTLVVLIVSG---------GAGPEAGALLLAELVAAEAEQL--KPAATHADDPAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 234 IMYTSGSTGRPKGVMMIHKNLIAgmtgQCEripelgpkdTYVGylplaHVLELTAEISCVT-------YGCRIGYSSPLt 306
Cdd:cd05959 168 WLYSSGSTGRPKGVVHLHADIYW----TAE---------LYAR-----NVLGIREDDVCFSaaklffaYGLGNSLTFPL- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 307 lsdqsskikkgSKGDCTVLKPTLMAAvpeimDRIYKnvmskvqemnYIQR---TLFkigydykleqikrgYDAP-LCNIL 382
Cdd:cd05959 229 -----------SVGATTVLMPERPTP-----AAVFK----------RIRRyrpTVF--------------FGVPtLYAAM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 LFKKV-KALLGGNVRMMLSGGAPLSPQT-QRFMNIcFCCPVGQGYGLTEtcgAGTI------TEVSDYSTGRvgaPLICC 454
Cdd:cd05959 269 LAAPNlPSRDLSSLRLCVSAGEALPAEVgERWKAR-FGLDILDGIGSTE---MLHIflsnrpGRVRYGTTGK---PVPGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 455 EIKLRDwQEGGYTCRDKPnprGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 534
Cdd:cd05959 342 EVELRD-EDGGDVADGEP---GELYVRGPSSATMYWNNRDKTRDTFQGE----WTRTGDKYVRDDDGFYTYAGRADDMLK 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 535 LqAGEYVSLGKVETALKNCPFIDNICAYAKSDQSYVI---SFVVPNQKKLTVLAEQKGVKgtwvEICNNPIMEAEILKEI 611
Cdd:cd05959 414 V-SGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTkpkAFVVLRPGYEDSEALEEELK----EFVKDRLAPYKYPRWI 488
|
570
....*....|....*..
gi 1935119612 612 KEVAD--KM---KLERF 623
Cdd:cd05959 489 VFVDElpKTatgKIQRF 505
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
85-576 |
2.10e-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: 97.73 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAqtcfkynfplvtlyatlgeeavtYGLNESGASYLITSV 164
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAV-----------------------LGILAAGAAYVPVDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELlesklkPA--LSEIPGLKHIIYVdkktINKSEYPEGLEIHSMQTVEELGAKPENLDIPPSKPVPTDLALIMYTSGSTG 242
Cdd:cd12114 70 DQ------PAarREAILADAGARLV----LTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 243 RPKGVMMIHK---NLIAGMTgqcERIpELGPKDTYVGYLPLAH---VLELTAEIScvtygcrIGYSspLTLSDQsskikk 316
Cdd:cd12114 140 TPKGVMISHRaalNTILDIN---RRF-AVGPDDRVLALSSLSFdlsVYDIFGALS-------AGAT--LVLPDE------ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 317 GSKGDCTVLKP-------TLMAAVPEIMDRIyknvmskvqeMNYiqrtlfkigydykLEQIKRgydaplcnillfkkvka 389
Cdd:cd12114 201 ARRRDPAHWAElierhgvTLWNSVPALLEML----------LDV-------------LEAAQA----------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 390 lLGGNVRM-MLSGG-APLS-PQT--QRFMNicfCCPVGQGyGLTETCGAGTITEVSDYSTGRV----GAPLICCEIKLRD 460
Cdd:cd12114 241 -LLPSLRLvLLSGDwIPLDlPARlrALAPD---ARLISLG-GATEASIWSIYHPIDEVPPDWRsipyGRPLANQRYRVLD 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 461 wqEGGytcRDKPN-PRGEIIIGGPNVSMGYFKNEEKT-EDFSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaG 538
Cdd:cd12114 316 --PRG---RDCPDwVPGELWIGGRGVALGYLGDPELTaARFVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR-G 389
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1935119612 539 EYVSLGKVETALKNCPFIDNICA--YAKSDQSYVISFVVP 576
Cdd:cd12114 390 YRIELGEIEAALQAHPGVARAVVvvLGDPGGKRLAAFVVP 429
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
81-579 |
2.69e-21 |
|
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: 97.15 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 81 NYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYL 160
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 161 ITSvellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvPTDLALIMYTSGS 240
Cdd:cd17650 89 LTQ----------------------------------------------------------------PEDLAYVIYTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 241 TGRPKGVMMIHKNlIAGMTGQCERIPELGPKDtyVGYLPLAHV--------LELTAEISCVTYGCRIGyssplTLSDQSS 312
Cdd:cd17650 105 TGKPKGVMVEHRN-VAHAAHAWRREYELDSFP--VRLLQMASFsfdvfagdFARSLLNGGTLVICPDE-----VKLDPAA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 313 --KIKKGSKGDCTVLKPTLMAAVpeiMDRIYKNvmskvqEMNYIQRTLFKIGYDykleqikrgydapLCNILLFKKVKAL 390
Cdd:cd17650 177 lyDLILKSRITLMESTPALIRPV---MAYVYRN------GLDLSAMRLLIVGSD-------------GCKAQDFKTLAAR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 391 LGGNVRMMLSggaplspqtqrfmnicfccpvgqgYGLTETCGAGTITEVSDYSTGR-----VGAPLICCEIKLRDwqegg 465
Cdd:cd17650 235 FGQGMRIINS------------------------YGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLD----- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 466 ytCRDKPNP---RGEIIIGGPNVSMGYFKNEEKTEDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGE 539
Cdd:cd17650 286 --ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVEnpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR-GF 362
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1935119612 540 YVSLGKVETALKNCPFIDNICAYAKSD---QSYVISFVVPNQK 579
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVAVREDkggEARLCAYVVAAAT 405
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
230-560 |
4.00e-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: 95.03 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLI-AGMtgQCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCR---IGYSSPL 305
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 TLSD--QSSKIkkgskgdctvlkpTLMAAVPEIMDRIyknvmskvqemnyiqrtlfkigydykLEQI-KRGYDAPlcnil 382
Cdd:cd17637 79 EALEliEEEKV-------------TLMGSFPPILSNL--------------------------LDAAeKSGVDLS----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 lfkKVKALLGGNVrmmlsggaplsPQT-QRFMNIC---FCCpvgqGYGLTETCGAGTITEVSDYStGRVGAPLICCEIKL 458
Cdd:cd17637 115 ---SLRHVLGLDA-----------PETiQRFEETTgatFWS----LYGQTETSGLVTLSPYRERP-GSAGRPGPLVRVRI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 459 RDWQeggytcrDKPNPR---GEIIIGGPNVSMGYFKNEEKTE-DFsvdENGqrWFCTGDIGEFHPDGCLQIIDRK--KDL 532
Cdd:cd17637 176 VDDN-------DRPVPAgetGEIVVRGPLVFQGYWNLPELTAyTF---RNG--WHHTGDLGRFDEDGYLWYAGRKpeKEL 243
|
330 340
....*....|....*....|....*...
gi 1935119612 533 VKlQAGEYVSLGKVETALKNCPFIDNIC 560
Cdd:cd17637 244 IK-PGGENVYPAEVEKVILEHPAIAEVC 270
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
155-575 |
4.18e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 97.36 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 155 SGASYLITSVELLEsKLKPaLSEIPGLKhIIYVDkktinksEYPEGLeIHsmqtVEELGAKPENlDIPPSKPVPTDLALI 234
Cdd:PLN02246 121 SGAKLIITQSCYVD-KLKG-LAEDDGVT-VVTID-------DPPEGC-LH----FSELTQADEN-ELPEVEISPDDVVAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 235 MYTSGSTGRPKGVMMIHKNLIAGMTGQCE-RIPELG--PKDTYVGYLPLAHVLELTAEISCvtyGCRIGysspltlsdqs 311
Cdd:PLN02246 185 PYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLYfhSDDVILCVLPMFHIYSLNSVLLC---GLRVG----------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 312 SKIKKGSKGDCTVL-------KPTLMAAVPEIMDRIYKNVMSKvqemnyiqrtlfkigyDYKLEQIkrgydaplcnillf 384
Cdd:PLN02246 251 AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKSPVVE----------------KYDLSSI-------------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 385 kkvkallggnvRMMLSGGAPLSPQTQ-----RFMNICFccpvGQGYGLTEtcgAGTI--------TEVSDYSTGRVGAPL 451
Cdd:PLN02246 301 -----------RMVLSGAAPLGKELEdafraKLPNAVL----GQGYGMTE---AGPVlamclafaKEPFPVKSGSCGTVV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 452 ICCEIKLRDWQEGGYTCRDKPnprGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 531
Cdd:PLN02246 363 RNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDPEATAN-TIDKDG--WLHTGDIGYIDDDDELFIVDRLKE 436
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1935119612 532 LVKLQaGEYVSLGKVETALKNCPFIDNICAYAKSDQS---YVISFVV 575
Cdd:PLN02246 437 LIKYK-GFQVAPAELEALLISHPSIADAAVVPMKDEVageVPVAFVV 482
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
83-533 |
5.75e-21 |
|
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: 96.92 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWLNYEDINQRVnhfgRGLAA---QGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYA-TLGEEAVTYG--LNESG 156
Cdd:cd05931 23 ETLTYAELDRRA----RAIAArlqAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpTPGRHAERLAaiLADAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLEsklkpalsEIPGLKHiiyvdkktinkseYPEGLEIHSMQTVEELGAKPENlDIPPSKPVPTDLALIMY 236
Cdd:cd05931 99 PRVVLTTAAALA--------AVRAFAA-------------SRPAAGTPRLLVVDLLPDTSAA-DWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 237 TSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTAEI-SCVTYGCRIGYSSPLT-LSDQSSKI 314
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYHDMGLIGGLlTPLYSGGPSVLMSPAAfLRRPLRWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 315 KKGSKGDCTvlkptlMAAVPeimdriyknvmskvqemNYiqrtlfkiGYDYkleQIKRGYDAPLCNILLfkkvkallgGN 394
Cdd:cd05931 236 RLISRYRAT------ISAAP-----------------NF--------AYDL---CVRRVRDEDLEGLDL---------SS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 395 VRMMLSGGAPLSPQT-QRFMNiCFcCPVG-------QGYGLTETC--------GAGTITEV----------------SDY 442
Cdd:cd05931 273 WRVALNGAEPVRPATlRRFAE-AF-APFGfrpeafrPSYGLAEATlfvsggppGTGPVVLRvdrdalagravavaadDPA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 443 STGRV--GAPLICCEIKLRDwQEGGYTCRDkpNPRGEIIIGGPNVSMGYFKNEEKTEDF---SVDENGQRWFCTGDIGEF 517
Cdd:cd05931 351 ARELVscGRPLPDQEVRIVD-PETGRELPD--GEVGEIWVRGPSVASGYWGRPEATAETfgaLAATDEGGWLRTGDLGFL 427
|
490
....*....|....*.
gi 1935119612 518 HpDGCLQIIDRKKDLV 533
Cdd:cd05931 428 H-DGELYITGRLKDLI 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
146-533 |
6.06e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 97.33 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 146 EAVTYGLNESGASYLITSVELLES----KLKPALSEIPGLKHIIYVD--------KKTINKSEYPE-GLEIHSMQTveEL 212
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVDlarylpgpKRLAVPLIRRKaHARILDFDA--EL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 213 GAKPENLDIPPSKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAgMTGQCERIPELGPKDTYVGYLPLAHVleltaeisc 292
Cdd:PRK07529 197 ARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA-NAWLGALLLGLGPGDTVFCGLPLFHV--------- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 293 vtYGCRIGYSSPLtlsdqsskikkgSKGDCTVLKPTLMAAVPEIMDRIYK-------NVMSKVQemnyiqrTLFkigydy 365
Cdd:PRK07529 267 --NALLVTGLAPL------------ARGAHVVLATPQGYRGPGVIANFWKiveryriNFLSGVP-------TVY------ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 366 kleqikrgydaplcNILLFKKVKALLGGNVRMMLSGGAPLSPQT-QRFMN---IcfccPVGQGYGLTE-TCGAGTITEVS 440
Cdd:PRK07529 320 --------------AALLQVPVDGHDISSLRYALCGAAPLPVEVfRRFEAatgV----RIVEGYGLTEaTCVSSVNPPDG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 441 DYSTGRVGAPLICCEIKLRDWQEGGYTCRD-KPNPRGEIIIGGPNVSMGYFkNEEKTEDFSVDEngqRWFCTGDIGEFHP 519
Cdd:PRK07529 382 ERRIGSVGLRLPYQRVRVVILDDAGRYLRDcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLED---GWLNTGDLGRIDA 457
|
410
....*....|....
gi 1935119612 520 DGCLQIIDRKKDLV 533
Cdd:PRK07529 458 DGYFWLTGRAKDLI 471
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
230-578 |
6.17e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.22 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTG----QCERIPELGPKDTYVGYLPLAHVleltaeiscvtYGCRIGYSSPL 305
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELfvrfEASQYEYPGSDNVYLAALPMFHI-----------YGLSLFVVGLL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 TLsdqsskikkGSkgdcTVLkptlmaavpeIMDRIYKNVMSKVqemnyIQR---TLFKIgydykleqikrgydAPLCNIL 382
Cdd:PLN02574 268 SL---------GS----TIV----------VMRRFDASDMVKV-----IDRfkvTHFPV--------------VPPILMA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 LFKKVKALLGG---NVRMMLSGGAPLSPQT-QRFMNICFCCPVGQGYGLTETCGAGT----ITEVSDYSTGRVGAPLIcc 454
Cdd:PLN02574 306 LTKKAKGVCGEvlkSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIQGYGMTESTAVGTrgfnTEKLSKYSSVGLLAPNM-- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 455 EIKLRDWQEGgytCRDKPNPRGEIIIGGPNVSMGYFKNEEKTeDFSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 534
Cdd:PLN02574 384 QAKVVDWSTG---CLLPPGNCGELWIQGPGVMKGYLNNPKAT-QSTIDKDG--WLRTGDIAYFDEDGYLYIVDRLKEIIK 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1935119612 535 LQaGEYVSLGKVETALKNCPFIDNICAYAKSDQ---SYVISFVVPNQ 578
Cdd:PLN02574 458 YK-GFQIAPADLEAVLISHPEIIDAAVTAVPDKecgEIPVAFVVRRQ 503
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-533 |
1.07e-20 |
|
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: 93.88 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLI--AGMTGQCERIPElgpKDTYVGYLPLAHVLELT-AEISCVTYGCRIGYSSP 304
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGERLGLTE---QDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 305 LTlsDQSSKIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYIQRTLFKIGydykleqikrgydaplcnil 382
Cdd:cd05917 78 SF--DPLAVLEAIEKEKCTALHgvPTMFIA-----------------ELEHPDFDKFDLS-------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 lfkkvkallggNVRMMLSGGAPLSPQT-QRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGR---VGAPLICCEIKL 458
Cdd:cd05917 119 -----------SLRTGIMAGAPCPPELmKRVIEVMNMKDVTIAYGMTETSPVSTQTRTDDSIEKRvntVGRIMPHTEAKI 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1935119612 459 RDwQEGGYTCrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDfsvDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:cd05917 188 VD-PEGGIVP--PVGVPGELCIRGYSVMKGYWNDPEKTAE---AIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI 256
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
77-551 |
2.35e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 94.95 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRwLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFK-------YNFPLVtlyatlgEEAVT 149
Cdd:PRK07798 22 LVCGDRR-LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKaravpvnVNYRYV-------EDELR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 150 YGLNESGASYLITSVELLEsKLKPALSEIPGLKHIIYVDKKTINKSEyPEGLEIHSMQTveelGAKPENLDIPPSkpvPT 229
Cdd:PRK07798 94 YLLDDSDAVALVYEREFAP-RVAEVLPRLPKLRTLVVVEDGSGNDLL-PGAVDYEDALA----AGSPERDFGERS---PD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLaLIMYTSGSTGRPKGVMMIHKNL-------IAGMTG--------QCERIPELGPKDTYVgYLPLAHVLELTAEISCVT 294
Cdd:PRK07798 165 DL-YLLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGepiedeeeLAKRAAAGPGMRRFP-APPLMHGAGQWAAFAALF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 295 ygcrigysspltlsdqsskikkgsKGDCTVLKPTLMAAVPEIMDRIYKNvmsKVQEMnyiqrtlFKIGydykleqikrgy 374
Cdd:PRK07798 243 ------------------------SGQTVVLLPDVRFDADEVWRTIERE---KVNVI-------TIVG------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 375 DA---PLcnillfkkVKALLGGN------VRMMLSGGAPLSPQT-QRFM----NICfccpVGQGYGLTET--CGAGTITE 438
Cdd:PRK07798 277 DAmarPL--------LDALEARGpydlssLFAIASGGALFSPSVkEALLellpNVV----LTDSIGSSETgfGGSGTVAK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 439 VSDYSTG-RVGAplicceiklrdwqeGGYTC----RDKPNPRGEIIIG----GPNVSMGYFKNEEKT-EDFSVdENGQRW 508
Cdd:PRK07798 345 GAVHTGGpRFTI--------------GPRTVvldeDGNPVEPGSGEIGwiarRGHIPLGYYKDPEKTaETFPT-IDGVRY 409
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1935119612 509 FCTGDIGEFHPDGCLQIIDRkKDLVKLQAGEYVSLGKVETALK 551
Cdd:PRK07798 410 AIPGDRARVEADGTITLLGR-GSVCINTGGEKVFPEEVEEALK 451
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
85-576 |
1.47e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.64 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLESKLKPALSEIPglkhiIYVdkkTINKSEYPEG--LEIHSMQTVEELGAKPENLDIPPskpvptDLALIMYTSGSTG 242
Cdd:PRK05852 124 DGPHDRAEPTTRWWP-----LTV---NVGGDSGPSGgtLSVHLDAATEPTPATSTPEGLRP------DDAMIMFTGGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 243 RPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTAEI-SCVTYGCRI-----GYSSPLTLSDqsskikk 316
Cdd:PRK05852 190 LPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYHGHGLIAALlATLASGGAVllparGRFSAHTFWD------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 317 gskgDCTVLKPTLMAAVPeimdriyknvmskvqemnyiqrTLFKIGYDYKLEQIKRGYDAPLcnillfkkvkallggnvR 396
Cdd:PRK05852 262 ----DIKAVGATWYTAVP----------------------TIHQILLERAATEPSGRKPAAL-----------------R 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 397 MMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDY--------STGRVG---APLIccEIKLRDWQEGG 465
Cdd:PRK05852 299 FIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIgqtenpvvSTGLVGrstGAQI--RIVGSDGLPLP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 466 ytcrdkPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGK 545
Cdd:PRK05852 377 ------AGAVGEVWLRGTTVVRGYLGDPTITAANFTDG----WLRTGDLGSLSAAGDLSIRGRIKELIN-RGGEKISPER 445
|
490 500 510
....*....|....*....|....*....|....
gi 1935119612 546 VETALKNCPFIDNICAYAKSDQSY---VISFVVP 576
Cdd:PRK05852 446 VEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
230-554 |
1.83e-19 |
|
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: 89.87 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCErIPELGPKDTYVGYLPLAHvleltaeiscvTYGCRIGYSSPLTlsd 309
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFH-----------TFGYKAGIVACLL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 qsskikKGSkgdcTVLkPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGY--DYKLEQIKRGYD-APLCNILLFKK 386
Cdd:cd17638 66 ------TGA----TVV-PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGrkKFDLSSLRAAVTgAATVPVELVRR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 387 VKALLGgnvrmmlsggaplspqtqrFMNicfccpVGQGYGLTEtCGAGTITEVSDYST---GRVGAPLICCEIKLRDwqe 463
Cdd:cd17638 135 MRSELG-------------------FET------VLTAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 464 ggytcrdkpnpRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSL 543
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAE-AIDADG--WLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYP 250
|
330
....*....|.
gi 1935119612 544 GKVETALKNCP 554
Cdd:cd17638 251 AEVEGALAEHP 261
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
85-576 |
3.71e-19 |
|
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: 90.45 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITsv 164
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldiPPSkpvPTDLALIMYTSGSTGRP 244
Cdd:cd17653 101 ---------------------------------------------------------TDS---PDDLAYIIFTSGSTGIP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLI-------AGMTgqceripeLGPKDTyvgylpLAHVLELTAEISCVTYGCRIGYSSPLTLSDQSSKIKKG 317
Cdd:cd17653 121 KGVMVPHRGVLnyvsqppARLD--------VGPGSR------VAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 318 SKG-DCTVLKPTLMAAVPeimdriyknvmskvqemnyiqrtlfkigydykleqiKRGYDaplcnillfkkvkallggNVR 396
Cdd:cd17653 187 ARTvDALMSTPSILSTLS------------------------------------PQDFP------------------NLK 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 397 MMLSGGAPLSP-------QTQRFMNicfccpvgqGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDWQEggytcR 469
Cdd:cd17653 213 TIFLGGEAVPPslldrwsPGRRLYN---------AYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADL-----Q 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 470 DKPNPR-GEIIIGGPNVSMGYFKNEEKTED---FSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 545
Cdd:cd17653 279 PVPEGVvGEICISGVQVARGYLGNPALTASkfvPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR-GFRINLEE 357
|
490 500 510
....*....|....*....|....*....|..
gi 1935119612 546 VE-TALKNCPFIDNicAYAKSDQSYVISFVVP 576
Cdd:cd17653 358 IEeVVLQSQPEVTQ--AAAIVVNGRLVAFVTP 387
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
77-533 |
4.04e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 91.09 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNF---PLVTLYaTLGEeaVTYGLN 153
Cdd:PRK07514 21 IETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAvflPLNTAY-TLAE--LDYFIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 154 ESGASYLITSvelleSKLKPALSEIPglkhiiyvdkktinkseypeglEIHSMQTVEELGAKPEN------LDIPPS-KP 226
Cdd:PRK07514 98 DAEPALVVCD-----PANFAWLSKIA----------------------AAAGAPHVETLDADGTGslleaaAAAPDDfET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 227 VPT---DLALIMYTSGSTGRPKGVMMIHKNLI--AGMTGQCERIpelGPKDTYVGYLPLAHVLELTAEISCvtygcrigy 301
Cdd:PRK07514 151 VPRgadDLAAILYTSGTTGRSKGAMLSHGNLLsnALTLVDYWRF---TPDDVLIHALPIFHTHGLFVATNV--------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 302 ssplTLSDQSSKIkkgskgdctvLKPTL-MAAVPEIMDRiyKNVMSKVQemnyiqrTLfkigYDYKLEQikRGYDAPLCn 380
Cdd:PRK07514 219 ----ALLAGASMI----------FLPKFdPDAVLALMPR--ATVMMGVP-------TF----YTRLLQE--PRLTREAA- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 illfkkvkallgGNVRMMLSGGAPLSPQTQRfmniCFCCPVGQG----YGLTETC--------G---AGTitevsdystg 445
Cdd:PRK07514 269 ------------AHMRLFISGSAPLLAETHR----EFQERTGHAilerYGMTETNmntsnpydGerrAGT---------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 446 rVGAPLICCEIKLRDWQEGgytcrdKPNPRGEI--I-IGGPNVSMGYFKNEEKT-EDFSVDenGqrWFCTGDIGEFHPDG 521
Cdd:PRK07514 323 -VGFPLPGVSLRVTDPETG------AELPPGEIgmIeVKGPNVFKGYWRMPEKTaEEFRAD--G--FFITGDLGKIDERG 391
|
490
....*....|..
gi 1935119612 522 CLQIIDRKKDLV 533
Cdd:PRK07514 392 YVHIVGRGKDLI 403
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
225-582 |
4.19e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 91.27 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 225 KP--VPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTgQCERI--PELGP-KDTYVGYLPLAHVLELTaeISCVTYgcri 299
Cdd:PRK08974 200 KPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QAKAAygPLLHPgKELVVTALPLYHIFALT--VNCLLF---- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 300 gysspltlsdqsskIKKGSKGdctvLKPTLMAAVPEIMDRIYKNVMSKVQEMNyiqrTLFkigydykleqikrgydaplc 379
Cdd:PRK08974 273 --------------IELGGQN----LLITNPRDIPGFVKELKKYPFTAITGVN----TLF-------------------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 380 NILL----FKKVKAllgGNVRMMLSGGAPL-SPQTQRFMNICfCCPVGQGYGLTEtCG---AGTITEVSDYStGRVGAPL 451
Cdd:PRK08974 311 NALLnneeFQELDF---SSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTE-CSplvSVNPYDLDYYS-GSIGLPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 452 ICCEIKLRDwQEGGYTCRDKPnprGEIIIGGPNVSMGYFKNEEKTEDfsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 531
Cdd:PRK08974 385 PSTEIKLVD-DDGNEVPPGEP---GELWVKGPQVMLGYWQRPEATDE--VIKDG--WLATGDIAVMDEEGFLRIVDRKKD 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 532 LVkLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQS---YVISFVVPNQKKLT 582
Cdd:PRK08974 457 MI-LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLT 509
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
223-582 |
9.14e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 90.08 E-value: 9.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 223 PSKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTgQCE-----------RIPELgpkdTYVGYLPLAHVLELTAeis 291
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-QMEawlqpafekkpRPDQL----NFVCALPLYHIFALTV--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 292 CVTYGCRIGYSSPLTLS--DQSSKIKKGSKgdctvLKPTLMAAVpeimdriyknvmskvqemnyiqRTLFkigydykleq 369
Cdd:PRK07059 270 CGLLGMRTGGRNILIPNprDIPGFIKELKK-----YQVHIFPAV----------------------NTLY---------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 370 ikrgydaplcNILL---------FKKVKALLGGnvrmmlsGGAPLSPQTQRFMNICfCCPVGQGYGLTET-----CGAGT 435
Cdd:PRK07059 313 ----------NALLnnpdfdkldFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETspvatCNPVD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 436 ITEVsdysTGRVGAPLICCEIKLRDwQEGgytcRDKPNPR-GEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDI 514
Cdd:PRK07059 375 ATEF----SGTIGLPLPSTEVSIRD-DDG----NDLPLGEpGEICIRGPQVMAGYWNRPDETAK-VMTADG--FFRTGDV 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935119612 515 GEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQ---SYVISFVVPNQKKLT 582
Cdd:PRK07059 443 GVMDERGYTKIVDRKKDMI-LVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEhsgEAVKLFVVKKDPALT 512
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
28-656 |
1.09e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 89.94 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 28 ATIDIPGADTLDKLFDHAVAKFgkKDClgtreilseenemqPNGKVFKKLIlgnyrwlNYEDINQRVNHFGRGLAAQ-GL 106
Cdd:PRK08751 17 AEIDLEQFRTVAEVFATSVAKF--ADR--------------PAYHSFGKTI-------TYREADQLVEQFAAYLLGElQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 107 KPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITsVELLESKLKPALSEIPgLKHII- 185
Cdd:PRK08751 74 KKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVV-IDNFGTTVQQVIADTP-VKQVIt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 186 --------------------YVDK----KTINKS-EYPEGLEIHSMQTVeelgakpenldiPPSKPVPTDLALIMYTSGS 240
Cdd:PRK08751 152 tglgdmlgfpkaalvnfvvkYVKKlvpeYRINGAiRFREALALGRKHSM------------PTLQIEPDDIAFLQYTGGT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 241 TGRPKGVMMIHKNLIAGMTGQCERIPELGP----KDTYVGYLPLAHVLELTAE--ISCVTYGCRIGYSSPltlSDQSSKI 314
Cdd:PRK08751 220 TGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTANglVFMKIGGCNHLISNP---RDMPGFV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 315 KKgskgdctvLKPTLMAAVPEImdriyknvmskvqemnyiqRTLFKigydyKLeqikrgYDAPLCNILLFKKVKALLGGN 394
Cdd:PRK08751 297 KE--------LKKTRFTAFTGV-------------------NTLFN-----GL------LNTPGFDQIDFSSLKMTLGGG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 395 VRMMLSggapLSPQTQRFMNIcfccPVGQGYGLTETCGAGTITEVS--DYStGRVGAPLICCEIKLRDwqeggytcrDKP 472
Cdd:PRK08751 339 MAVQRS----VAERWKQVTGL----TLVEAYGLTETSPAACINPLTlkEYN-GSIGLPIPSTDACIKD---------DAG 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 473 N--PRGEI---IIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVE 547
Cdd:PRK08751 401 TvlAIGEIgelCIKGPQVMKGYWKRPEETAK-VMDADG--WLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIE 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 548 TALKNCPFIDNICAYAksdqsyvisfvVPNQKKLTVlaeqkgVKGTWVEicNNPIMEAEilkEIKEVAdKMKLERFETPI 627
Cdd:PRK08751 477 DVIAMMPGVLEVAAVG-----------VPDEKSGEI------VKVVIVK--KDPALTAE---DVKAHA-RANLTGYKQPR 533
|
650 660
....*....|....*....|....*....
gi 1935119612 628 KVRLSPEpwTPEtglvTDAFKLKRKELKN 656
Cdd:PRK08751 534 IIEFRKE--LPK----TNVGKILRRELRD 556
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
85-576 |
1.51e-18 |
|
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: 88.91 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEwMIAAqtcfkynfplvtLYATLGeeavtyglneSGASYLitsv 164
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPD-LVVA------------LLAVLK----------AGAAYV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellesKLKPAlseipglkhiiyvdkktinkseYPEgleihsmqtvEELGAKPENLDIPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:cd12115 78 -----PLDPA----------------------YPP----------ERLRFILEDAQARLVLTDPDDLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGM--TGQceripELGPKDtyvgylpLAHVLELTA--------EISC-VTYGCRIGY-SSPLTLSDQss 312
Cdd:cd12115 121 KGVAIEHRNAAAFLqwAAA-----AFSAEE-------LAGVLASTSicfdlsvfELFGpLATGGKVVLaDNVLALPDL-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 313 kikkGSKGDCTVLK--PTLMAAVPEiMDRIYKNVmskvQEMNY----IQRTLF-KIgydYKLEQIKRGYDaplcnillfk 385
Cdd:cd12115 187 ----PAAAEVTLINtvPSAAAELLR-HDALPASV----RVVNLagepLPRDLVqRL---YARLQVERVVN---------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 386 kvkaLLGGNVRMMLSGGAPLSPQTQRFMNICFccPVgqgygltetcgAGTITEVSDystgRVGAPLicceiklrdwqegg 465
Cdd:cd12115 245 ----LYGPSEDTTYSTVAPVPPGASGEVSIGR--PL-----------ANTQAYVLD----RALQPV-------------- 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 466 ytcrdKPNPRGEIIIGGPNVSMGYFKNEEKT-EDFSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVS 542
Cdd:cd12115 290 -----PLGVPGELYIGGAGVARGYLGRPGLTaERFLPDpfGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVR-GFRIE 363
|
490 500 510
....*....|....*....|....*....|....*..
gi 1935119612 543 LGKVETALKNCPFIDNICAYAKSDQS---YVISFVVP 576
Cdd:cd12115 364 LGEIEAALRSIPGVREAVVVAIGDAAgerRLVAYIVA 400
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-566 |
1.88e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 88.65 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 93 RVNHFGRGLAAQGLKPKSAIAI-------FCETRAEWMIAAQTCFKYnfpLVTLYATLGEEAVTYgLNESGASYLITSVE 165
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLilpnrftYIELSFAVAYAGGRLGLV---FVPLNPTLKESVLRY-LVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 166 LLESKLKPALSEIPGLKHIIYVDkktinkseypegleihsmqtveelGAKPENLDIPPSKPVPTDLALIMYTSGSTGRPK 245
Cdd:cd05922 78 GAADRLRDALPASPDPGTVLDAD------------------------GIRAARASAPAHEVSHEDLALLLYTSGSTGSPK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 246 GVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTAEISCVTYGCRI----GYSSPLTLSDqsskikkgskgD 321
Cdd:cd05922 134 LVRLSHQNLLANARSIAEYL-GITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDDAFWE-----------D 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 322 CTVLKPTLMAAVPeimdriyknvmskvqemnYIQRTLFKIGYDykleqikrgyDAPLCNIllfkkvkallggnvRMMLSG 401
Cdd:cd05922 202 LREHGATGLAGVP------------------STYAMLTRLGFD----------PAKLPSL--------------RYLTQA 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 402 GAPLSPQT-QRFmnicfcCPVGQG------YGLTETCGAGTI--TEVSDYSTGRVGAPLICCEIKLRDwQEGGytcRDKP 472
Cdd:cd05922 240 GGRLPQETiARL------RELLPGaqvyvmYGQTEATRRMTYlpPERILEKPGSIGLAIPGGEFEILD-DDGT---PTPP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 473 NPRGEIIIGGPNVSMGYFkNEEKTEDFSVDENGQRWfcTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVETALKN 552
Cdd:cd05922 310 GEPGEIVHRGPNVMKGYW-NDPPYRRKEGRGGGVLH--TGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIEAAARS 385
|
490
....*....|....
gi 1935119612 553 CPFIDNICAYAKSD 566
Cdd:cd05922 386 IGLIIEAAAVGLPD 399
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
60-563 |
2.06e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 89.05 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 60 ILSEENEMQPNgkvfKKLILGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAE---------WMIAAQTcf 130
Cdd:PRK06155 26 MLARQAERYPD----RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEfldvflgcaWLGAIAV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 131 kynfPLVTlyATLGEEaVTYGLNESGASYLITSVELLESkLKPALSEIPGLKHIIYVDKKtiNKSEYPEGLEIHSMQTVE 210
Cdd:PRK06155 100 ----PINT--ALRGPQ-LEHILRNSGARLLVVEAALLAA-LEAADPGDLPLPAVWLLDAP--ASVSVPAGWSTAPLPPLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 211 ELgakpenldIPPSKPVPTDLALIMYTSGSTGRPKGVMMIHKNL-IAG-MTGqceRIPELGPKDTYVGYLPLAHVLELTA 288
Cdd:PRK06155 170 AP--------APAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyWWGrNSA---EDLEIGADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 289 EISCVTYGCRIgysspltlsdqsskikkgskgdctVLKPTLMAAvpeimdRIYKNVmskvqemnyiQRTLFKIGYdykle 368
Cdd:PRK06155 239 FFQALLAGATY------------------------VLEPRFSAS------GFWPAV----------RRHGATVTY----- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 369 qikrgYDAPLCNILLFKKVKALLGGN-VRMMLSGGAPlsPQTQRFMNICFCCPVGQGYGLTET---CGaGTITEVSDYST 444
Cdd:PRK06155 274 -----LLGAMVSILLSQPARESDRAHrVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETnfvIA-VTHGSQRPGSM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 445 GRVgAPLIccEIKLRDwqEGGytcRDKPNPR-GEIIIGG--PNVSM-GYFKNEEKTedfsVDENGQRWFCTGDIGEFHPD 520
Cdd:PRK06155 346 GRL-APGF--EARVVD--EHD---QELPDGEpGELLLRAdePFAFAtGYFGMPEKT----VEAWRNLWFHTGDRVVRDAD 413
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1935119612 521 GCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICAYA 563
Cdd:PRK06155 414 GWFRFVDRIKDAIRRR-GENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
236-641 |
6.41e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 86.97 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 236 YTSGSTGRPKGVMMIHKN-----LIAGMTGqceripELGPKDTYVGYLPLAHvleltaeiscvtygCRiGYSSPLTLSdq 310
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGaylnaLANILEW------EMKQHPVYLWTLPMFH--------------CN-GWCFPWTVA-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 311 sskikkgSKGDCTVLKPTLMAavPEIMDRIYKNvmsKVQEMNyiqrtlfkigydykleqikrgyDAPLCNILLF---KKV 387
Cdd:cd12118 197 -------AVGGTNVCLRKVDA--KAIYDLIEKH---KVTHFC----------------------GAPTVLNMLAnapPSD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 388 KALLGGNVRMMlSGGAPLSPQT-QRFMNICFCcpVGQGYGLTETCGAGTITEVSDYSTG-----------RVGAPLICCE 455
Cdd:cd12118 243 ARPLPHRVHVM-TAGAPPPAAVlAKMEELGFD--VTHVYGLTETYGPATVCAWKPEWDElpteerarlkaRQGVRYVGLE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 456 -IKLRDWQEGgytcrdKPNPR-----GEIIIGGPNVSMGYFKNEEKT-EDFsvdENGqrWFCTGDIGEFHPDGCLQIIDR 528
Cdd:cd12118 320 eVDVLDPETM------KPVPRdgktiGEIVFRGNIVMKGYLKNPEATaEAF---RGG--WFHSGDLAVIHPDGYIEIKDR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 529 KKDLVkLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSYVIS---FVvpnqkKLtvlaeQKGVKGTwveicnnpimEA 605
Cdd:cd12118 389 SKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVpcaFV-----EL-----KEGAKVT----------EE 447
|
410 420 430
....*....|....*....|....*....|....*.
gi 1935119612 606 EILKEIKEvadkmKLERFETPIKVRLSPEPWTPeTG 641
Cdd:cd12118 448 EIIAFCRE-----HLAGFMVPKTVVFGELPKTS-TG 477
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
85-533 |
6.60e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 87.40 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYL---- 160
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcld 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 161 --------ITSVELLESKLKPALSE-IPGLKHIIY--VDKKTINK-SEYPEGLEIHSMQTVE-------ELGAKPENldi 221
Cdd:PRK06710 130 lvfprvtnVQSATKIEHVIVTRIADfLPFPKNLLYpfVQKKQSNLvVKVSESETIHLWNSVEkevntgvEVPCDPEN--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 222 ppskpvptDLALIMYTSGSTGRPKGVMMIHKNLIAG-MTG-----QCERIPELgpkdtYVGYLPLAHVLELTAEIS-CVT 294
Cdd:PRK06710 207 --------DLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGvqwlyNCKEGEEV-----VLGVLPFFHVYGMTAVMNlSIM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 295 YGCRIGYSSPLTLSDQSSKIKKGskgdctvlKPTLMAAVPEImdriyknvmskvqemnYIQrtlfkigydykleqikrgy 374
Cdd:PRK06710 274 QGYKMVLIPKFDMKMVFEAIKKH--------KVTLFPGAPTI----------------YIA------------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 375 dapLCNILLFKKVKAllgGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYST-GRVGAPLIC 453
Cdd:PRK06710 311 ---LLNSPLLKEYDI---SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 454 CEIKLRDWQEGGYTcrdKPNPRGEIIIGGPNVSMGYFKNEEKTEdfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:PRK06710 385 TEAMIMSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETA--AVLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMI 457
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
206-556 |
8.86e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 86.78 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 206 MQTVEELGAKPENLDIPPSKPVPTD-LALIMYTSGSTGRPKGVMMIHKNLIA-----GMTGQceripeLGPKDTYVGYLP 279
Cdd:PRK09088 111 VEDLAAFIASADALEPADTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQtahnfGVLGR------VDAHSSFLCDAP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 280 LAHVLELTAEI-SCVTYGCRI----GYSSPLTLsdqsskikkGSKGDCTvLKPTLMAAVPEIMDRIyknvmskvqemnyi 354
Cdd:PRK09088 185 MFHIIGLITSVrPVLAVGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAF-------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 355 qrtlfkigydykleQIKRGYDAplcnillfkkvKALlgGNVRMMLSGGAPlSPQTQRFMNICFCCPVGQGYGLTEtcgAG 434
Cdd:PRK09088 241 --------------RAQPGFDA-----------AAL--RHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSE---AG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 435 TITEVS---DYSTGRVGAPLICC-EIKLRDWQEGGYTCRdkPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFC 510
Cdd:PRK09088 290 TVFGMSvdcDVIRAKAGAAGIPTpTVQTRVVDDQGNDCP--AGVPGELLLRGPNLSPGYWRRPQATAR-AFTGDG--WFR 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1935119612 511 TGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVETALKNCPFI 556
Cdd:PRK09088 365 TGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-581 |
8.97e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT 4654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 SVELLEsklkpalsEIPglkhiiyvdkktinkseYPEGLEIHSMQTVEELGAKPENldIPPSKPVPTDLALIMYTSGSTG 242
Cdd:PRK12316 4655 QSHLLQ--------RLP-----------------IPDGLASLALDRDEDWEGFPAH--DPAVRLHPDNLAYVIYTSGSTG 4707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 243 RPKGVMMIHKNLIAGMTGQCERiPELGPKDTYVGYLPLAhvLELTAEiscvtygcriGYSSPLTlsdqsskikkgsKGDC 322
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFS--FDGSHE----------GLYHPLI------------NGAS 4762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 323 TVLKPTLMAAVPEIMDRIYKNVMSKVQemnyiqrtlFKIGYDYKLEQIKRGYDAPlcnillfkkvkallgGNVRMMLSGG 402
Cdd:PRK12316 4763 VVIRDDSLWDPERLYAEIHEHRVTVLV---------FPPVYLQQLAEHAERDGEP---------------PSLRVYCFGG 4818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 403 APLSPQTQRFMnICFCCPVG--QGYGLTETCGAGTITEVSDYST-GRVGAPlICCEIKLRdwqeGGYTCRDKPNPR---- 475
Cdd:PRK12316 4819 EAVAQASYDLA-WRALKPVYlfNGYGPTETTVTVLLWKARDGDAcGAAYMP-IGTPLGNR----SGYVLDGQLNPLpvgv 4892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 476 -GEIIIGGPNVSMGYFKNEEKT-EDF---SVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETAL 550
Cdd:PRK12316 4893 aGELYLGGEGVARGYLERPALTaERFvpdPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIR-GFRIELGEIEARL 4971
|
490 500 510
....*....|....*....|....*....|...
gi 1935119612 551 KNCPFIDN--ICAYAKSDQSYVISFVVPNQKKL 581
Cdd:PRK12316 4972 REHPAVREavVIAQEGAVGKQLVGYVVPQDPAL 5004
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
102-587 |
1.19e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 86.55 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 102 AAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVELLEsKLKPALSEIpGL 181
Cdd:PRK08314 54 QECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAP-KVAPAVGNL-RL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 182 KHII------YVDKKtinkSEY--PEGLEI-HSMQTVEELGAKP------ENLDIPPSKPVPTDLALIMYTSGSTGRPKG 246
Cdd:PRK08314 132 RHVIvaqysdYLPAE----PEIavPAWLRAePPLQALAPGGVVAwkealaAGLAPPPHTAGPDDLAVLPYTSGTTGVPKG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 247 VMMIHKNLIAGMTGQCeRIPELGPKDTYVGYLPLAHVLeltaeiscvtyGCRIGYSSP---------LTLSDQSSKIKKG 317
Cdd:PRK08314 208 CMHTHRTVMANAVGSV-LWSNSTPESVVLAVLPLFHVT-----------GMVHSMNAPiyagatvvlMPRWDREAAARLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 318 SKGDCTVLK--PTLMA---AVPEIMDRIYKNVMSkvqemnyiqrtlfkigydykleqikrgydaplcnillfkkvkalLG 392
Cdd:PRK08314 276 ERYRVTHWTniPTMVVdflASPGLAERDLSSLRY--------------------------------------------IG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 393 GnvrmmlsGGAPLsPQT------QRFmNICFCcpvgQGYGLTETcGAGTITEVSDystgR-----VGAPLICCEIKLRDW 461
Cdd:PRK08314 312 G-------GGAAM-PEAvaerlkELT-GLDYV----EGYGLTET-MAQTHSNPPD----RpklqcLGIPTFGVDARVIDP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 462 QeggyTCRDKP-NPRGEIIIGGPNVSMGYFKNEEKTEDFSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEY 540
Cdd:PRK08314 374 E----TLEELPpGEVGEIVVHGPQVFKGYWNRPEATAEAFIEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFK 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1935119612 541 VSLGKVETALKNCPFIDNICAYAKSDQ---SYVISFVVPNQ-KKLTVLAEQ 587
Cdd:PRK08314 449 VWPAEVENLLYKHPAIQEACVIATPDPrrgETVKAVVVLRPeARGKTTEEE 499
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
229-567 |
1.62e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 86.19 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 229 TDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERI-PELGPKDTYVGYLPLAHVLELTAeISCVTYgcrigysspltl 307
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVgPEMIGQVVTLGLIPFFHIYGITG-ICCATL------------ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 308 sDQSSKIKKGSKGDCTVLKPTLMAA-------VPEIMDRIYKNVMskVQEmnyiqrtlfkigydYKLEQIKrgydaplcn 380
Cdd:PLN02330 251 -RNKGKVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKNPI--VEE--------------FDLSKLK--------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 illfkkvkallggnVRMMLSGGAPLSPQ-----TQRFMNIcfccPVGQGYGLTE-TCGagTITEvSDYSTGR-------V 447
Cdd:PLN02330 305 --------------LQAIMTAAAPLAPElltafEAKFPGV----QVQEAYGLTEhSCI--TLTH-GDPEKGHgiakknsV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 448 GAPLICCEIKLRDWQEGgytcRDKP-NPRGEIIIGGPNVSMGYFKNEEKTeDFSVDENGqrWFCTGDIGEFHPDGCLQII 526
Cdd:PLN02330 364 GFILPNLEVKFIDPDTG----RSLPkNTPGELCVRSQCVMQGYYNNKEET-DRTIDEDG--WLHTGDIGYIDDDGDIFIV 436
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1935119612 527 DRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICAYAKSDQ 567
Cdd:PLN02330 437 DRIKELIKYK-GFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
212-550 |
3.46e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 84.66 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 212 LGAKPENLDIPPSKPV--------------PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGY 277
Cdd:PRK07787 97 LGPAPDDPAGLPHVPVrlharswhrypepdPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW-QWTADDVLVHG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 278 LPLAHVleltaeiscvtYGCRIGYSSPLTLSDQSSKIKKGSK---GDCTVLKPTLMAAVPEIMDRIYKNVmskvqemnyi 354
Cdd:PRK07787 176 LPLFHV-----------HGLVLGVLGPLRIGNRFVHTGRPTPeayAQALSEGGTLYFGVPTVWSRIAADP---------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 355 qrtlfkigydykleqikrgyDAPlcnillfkkvKALlgGNVRMMLSGGAPLS-PQTQRFMNICFCCPVgQGYGLTETcga 433
Cdd:PRK07787 235 --------------------EAA----------RAL--RGARLLVSGSAALPvPVFDRLAALTGHRPV-ERYGMTET--- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 434 gTITeVS-----DYSTGRVGAPLICCEIKLRDwqEGGYTCRDKPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrW 508
Cdd:PRK07787 279 -LIT-LStradgERRPGWVGLPLAGVETRLVD--EDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAA-AFTADG--W 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1935119612 509 FCTGDIGEFHPDGCLQIIDRKK-DLVKlqAGEY-VSLGKVETAL 550
Cdd:PRK07787 352 FRTGDVAVVDPDGMHRIVGREStDLIK--SGGYrIGAGEIETAL 393
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
228-586 |
4.11e-17 |
|
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: 84.28 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGqCERIPELGPKDTYVgylpLAH-------VLELtaeISCVTYGCRIG 300
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDDVWT----LFHsyafdfsVWEI---WGALLHGGRLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 301 YSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAavpeimdriYKNVMSKVQEMNyiqrtlfkigydykleqikrgyDAPLcn 380
Cdd:cd17643 164 VVPYEVARSPEDFARLLRDEGVTVLNQTPSA---------FYQLVEAADRDG----------------------RDPL-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 illfkkvkallggNVRMMLSGGAPLSPQTQRFMNICFCCPVGQ---GYGLTETCGAGTITEVSDYSTGRVGAPLICCEIK 457
Cdd:cd17643 211 -------------ALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETTVHVTFRPLDAADLPAAAASPIGRPLP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 458 lrDWQEGGYTCRDKPNPR---GEIIIGGPNVSMGYF-KNEEKTEDFSVDEN---GQRWFCTGDIGEFHPDGCLQIIDRKK 530
Cdd:cd17643 278 --GLRVYVLDADGRPVPPgvvGELYVSGAGVARGYLgRPELTAERFVANPFggpGSRMYRTGDLARRLPDGELEYLGRAD 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1935119612 531 DLVKLQaGEYVSLGKVETALKNCPFIDNICAYAKSD---QSYVISFVVPNQKKLTVLAE 586
Cdd:cd17643 356 EQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDepgDTRLVAYVVADDGAAADIAE 413
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
176-554 |
4.95e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.85 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 176 SEIPGLKHIIYVDKKTinKSEYPEGLEIHSMQTVEELGAKPENLDIppsKPVPTDLALIMYTSGSTGRPKGVMMIHKNLI 255
Cdd:PLN02860 124 DRLPSLMWQVFLESPS--SSVFIFLNSFLTTEMLKQRALGTTELDY---AWAPDDAVLICFTSGTTGRPKGVTISHSALI 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 256 A------GMTGQCEripelgpKDTYVGYLPLAHVleltaeiscvtyGcriGYSSPLTLSdqsskikkgSKGDCTVLKPTL 329
Cdd:PLN02860 199 VqslakiAIVGYGE-------DDVYLHTAPLCHI------------G---GLSSALAML---------MVGACHVLLPKF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 330 MAAVpeIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYKLEQIKRGydaplcnillfkkvkallggnVRMMLSGGAPLSPQ- 408
Cdd:PLN02860 248 DAKA--ALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPS---------------------VRKILNGGGSLSSRl 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 409 TQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPL-ICCEIKLRDWQEGGYTCRDKPNPRGEIIIG------ 481
Cdd:PLN02860 305 LPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLqTVNQTKSSSVHQPQGVCVGKPAPHVELKIGldessr 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 482 -------GPNVSMGYF-KNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNC 553
Cdd:PLN02860 385 vgriltrGPHVMLGYWgQNSETASVLSNDG----WLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQH 459
|
.
gi 1935119612 554 P 554
Cdd:PLN02860 460 P 460
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
85-566 |
6.76e-17 |
|
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: 83.71 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLEsklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippsKPVPTDLALIMYTSGSTGRP 244
Cdd:cd05969 81 ELYE--------------------------------------------------------RTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIA-GMTGQceRIPELGPKDTYVgylplahvleLTAEISCVTyGCRIGYSSPLTLSdqsskikkgskgdCT 323
Cdd:cd05969 105 KGVLHVHDAMIFyYFTGK--YVLDLHPDDIYW----------CTADPGWVT-GTVYGIWAPWLNG-------------VT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 324 VLkptlmaavpeimdriyknvmskVQEMNYIQRTLFKIGYDYKleqIKRGYDAPlCNILLFKKVKALLG-----GNVRMM 398
Cdd:cd05969 159 NV----------------------VYEGRFDAESWYGIIERVK---VTVWYTAP-TAIRMLMKEGDELArkydlSSLRFI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 399 LSGGAPLSPQTQRFMNICFCCPVGQGYGLTETcgaGTITeVSDY-----STGRVGAPLICCEIKLRDwQEGGYTcrdKPN 473
Cdd:cd05969 213 HSVGEPLNPEAIRWGMEVFGVPIHDTWWQTET---GSIM-IANYpcmpiKPGSMGKPLPGVKAAVVD-ENGNEL---PPG 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 474 PRGEIII--GGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVETALK 551
Cdd:cd05969 285 TKGILALkpGWPSMFRGIWNDEERYKNSFIDG----WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALM 359
|
490
....*....|....*
gi 1935119612 552 NCPFIDNICAYAKSD 566
Cdd:cd05969 360 EHPAVAEAGVIGKPD 374
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
228-577 |
8.52e-17 |
|
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: 83.75 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLA---HVLE-LTAEIS----CVTygcri 299
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG-LTSESRVLQFASYTfdvSILEiFTTLAAggclCIP----- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 300 gySSPLTLSDQSSKIKKgSKGDCTVLKPTLMA-----AVPEImdriyknvmskvqemnyiqRTLFKIGydyklEQIKRgy 374
Cdd:cd05918 179 --SEEDRLNDLAGFINR-LRVTWAFLTPSVARlldpeDVPSL-------------------RTLVLGG-----EALTQ-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 375 daplcnillfkKVKALLGGNVRMMlsggaplspqtqrfmnicfccpvgQGYGLTETCGAGTITEVSDYSTGR-VGAPL-- 451
Cdd:cd05918 230 -----------SDVDTWADRVRLI------------------------NAYGPAECTIAATVSPVVPSTDPRnIGRPLga 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 452 ICCEIKLRDwqeggytcRDKPNPR---GEIIIGGPNVSMGYFKNEEKTED-F---------SVDENGQRWFCTGDIGEFH 518
Cdd:cd05918 275 TCWVVDPDN--------HDRLVPIgavGELLIEGPILARGYLNDPEKTAAaFiedpawlkqEGSGRGRRLYRTGDLVRYN 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1935119612 519 PDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNC-PFIDNICA--YAKSD---QSYVISFVVPN 577
Cdd:cd05918 347 PDGSLEYVGRKDTQVKIR-GQRVELGEIEHHLRQSlPGAKEVVVevVKPKDgssSPQLVAFVVLD 410
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
77-658 |
1.40e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 83.06 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWlNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESG 156
Cdd:PRK08316 30 LVFGDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITS---VELLESKLKPALSEIPGLKHIIYvdkktinKSEYPEGLeiHSMQTVEELGAKPENLDIPPSkpvpTDLAL 233
Cdd:PRK08316 109 ARAFLVDpalAPTAEAALALLPVDTLILSLVLG-------GREAPGGW--LDFADWAEAGSVAEPDVELAD----DDLAQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 234 IMYTSGSTGRPKGVMMIHKNLIAGMTGqCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYgcrIGYSSPLTLSdqssk 313
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTHRALIAEYVS-CIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLY---VGATNVILDA----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 314 ikkgskgdctvlkPTLmaavPEIMDRIYKnvmskvqemnYIQRTLFkigydykleqikrgydAP------LCNILLFKKV 387
Cdd:PRK08316 247 -------------PDP----ELILRTIEA----------ERITSFF----------------APptvwisLLRHPDFDTR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 388 ------KALLGGNVrMmlsGGAPLSPQTQRFMNICF--CcpvgqgYGLTETCGAGTI--TEVSDYSTGRVGAPLICCEIK 457
Cdd:PRK08316 284 dlsslrKGYYGASI-M---PVEVLKELRERLPGLRFynC------YGQTEIAPLATVlgPEEHLRRPGSAGRPVLNVETR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 458 LRDwqEGGytcRD-KPNPRGEIIIGGPNVSMGYFKNEEKTED-FsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKl 535
Cdd:PRK08316 354 VVD--DDG---NDvAPGEVGEIVHRSPQLMLGYWDDPEKTAEaF---RGG--WFHSGDLGVMDEEGYITVVDRKKDMIK- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 536 QAGEYVSLGKVETALkncpfidnicaYAKSDQSYVISFVVPNQKkltvlaeqkgvkgtWVEIC--------NNPIMEAEI 607
Cdd:PRK08316 423 TGGENVASREVEEAL-----------YTHPAVAEVAVIGLPDPK--------------WIEAVtavvvpkaGATVTEDEL 477
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1935119612 608 LKEIKEvadkmKLERFETPIKVRLSPE-PWTPeTGlvtdafKLKRKELKNHY 658
Cdd:PRK08316 478 IAHCRA-----RLAGFKVPKRVIFVDElPRNP-SG------KILKRELRERY 517
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
85-575 |
1.70e-16 |
|
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: 82.38 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 EllesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvptDLALIMYTSGSTGRP 244
Cdd:cd05972 81 E----------------------------------------------------------------DPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGqCERIPELGPKDTYvgyLPLAHvlelTAEISCVTYGcrigYSSPLTLSdqsskikkgskgdCTV 324
Cdd:cd05972 97 KGVLHTHSYPLGHIPT-AAYWLGLRPDDIH---WNIAD----PGWAKGAWSS----FFGPWLLG-------------ATV 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 325 LKPTLMAAVPEimdRIYKnVMSKvqemnyiqrtlfkigydyklEQIKRGYDAPLCNILLFKKvkALLGGN---VRMMLSG 401
Cdd:cd05972 152 FVYEGPRFDAE---RILE-LLER--------------------YGVTSFCGPPTAYRMLIKQ--DLSSYKfshLRLVVSA 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 402 GAPLSPQTQRFMNICFCCPVGQGYGLTETcgagTITeVSDYST-----GRVGAPLICCEIKLRDwQEGGYTcrdKPNPRG 476
Cdd:cd05972 206 GEPLNPEVIEWWRAATGLPIRDGYGQTET----GLT-VGNFPDmpvkpGSMGRPTPGYDVAIID-DDGREL---PPGEEG 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 477 EIIIGGPNVSM--GYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCP 554
Cdd:cd05972 277 DIAIKLPPPGLflGYVGDPEKTEASIRGD----YYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHP 351
|
490 500
....*....|....*....|....
gi 1935119612 555 FIDNICAYAKSDQSY---VISFVV 575
Cdd:cd05972 352 AVAEAAVVGSPDPVRgevVKAFVV 375
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
230-575 |
3.82e-16 |
|
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: 80.38 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVGYLPLAHVLE-------LTAEISCVTYGCRIGYS 302
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiltcLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 303 SPLtlsdqssKIKKGSKGDCTVLKPTLMAAVPEImdriYKNVMSKVQEMNYIQrtlfkIGYDYKLEQIKRgydaplcNIL 382
Cdd:cd17635 82 SLF-------KILTTNAVTTTCLVPTLLSKLVSE----LKSANATVPSLRLIG-----YGGSRAIAADVR-------FIE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 LFKKVKallggnvrmmlsggaplspqtqrfmnicfccpVGQGYGLTETCGAGTITEVSDY-STGRVGAPLICCEIKLRDw 461
Cdd:cd17635 139 ATGLTN--------------------------------TAQVYGLSETGTALCLPTDDDSiEINAVGRPYPGVDVYLAA- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 462 QEGGYTCRDKpnpRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYV 541
Cdd:cd17635 186 TDGIAGPSAS---FGTIWIKSPANMLGYWNNPERTAEVLIDG----WVNTGDLGERREDGFLFITGRSSESI-NCGGVKI 257
|
330 340 350
....*....|....*....|....*....|....*..
gi 1935119612 542 SLGKVETALKNCPFIDNICAYAKSDQSY---VISFVV 575
Cdd:cd17635 258 APDEVERIAEGVSGVQECACYEISDEEFgelVGLAVV 294
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
85-586 |
5.99e-16 |
|
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: 80.85 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLitsv 164
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 eLLESKLKPALSEIPGLkhiiyvdkktinkseypeGLEIHSMQTVEELGAKPenlDIPPSkpvPTDLALIMYTSGSTGRP 244
Cdd:cd17651 97 -LTHPALAGELAVELVA------------------VTLLDQPGAAAGADAEP---DPALD---ADDLAYVIYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPL---AHVLELTAEISCvtygcrigysspltlsdqsskikkgskGD 321
Cdd:cd17651 152 KGVVMPHRSLANLVAWQARASS-LGPGARTLQFAGLgfdVSVQEIFSTLCA---------------------------GA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 322 CTVLKP--------TLMAAVPEI-MDRIY-KNVMskVQEMnyiqrtlfkigydykLEQIKRGYDAPLcnillfkkvkALl 391
Cdd:cd17651 204 TLVLPPeevrtdppALAAWLDEQrISRVFlPTVA--LRAL---------------AEHGRPLGVRLA----------AL- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 392 ggnvRMMLSGGAPLS--------PQTQRFMNICFccpvgqGYGLTETCGAgTITEVSDYSTGR-----VGAPLICCEIKL 458
Cdd:cd17651 256 ----RYLLTGGEQLVltedlrefCAGLPGLRLHN------HYGPTETHVV-TALSLPGDPAAWpapppIGRPIDNTRVYV 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 459 RDwqeggytCRDKPNPR---GEIIIGGPNVSMGYFKNEEKT-EDFSVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDL 532
Cdd:cd17651 325 LD-------AALRPVPPgvpGELYIGGAGLARGYLNRPELTaERFVPDPfvPGARMYRTGDLARWLPDGELEFLGRADDQ 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1935119612 533 VKLQaGEYVSLGKVETALKNCPFIDNICAYAKSDQS---YVISFVVPNQKKLTVLAE 586
Cdd:cd17651 398 VKIR-GFRIELGEIEAALARHPGVREAVVLAREDRPgekRLVAYVVGDPEAPVDAAE 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-576 |
6.04e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.31 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITsv 164
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS-- 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellESKLKPALSEIPGLKHIIYvDKKTINKSEYPEgleihsmqtveelgakpENLDIppsKPVPTDLALIMYTSGSTGRP 244
Cdd:PRK12316 615 ---QSHLGRKLPLAAGVQVLDL-DRPAAWLEGYSE-----------------ENPGT---ELNPENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDqsskikkgskgdctv 324
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRD--------------- 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 325 lkptlMAAVPEIMDRIYKNVMSKVQEMnyiqrtlfkigydykLEQIKRGYDAPLCNILLfkkvkallggnvRMMLSGGA- 403
Cdd:PRK12316 735 -----PAKLVELINREGVDTLHFVPSM---------------LQAFLQDEDVASCTSLR------------RIVCSGEAl 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 404 PLSPQTQRFMNIcFCCPVGQGYGLTETCGAGT----ITEVSDysTGRVGAPLICCEIKLRDWQEGgytcrdkPNP---RG 476
Cdd:PRK12316 783 PADAQEQVFAKL-PQAGLYNLYGPTEAAIDVThwtcVEEGGD--SVPIGRPIANLACYILDANLE-------PVPvgvLG 852
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 477 EIIIGGPNVSMGYFKNEEKT-EDFSVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNC 553
Cdd:PRK12316 853 ELYLAGRGLARGYHGRPGLTaERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRIELGEIEARLLEH 931
|
490 500
....*....|....*....|...
gi 1935119612 554 PFIDNICAYAKSDQSYViSFVVP 576
Cdd:PRK12316 932 PWVREAAVLAVDGKQLV-GYVVL 953
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
85-554 |
6.43e-16 |
|
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: 80.78 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLESKlkPALSEIPGLKHIIYvdkktinkSEYPEGLeihsmqtveelgakpenldiPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:cd17646 104 DLAARL--PAGGDVALLGDEAL--------AAPPATP--------------------PLVPPRPDNLAYVIYTSGSTGRP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLA---HVLELTAEISCvtyGCRIGYSSPLTLSDqsskikkgskgd 321
Cdd:cd17646 154 KGVMVTHAGIVNRLLWMQDEYP-LGPGDRVLQKTPLSfdvSVWELFWPLVA---GARLVVARPGGHRD------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 322 ctvlkptlMAAVPEIMDRIYKNVMSKVQEMnyiqrtlfkigydykLEQIKRGYDAPLCnillfkkvkallgGNVRMMLSG 401
Cdd:cd17646 218 --------PAYLAALIREHGVTTCHFVPSM---------------LRVFLAEPAAGSC-------------ASLRRVFCS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 402 GAPLSPQT-QRFMNIcFCCPVGQGYGLTETCGAGTITEVS-DYSTGRV--GAPLICCEIKLRDwqeggytCRDKPNPR-- 475
Cdd:cd17646 262 GEALPPELaARFLAL-PGAELHNLYGPTEAAIDVTHWPVRgPAETPSVpiGRPVPNTRLYVLD-------DALRPVPVgv 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 476 -GEIIIGGPNVSMGYFKNEEKT-EDFSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALK 551
Cdd:cd17646 334 pGELYLGGVQLARGYLGRPALTaERFVPDpfGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIR-GFRVEPGEIEAALA 412
|
...
gi 1935119612 552 NCP 554
Cdd:cd17646 413 AHP 415
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
136-550 |
6.57e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.15 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 136 LVTLYATLGEEAVTYGLNESGASYLITSVELLESkLKPALSEIPGLKhIIYVDkktINKSEYPEGLEIHSMQTVEELGAK 215
Cdd:PRK08162 95 LNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEV-AREALALLPGPK-PLVID---VDDPEYPGGRFIGALDYEAFLASG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 216 PENLDIPPskpvPTD----LALiMYTSGSTGRPKGVMMIHK--------NLIAGmtgqceripELGPKDTYVGYLPLAHv 283
Cdd:PRK08162 170 DPDFAWTL----PADewdaIAL-NYTSGTTGNPKGVVYHHRgaylnalsNILAW---------GMPKHPVYLWTLPMFH- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 284 leltaeiscvtygCRiGYSSPLTLsdqsskikkgskgdctvlkpTLMAAVpeimdriykNV-MSKVQEmnyiqRTLFKIG 362
Cdd:PRK08162 235 -------------CN-GWCFPWTV--------------------AARAGT---------NVcLRKVDP-----KLIFDLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 363 YDyklEQIKRGYDAP-----LCNilLFKKVKALLGGNVRMMLSGGAPLSPQTQRFMNICFCcpVGQGYGLTETCGAGTI- 436
Cdd:PRK08162 267 RE---HGVTHYCGAPivlsaLIN--APAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD--LTHVYGLTETYGPATVc 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 437 ---TEVSDYSTGRvgapliccEIKLRDWQ------EGGYTCRD----KPNPR-----GEIIIGGpNVSM-GYFKNEEKTE 497
Cdd:PRK08162 340 awqPEWDALPLDE--------RAQLKARQgvryplQEGVTVLDpdtmQPVPAdgetiGEIMFRG-NIVMkGYLKNPKATE 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 498 D-FsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVETAL 550
Cdd:PRK08162 411 EaF---AGG--WFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVL 458
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
85-554 |
7.05e-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: 80.71 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEwMIAAQtcfkynfpLVTLYA---------TLGEEAVTYGLNES 155
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVAL--------LAVLKAgaayvpldpELPAERLAFMLADA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 156 GASYLITSvellesklkPALSEIPGlkhiiyvdkktinkseypeGLEIHSMQTVEELGAKPENLDIPPSkpvPTDLALIM 235
Cdd:cd12117 94 GAKVLLTD---------RSLAGRAG-------------------GLEVAVVIDEALDAGPAGNPAVPVS---PDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 236 YTSGSTGRPKGVMMIHKNLIAGMTGQCERipELGPKDTYVGYLPL---AHVLELtaeiscvtYGCRIgysspltlsdqss 312
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVRLVKNTNYV--TLGPDDRVLQTSPLafdASTFEI--------WGALL------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 313 kikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSkvqemnyiqrTLFKIgydykleqikrgydAPLCNILLFKKVKALLG 392
Cdd:cd12117 200 -----NGARLVLAPKGTLLDPDALGALIAEEGVT----------VLWLT--------------AALFNQLADEDPECFAG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 393 gnVRMMLSGGAPLSPQ-TQRFMNICFCCPVGQGYGLTETCGAGT---ITEVsDYSTGRV--GAPLICCEIKLRDwqEGGy 466
Cdd:cd12117 251 --LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTTFTTshvVTEL-DEVAGSIpiGRPIANTRVYVLD--EDG- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 467 tcrdKPNPR---GEIIIGGPNVSMGYFKNEEKTEDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEY 540
Cdd:cd12117 325 ----RPVPPgvpGELYVGGDGLALGYLNRPALTAERFVAdpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR-GFR 399
|
490
....*....|....
gi 1935119612 541 VSLGKVETALKNCP 554
Cdd:cd12117 400 IELGEIEAALRAHP 413
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-655 |
7.92e-16 |
|
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: 80.17 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 87 YEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVel 166
Cdd:cd05971 9 FKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 167 lesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvPTDLALIMYTSGSTGRPKG 246
Cdd:cd05971 87 -------------------------------------------------------------SDDPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 247 VMMIHKNLIaGMTGQCERIPELGPKDTYVGYLPlahvleltAEISCVtygcrigysspltlsdqsskikkGSKGDctVLK 326
Cdd:cd05971 106 ALHAHRVLL-GHLPGVQFPFNLFPRDGDLYWTP--------ADWAWI-----------------------GGLLD--VLL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 327 PTLMAAVPEIMDRIYKNVMSKVQEM--NYIQRTLFKIGYDYKLeqIKRGYDAplcnillfKKVKALlggNVRMMLSGGAP 404
Cdd:cd05971 152 PSLYFGVPVLAHRMTKFDPKAALDLmsRYGVTTAFLPPTALKM--MRQQGEQ--------LKHAQV---KLRAIATGGES 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 405 LSPQTQRFMNICFCCPVGQGYGLTEtCGA--GTITEVSDYSTGRVGAPLICCEIKLRDwQEGGytcRDKPNPRGEIIIGG 482
Cdd:cd05971 219 LGEELLGWAREQFGVEVNEFYGQTE-CNLviGNCSALFPIKPGSMGKPIPGHRVAIVD-DNGT---PLPPGEVGEIAVEL 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 483 PNVSM--GYFKNEEKTED-FSVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCPFIDNI 559
Cdd:cd05971 294 PDPVAflGYWNNPSATEKkMAGD-----WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMA 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 560 CAYAKSDQ---SYVISFVVPNQKKLTvlaeqkgvkgtwveicnnpimEAEILKEIKEVAdKMKLERFETPIKVRLSPEPW 636
Cdd:cd05971 368 AVVGIPDPirgEIVKAFVVLNPGETP---------------------SDALAREIQELV-KTRLAAHEYPREIEFVNELP 425
|
570
....*....|....*....
gi 1935119612 637 TPETGlvtdafKLKRKELK 655
Cdd:cd05971 426 RTATG------KIRRRELR 438
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
80-585 |
9.56e-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: 80.55 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRW--LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFkynfplvtlYATLGEEAVT--YGLNES 155
Cdd:cd05921 19 GNGGWrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAM---------YAGVPAAPVSpaYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 156 GASYLITSVELLESKLKPALSEIP---GLKHIIYVDKKTINKSEYPEGLEIHSMqtvEELGAKPENLDIPPSKPV--PTD 230
Cdd:cd05921 90 DLAKLKHLFELLKPGLVFAQDAAPfarALAAIFPLGTPLVVSRNAVAGRGAISF---AELAATPPTAAVDAAFAAvgPDT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 231 LALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKD-TYVGYLPLAHVLELTAEISCVTYGCRIGYsspltlsd 309
Cdd:cd05921 167 VAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNHTFGGNHNFNLVLYNGGTLY-------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 qsskIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyiqrtlfKIGYDYKLEQIKRgyDAPLCNiLL 383
Cdd:cd05921 239 ----IDDG--------KPmpggfeETLRNLREISPTVYFNV---------------PAGWEMLVAALEK--DEALRR-RF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 384 FKkvkallggNVRMMLSGGAPLSPQTQRFMNICFCCPVGQ------GYGLTETCGAGTITEVSDYSTGRVGAPLICCEIK 457
Cdd:cd05921 289 FK--------RLKLMFYAGAGLSQDVWDRLQALAVATVGEripmmaGLGATETAPTATFTHWPTERSGLIGLPAPGTELK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 458 LrdwqeggYTCRDKPnprgEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEF----HPDGCLQIIDRKKDLV 533
Cdd:cd05921 361 L-------VPSGGKY----EVRVKGPNVTPGYWRQPELTAQ-AFDEEG--FYCLGDAAKLadpdDPAKGLVFDGRVAEDF 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 534 KLQAGEYVSLGKVETALKNC--PFIDNICAyAKSDQSYVISFVVPNQKKLTVLA 585
Cdd:cd05921 427 KLASGTWVSVGPLRARAVAAcaPLVHDAVV-AGEDRAEVGALVFPDLLACRRLV 479
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
230-550 |
1.05e-15 |
|
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: 79.81 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYvgylplahvleLTAEISCVTYGCRIGYSSPLtlsd 309
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRV-----------FSSAKMFFGYGLGNSLWFPL---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 qsskikkgSKGDCTVLKPTlmAAVPEimdriykNVMSKVQEMnyiQRTLFkigydykleqikrgYDAP--LCNILLFKKV 387
Cdd:cd05919 157 --------AVGASAVLNPG--WPTAE-------RVLATLARF---RPTVL--------------YGVPtfYANLLDSCAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 388 KALLGGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDwqEGGYT 467
Cdd:cd05919 203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD--EEGHT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 468 CrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVE 547
Cdd:cd05919 281 I--PPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG----WYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVE 353
|
...
gi 1935119612 548 TAL 550
Cdd:cd05919 354 SLI 356
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
85-576 |
1.80e-15 |
|
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: 79.40 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITsv 164
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgaKPENLdippskpvptdlALIMYTSGSTGRP 244
Cdd:cd17644 104 --------------------------------------------------QPENL------------AYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLiagmtgqceripelgpkdtyvgylpLAHVLELTAEIScVTYGCRIGYSSPLTLSDQSSKIKKgskgdcTV 324
Cdd:cd17644 122 KGVMIEHQSL-------------------------VNLSHGLIKEYG-ITSSDRVLQFASIAFDVAAEEIYV------TL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 325 LKPTLMAAVPEIMDRIYKNVMSKVQEMnyiQRTLFKIGYDYKLEqikrgydapLCNILLfkKVKALLGGNVRMMLSGGAP 404
Cdd:cd17644 170 LSGATLVLRPEEMRSSLEDFVQYIQQW---QLTVLSLPPAYWHL---------LVLELL--LSTIDLPSSLRLVIVGGEA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 405 LSPQTQ-----------RFMNicfccpvgqGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKlrdwQEGGYTCRD--K 471
Cdd:cd17644 236 VQPELVrqwqknvgnfiQLIN---------VYGPTEATIAATVCRLTQLTERNITSVPIGRPIA----NTQVYILDEnlQ 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 472 PNP---RGEIIIGGPNVSMGYFKNEEKTED------FSVDEnGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVS 542
Cdd:cd17644 303 PVPvgvPGELHIGGVGLARGYLNRPELTAEkfishpFNSSE-SERLYKTGDLARYLPDGNIEYLGRIDNQVKIR-GFRIE 380
|
490 500 510
....*....|....*....|....*....|....*..
gi 1935119612 543 LGKVETALKNCPFIDNICAYAKSDQS---YVISFVVP 576
Cdd:cd17644 381 LGEIEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVP 417
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
61-569 |
1.88e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 79.82 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 61 LSEENEMQPNGKVFKklILGNYrwLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEW---MIAAQTCFKYNFPlV 137
Cdd:PRK07786 23 LARHALMQPDAPALR--FLGNT--TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFvesVLAANMLGAIAVP-V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 138 TLYATLGEeaVTYGLNESGASYLITsvellESKLKPALSEI----PGLKHIIYVDKKTinkseypEGLEIHSMQTVEELG 213
Cdd:PRK07786 98 NFRLTPPE--IAFLVSDCGAHVVVT-----EAALAPVATAVrdivPLLSTVVVAGGSS-------DDSVLGYEDLLAEAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 214 AKPENLDIPPSKPvptdlALIMYTSGSTGRPKGVMMIHKNLiAGMTGQCERIPELGPKDTyVGYL--PLAHVleltAEIS 291
Cdd:PRK07786 164 PAHAPVDIPNDSP-----ALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADINSD-VGFVgvPLFHI----AGIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 292 CVTYGCRIGYSspltlsdqsskikkgskgdcTVLKPTLMAAVPEIMDriyknvmskVQEMNYIQrTLFKIGYDYKL---E 368
Cdd:PRK07786 233 SMLPGLLLGAP--------------------TVIYPLGAFDPGQLLD---------VLEAEKVT-GIFLVPAQWQAvcaE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 369 QIKRGYDAPLcnillfkkvkallggnvRMMLSGGAPLSPQTQRFMNICFccPVGQ---GYGLTE----TC---GAGTITE 438
Cdd:PRK07786 283 QQARPRDLAL-----------------RVLSWGAAPASDTLLRQMAATF--PEAQilaAFGQTEmspvTCmllGEDAIRK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 439 VsdystGRVGAPLICCEIKLRDwqeggYTCRD-KPNPRGEIIIGGPNVSMGYFKNEEKTED-FsvdENGqrWFCTGDIGE 516
Cdd:PRK07786 344 L-----GSVGKVIPTVAARVVD-----ENMNDvPVGEVGEIVYRAPTLMSGYWNNPEATAEaF---AGG--WFHSGDLVR 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1935119612 517 FHPDGCLQIIDRKKDLVkLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSY 569
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW 460
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
85-550 |
2.34e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 79.55 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKyNFPLVT-LYATLGEEAVTYGLNESGASYLITS 163
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALK-NGAIVGpLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 164 VELLESKLKPalsEIPGLKHIIYVDkktiNKSEYPEGLeihsMQTVEELGAKPENLDIPPSKPvpTDLALIMYTSGSTGR 243
Cdd:PRK04319 153 PALLERKPAD---DLPSLKHVLLVG----EDVEEGPGT----LDFNALMEQASDEFDIEWTDR--EDGAILHYTSGSTGK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 244 PKGVMMIHKNLIAG-MTGqcERIPELGPKDTY-----VGYL---------PLAHvleltaEISCVTYGCRIG----YSsp 304
Cdd:PRK04319 220 PKGVLHVHNAMLQHyQTG--KYVLDLHEDDVYwctadPGWVtgtsygifaPWLN------GATNVIDGGRFSperwYR-- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 305 lTLSDQssKIkkgskgdcTV--LKPT----LMAAVPEIMDRiyknvmskvqemnyiqrtlfkigydykleqikrgYDAPl 378
Cdd:PRK04319 290 -ILEDY--KV--------TVwyTAPTairmLMGAGDDLVKK----------------------------------YDLS- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 379 cnillfkkvkallggNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETcGAGTI--TEVSDYSTGRVGAPLICCEI 456
Cdd:PRK04319 324 ---------------SLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTET-GGIMIanYPAMDIKPGSMGKPLPGIEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 457 KLRDWQEGGytcrDKPNPRGEIII--GGPnvSM--GYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDL 532
Cdd:PRK04319 388 AIVDDQGNE----LPPNRMGNLAIkkGWP--SMmrGIWNNPEKYESYFAGD----WYVSGDSAYMDEDGYFWFQGRVDDV 457
|
490
....*....|....*...
gi 1935119612 533 VKlQAGEYVSLGKVETAL 550
Cdd:PRK04319 458 IK-TSGERVGPFEVESKL 474
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
77-578 |
2.59e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.59 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRwLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESG 156
Cdd:PRK12467 531 LVFGEQV-LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSG 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLESKLKPAlseipGLKHIIYVDkktinkseyPEGLEIHSMQTVEELGAKPENLdippskpvptdlALIMY 236
Cdd:PRK12467 610 VRLLLTQSHLLAQLPVPA-----GLRSLCLDE---------PADLLCGYSGHNPEVALDPDNL------------AYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 237 TSGSTGRPKGVMMIHKNLiAGMTGQCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDQSSKIKK 316
Cdd:PRK12467 664 TSGSTGQPKGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAAL 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 317 GSKGDCTVLKptlmaAVPeimdriyknvmskvqemnyiqrTLFKIGYDYKLEQIKRGYDAPLCnillfkkvkallGGNVr 396
Cdd:PRK12467 743 MADQGVTVLK-----IVP----------------------SHLQALLQASRVALPRPQRALVC------------GGEA- 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 397 MMLSGGAP---LSPQTqRFMNIcfccpvgqgYGLTETCGAGTITEVS----DYSTGRVGAPLICCEIKLRDwqegGYTCR 469
Cdd:PRK12467 783 LQVDLLARvraLGPGA-RLINH---------YGPTETTVGVSTYELSdeerDFGNVPIGQPLANLGLYILD----HYLNP 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 470 DKPNPRGEIIIGGPNVSMGYFKNEEKT-EDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 545
Cdd:PRK12467 849 VPVGVVGELYIGGAGLARGYHRRPALTaERFVPDpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR-GFRIELGE 927
|
490 500 510
....*....|....*....|....*....|....*
gi 1935119612 546 VETALKNCPFIDN--ICAYAKSDQSYVISFVVPNQ 578
Cdd:PRK12467 928 IEARLLAQPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
228-533 |
2.96e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 79.07 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTAeiscvtygcriGYSSPLTl 307
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST-EWKTKDRILSWMPLTHDMGLIA-----------FHLAPLI- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 308 sdqsskikkgsKGDCTVLKPTLMAAVPEImdriykNVMSKVQEMNYIQRTLFKIGYDYKLEQIK--RGYDAPLCNIllfk 385
Cdd:cd05908 172 -----------AGMNQYLMPTRLFIRRPI------LWLKKASEHKATIVSSPNFGYKYFLKTLKpeKANDWDLSSI---- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 386 kvkallggnvRMMLSGGAPLSPQ-TQRFMNIC--------FCCPVgqgYGLTETCGAGTI-------------------- 436
Cdd:cd05908 231 ----------RMILNGAEPIDYElCHEFLDHMskyglkrnAILPV---YGLAEASVGASLpkaqspfktitlgrrhvthg 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 437 --------TEVSDYSTGRVGAPLICCEIKLRDWQ----EGGYTcrdkpnprGEIIIGGPNVSMGYFKNEEKTEDFSVDEN 504
Cdd:cd05908 298 epepevdkKDSECLTFVEVGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEATAKVFTDDG 369
|
330 340
....*....|....*....|....*....
gi 1935119612 505 gqrWFCTGDIGeFHPDGCLQIIDRKKDLV 533
Cdd:cd05908 370 ---WLKTGDLG-FIRNGRLVITGREKDII 394
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
228-568 |
1.24e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.44 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTgQCERIPELGPKDTYVGYLPLAHVLELTAEI-SCVTYGCRIG-YSSPL 305
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFGLTVGLfTPLLTGAEVFlYPSPL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 -------TLSDQsskikkgskgDCTVL--KPTLMAavpeimdriyknvmskvqemNYIQrtlFKIGYDYkleqikrgyda 376
Cdd:PRK08043 443 hyrivpeLVYDR----------NCTVLfgTSTFLG--------------------NYAR---FANPYDF----------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 377 plcnillfkkvkallgGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEI 456
Cdd:PRK08043 479 ----------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDA 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 457 KLRDWQ--EGGytcrdkpnprGEIIIGGPNVSMGYFKNEEKTE---DFSVDENGQR---WFCTGDIGEFHPDGCLQIIDR 528
Cdd:PRK08043 543 RLLSVPgiEQG----------GRLQLKGPNIMNGYLRVEKPGVlevPTAENARGEMergWYDTGDIVRFDEQGFVQIQGR 612
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1935119612 529 KKDLVKLqAGEYVSLGKVET-ALKNCPfIDNICAYAKSDQS 568
Cdd:PRK08043 613 AKRFAKI-AGEMVSLEMVEQlALGVSP-DKQHATAIKSDAS 651
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-576 |
1.72e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.69 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS 3162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELlesklkpALSEIPGLKhIIYVDKKTINKSEYPegleihsmqtveelgakpenldiPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:PRK12316 3163 HL-------RLPLAQGVQ-VLDLDRGDENYAEAN-----------------------PAIRTMPENLAYVIYTSGSTGKP 3211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLI--AGMTGQCEripELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDQsskikkgskgdc 322
Cdd:PRK12316 3212 KGVGIRHSALSnhLCWMQQAY---GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP------------ 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 323 tvlkptlmAAVPEIMDRIYKNVMSKVQEMNYiqrtlfkigydykleqikrgydaplcniLLFKKVKALLGGNVRMMLSGG 402
Cdd:PRK12316 3277 --------ALLVELINSEGVDVLHAYPSMLQ----------------------------AFLEEEDAHRCTSLKRIVCGG 3320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 403 APLSPQTQRFMNICFccPVGQGYGLTETCGAGTITEVSDY--STGRVGAPLICCEIKLRDWQEggytcrdKPNPRG---E 477
Cdd:PRK12316 3321 EALPADLQQQVFAGL--PLYNLYGPTEATITVTHWQCVEEgkDAVPIGRPIANRACYILDGSL-------EPVPVGalgE 3391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 478 IIIGGPNVSMGYFKNEEKT-EDFSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCP 554
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLTaERFVPDpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHP 3470
|
490 500
....*....|....*....|..
gi 1935119612 555 FIDNICAYAKSDQSyVISFVVP 576
Cdd:PRK12316 3471 WVREAVVLAVDGRQ-LVAYVVP 3491
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
85-582 |
2.26e-14 |
|
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: 75.90 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQG-LKPKSAIAIFCEtRAEWMIAA-QTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAeIRPDDLVGLVLD-KSELMIIAiLAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVIT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 SvellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvPTDLALIMYTSGSTG 242
Cdd:cd17648 92 N----------------------------------------------------------------STDLAYAIYTSGTTG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 243 RPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVGYLPlAHVLELTAEiscvtygcrigyssPLTLSDQSskikkgskGDC 322
Cdd:cd17648 108 KPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFS-NYVFDFFVE--------------QMTLALLN--------GQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 323 TVLKPTLMAAVPeimDRIYKnvmskvqemnYIQRTlfKIGYDYKLEQIKRGYDAPLCNILlfkkvkallggnvRMMLSGG 402
Cdd:cd17648 165 LVVPPDEMRFDP---DRFYA----------YINRE--KVTYLSGTPSVLQQYDLARLPHL-------------KRVDAAG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 403 APLSPQTQRFMNICFCCPVGQGYGLTETcgagTITE-VSDYSTGRVGAPLICCEIKLRDWqeggYTCRD--KPNP---RG 476
Cdd:cd17648 217 EEFTAPVFEKLRSRFAGLIINAYGPTET----TVTNhKRFFPGDQRFDKSLGRPVRNTKC----YVLNDamKRVPvgaVG 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 477 EIIIGGPNVSMGYFKNEEKTED------FSVDE-----NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 545
Cdd:cd17648 289 ELYLGGDGVARGYLNRPELTAErflpnpFQTEQerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIR-GQRIEPGE 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1935119612 546 VETALKNCPFIDNICAYAKSD--------QSYVISFVVPNQKKLT 582
Cdd:cd17648 368 VEAALASYPGVRECAVVAKEDasqaqsriQKYLVGYYLPEPGHVP 412
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-281 |
2.89e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.92 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLEsKLKPalseipglkhiiyvdkktinkseyPEGLEIHSMQTVEELGAKPENLdiPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:PRK12316 2109 HLLE-RLPL------------------------PAGVARLPLDRDAEWADYPDTA--PAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLA 281
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS 2197
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
77-533 |
5.89e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 75.02 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWlNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAE-W--MIAAQTC-FKYnfplVTLYATLGEEAVTYGL 152
Cdd:PRK06188 31 LVLGDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLmaIGAAQLAgLRR----TALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 153 NESGASYLITSVELLESKLKPALSEIPGLKHIIyvdkkTINKSEYPEGLeihsMQTVEELGAKPenldiPPSKPVPTDLA 232
Cdd:PRK06188 106 EDAGISTLIVDPAPFVERALALLARVPSLKHVL-----TLGPVPDGVDL----LAAAAKFGPAP-----LVAAALPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 233 LIMYTSGSTGRPKGVMMIHKNlIAGMTGQCERIPELGPKDTYVGYLPLAHVleltaeiscvtygcrigysspltlsdqss 312
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRS-IATMAQIQLAEWEWPADPRFLMCTPLSHA----------------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 313 kikkgskGDCTVLkPTLMAAVPEIMDRIY--KNVMSKVQEMNyIQRTLFKIGYDYKLeqikrgYDAPLCnillfkkVKAL 390
Cdd:PRK06188 222 -------GGAFFL-PTLLRGGTVIVLAKFdpAEVLRAIEEQR-ITATFLVPTMIYAL------LDHPDL-------RTRD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 391 LGGnVRMMLSGGAPLSPQ-----TQRFMNIcfccpVGQGYGLTETCGAGTITEVSDYSTGRV------GAPLICCEIKLR 459
Cdd:PRK06188 280 LSS-LETVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALL 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935119612 460 DWQeggytcrDKPNPR---GEIIIGGPNVSMGYFKNEEKT-EDFsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:PRK06188 354 DED-------GREVAQgevGEICVRGPLVMDGYWNRPEETaEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKDMI 419
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-566 |
9.55e-14 |
|
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: 73.28 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAgMTGQCERIPELGPKDTYVGYLPLAHV-------LELTAEISCVTYGCRIG 300
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVY-NAWMLALNSLFDPDDVLLCGLPLFHVngsvvtlLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 301 YSSPLTLSDQSSKIKKgskgdctvLKPTLMAAVPEIMDriyknvmskvqemnyiqrtlfkigydyKLEQIKRGYDAplcn 380
Cdd:cd05944 80 YRNPGLFDNFWKLVER--------YRITSLSTVPTVYA---------------------------ALLQVPVNADI---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 illfkkvkallgGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTE-TCGAGTITEVSDYSTGRVGAPLICCEIKLR 459
Cdd:cd05944 121 ------------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 460 DWQEGGYTCRD-KPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAG 538
Cdd:cd05944 189 VLDGVGRLLRDcAPDEVGEICVAGPGVFGGYLYTEGNKNAFVAD----GWLNTGDLGRLDADGYLFITGRAKDLI-IRGG 263
|
330 340
....*....|....*....|....*...
gi 1935119612 539 EYVSLGKVETALKNCPFIDNICAYAKSD 566
Cdd:cd05944 264 HNIDPALIEEALLRHPAVAFAGAVGQPD 291
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
85-533 |
9.67e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 74.17 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEW---MIAAQTCFKYNFPlVTLYATlGEEaVTYGLNESGASYLI 161
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFfevYWAARRSGLYYTP-INWHLT-AAE-IAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 162 TSVELLESkLKPALSEIP-GLKHIIYVDKKTINKSEYPEgleihsmqtveELGAKPenlDIPPSKPVPTDLALimYTSGS 240
Cdd:PRK08276 89 VSAALADT-AAELAAELPaGVPLLLVVAGPVPGFRSYEE-----------ALAAQP---DTPIADETAGADML--YSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 241 TGRPKGV------MMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHvleltaeiscvtygcrigySSPLTLSDQSSKI 314
Cdd:PRK08276 152 TGRPKGIkrplpgLDPDEAPGMMLALLGFGMY-GGPDSVYLSPAPLYH-------------------TAPLRFGMSALAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 315 kkgskGDCTVLkptlmaavpeiMDRiyknvMSKVQEMNYIQRtlFKIGYDY----------KL-EQIKRGYDaplcnill 383
Cdd:PRK08276 212 -----GGTVVV-----------MEK-----FDAEEALALIER--YRVTHSQlvptmfvrmlKLpEEVRARYD-------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 384 fkkVKALlggnvRMMLSGGAPLSPQTQRFMnICFCCPV-GQGYGLTETCGAGTITEVsDYST--GRVGAPLIcCEIKLRD 460
Cdd:PRK08276 261 ---VSSL-----RVAIHAAAPCPVEVKRAM-IDWWGPIiHEYYASSEGGGVTVITSE-DWLAhpGSVGKAVL-GEVRILD 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935119612 461 wqEGGytcrdKPNPRGEI-----IIGGPNVSmgYFKNEEKTEDfsvDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:PRK08276 330 --EDG-----NELPPGEIgtvyfEMDGYPFE--YHNDPEKTAA---ARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI 395
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
425-618 |
1.08e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 73.78 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 425 YGLTETCGAGT---ITE--VSDYSTGRVGAPLICCEIKLRDwqEGGYTCrdkPNP-RGEIIIGGPNVSMGYFKNEEKTED 498
Cdd:PRK04813 293 YGPTEATVAVTsieITDemLDQYKRLPIGYAKPDSPLLIID--EEGTKL---PDGeQGEIVISGPSVSKGYLNNPEKTAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 499 FSVDENGQRWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAGEYVSLGKVETALKNCPFIDNICA--YAKSDQ-SYVISFVV 575
Cdd:PRK04813 368 AFFTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVESAVVvpYNKDHKvQYLIAYVV 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1935119612 576 PNQKKLTvlaeqkgvkgtwveicnnpiMEAEILKEIK-EVADKM 618
Cdd:PRK04813 446 PKEEDFE--------------------REFELTKAIKkELKERL 469
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
228-580 |
2.09e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 73.85 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVLELTAeiscvtygcriGYSSPLtl 307
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLTG-----------GLVLPL-- 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 308 sdqSSKIKkgskgdcTVLKPTLM--AAVPEImdrIYKnvmskvqemnyIQRTLFkIGYDYKLEQIKR---GYDaplcnil 382
Cdd:PRK06814 858 ---LSGVK-------VFLYPSPLhyRIIPEL---IYD-----------TNATIL-FGTDTFLNGYARyahPYD------- 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 lFKkvkallggNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTET-----------CGAGTItevsdystGRVgAPL 451
Cdd:PRK06814 906 -FR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapvialntpmhNKAGTV--------GRL-LPG 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 452 IccEIKLRD---WQEGgytcrdkpnprGEIIIGGPNVSMGYFKnEEKTEDFSVDENGqrWFCTGDIGEFHPDGCLQIIDR 528
Cdd:PRK06814 968 I--EYRLEPvpgIDEG-----------GRLFVRGPNVMLGYLR-AENPGVLEPPADG--WYDTGDIVTIDEEGFITIKGR 1031
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1935119612 529 KKDLVKLqAGEYVSLGKVETAlkncpfidnICAYAKSDQSYVISfvVPNQKK 580
Cdd:PRK06814 1032 AKRFAKI-AGEMISLAAVEEL---------AAELWPDALHAAVS--IPDARK 1071
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
228-577 |
3.78e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.77 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNL---IAGMTGQCERIPELGPKDtYVGYLPLAHvleltaeiscvTYGCRIGYSsP 304
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPV-SLDWMPWNH-----------TMGGNANFN-G 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 305 LTLSDQSSKIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyiqrtlfKIGYDYKLEQIKRgyDAPL 378
Cdd:PRK12582 286 LLWGGGTLYIDDG--------KPlpgmfeETIRNLREISPTVYGNV---------------PAGYAMLAEAMEK--DDAL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 379 CNiLLFKkvkallggNVRMMLSGGAPLSPQTQRFMNICFCCPVGQ------GYGLTETcgAGTITEVSdYSTGRV---GA 449
Cdd:PRK12582 341 RR-SFFK--------NLRLMAYGGATLSDDLYERMQALAVRTTGHripfytGYGATET--APTTTGTH-WDTERVgliGL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 450 PLICCEIKLRdwqeggytcrdkpnPRG---EIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEF-HPDGCLQ- 524
Cdd:PRK12582 409 PLPGVELKLA--------------PVGdkyEVRVKGPNVTPGYHKDPELTAA-AFDEEG--FYRLGDAARFvDPDDPEKg 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1935119612 525 -IID-RKKDLVKLQAGEYVSLGKVET-ALKNC-PFIDNICAyAKSDQSYVISFVVPN 577
Cdd:PRK12582 472 lIFDgRVAEDFKLSTGTWVSVGTLRPdAVAACsPVIHDAVV-AGQDRAFIGLLAWPN 527
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
87-533 |
3.85e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 72.34 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 87 YEDINQRVNHFGRGLAAQGLKPKSAIAIF----CET----RAEWMI-AAQTCFKYNFPLVTLyATLGEEAVTYgLNESGA 157
Cdd:PRK07768 32 WGEVHERARRIAGGLAAAGVGPGDAVAVLagapVEIaptaQGLWMRgASLTMLHQPTPRTDL-AVWAEDTLRV-IGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 158 SYLITSVELLEskLKPALSEIpGLKHIiyvdkktinkseypegleihsmqTVEELgakpenLDIPPSKPVPT---DLALI 234
Cdd:PRK07768 110 KAVVVGEPFLA--AAPVLEEK-GIRVL-----------------------TVADL------LAADPIDPVETgedDLALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 235 MYTSGSTGRPKGVMMIHKNLIAGMTGQCERI---PElgpKDTYVGYLPLAHVLELTAEISC-VTYGCRIGYSSPLT-LSD 309
Cdd:PRK07768 158 QLTSGSTGSPKAVQITHGNLYANAEAMFVAAefdVE---TDVMVSWLPLFHDMGMVGFLTVpMYFGAELVKVTPMDfLRD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 qsskikkgskgdctvlkPTLMaavPEIMDRiYKNVMSKVQEMNY--IQRTLFKigydykleQIKRG-YDAplcnillfkk 386
Cdd:PRK07768 235 -----------------PLLW---AELISK-YRGTMTAAPNFAYalLARRLRR--------QAKPGaFDL---------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 387 vkallgGNVRMMLSGGAPLSPQT-QRFmnicfcCPVGQG-----------YGLTET--------CGAGTITEVSD----Y 442
Cdd:PRK07768 276 ------SSLRFALNGAEPIDPADvEDL------LDAGARfglrpeailpaYGMAEAtlavsfspCGAGLVVDEVDadllA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 443 STGR--------------VGAPLICCEIKLRDwqEGGYTCrdkpNPR--GEIIIGGPNVSMGYFkneekTED---FSVDE 503
Cdd:PRK07768 344 ALRRavpatkgntrrlatLGPPLPGLEVRVVD--EDGQVL----PPRgvGVIELRGESVTPGYL-----TMDgfiPAQDA 412
|
490 500 510
....*....|....*....|....*....|
gi 1935119612 504 NGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:PRK07768 413 DG--WLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
85-554 |
7.10e-13 |
|
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: 71.13 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITsv 164
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpVPTDLALIMYTSGSTGRP 244
Cdd:cd17652 91 --------------------------------------------------------------TPDNLAYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPL---AHVLELTAEISCvtyGCR--IGYSSPLTLSDQSSKIKKGSK 319
Cdd:cd17652 109 KGVVVTHRGLANLAAAQIAAF-DVGPGSRVLQFASPsfdASVWELLMALLA---GATlvLAPAEELLPGEPLADLLREHR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 320 GDCTVLKPTLMAAVPEimdriyknvmskvqemnyiqrtlfkigydykleqikrgydaplcnillfkkvKALLGGnvRMML 399
Cdd:cd17652 185 ITHVTLPPAALAALPP----------------------------------------------------DDLPDL--RTLV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 400 SGGAPLSPQ-------TQRFMNicfccpvgqGYGLTETCGAGTITEVSdySTGRV---GAPLICCEIK-LRDWQEggytc 468
Cdd:cd17652 211 VAGEACPAElvdrwapGRRMIN---------AYGPTETTVCATMAGPL--PGGGVppiGRPVPGTRVYvLDARLR----- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 469 rdkPNP---RGEIIIGGPNVSMGYFKNEEKT-EDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYV 541
Cdd:cd17652 275 ---PVPpgvPGELYIAGAGLARGYLNRPGLTaERFVADpfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIR-GFRI 350
|
490
....*....|...
gi 1935119612 542 SLGKVETALKNCP 554
Cdd:cd17652 351 ELGEVEAALTEHP 363
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
228-550 |
7.54e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 71.45 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAG--MTGQCERIPELGPKdTYVGYLPLAHVLELTAEISCVTY--Gcrigyss 303
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANqqMLAQTFPFLAEEPP-VLVDWLPWNHTFGGNHNLGIVLYngG------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 304 plTLSdqsskIKKGskgdctvlKPTlmaavPEIMDRIYKNvmskvqeMNYIQRTLF---KIGYDYKLEQIKRgyDAPLCN 380
Cdd:PRK08180 280 --TLY-----IDDG--------KPT-----PGGFDETLRN-------LREISPTVYfnvPKGWEMLVPALER--DAALRR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 ILLfkkvkallgGNVRMMLSGGAPLSPQT----QRF-MNIC-----FCCpvgqGYGLTETCGAGTITEVSDYSTGRVGAP 450
Cdd:PRK08180 331 RFF---------SRLKLLFYAGAALSQDVwdrlDRVaEATCgerirMMT----GLGMTETAPSATFTTGPLSRAGNIGLP 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 451 LICCEIKLRDwqEGGytcrdkpnpRGEIIIGGPNVSMGYFKNEEKT-EDFsvDENGqrWFCTGDIGEFH-PDgclqiiDR 528
Cdd:PRK08180 398 APGCEVKLVP--VGG---------KLEVRVKGPNVTPGYWRAPELTaEAF--DEEG--YYRSGDAVRFVdPA------DP 456
|
330 340 350
....*....|....*....|....*....|.
gi 1935119612 529 KKDLV---------KLQAGEYVSLGKVETAL 550
Cdd:PRK08180 457 ERGLMfdgriaedfKLSSGTWVSVGPLRARA 487
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
77-554 |
8.26e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 71.27 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNyRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAI-------FCETRAewmiAAQTCFKYNFPlVTLYATlgEEAVT 149
Cdd:PRK12406 5 IISGD-RRRSFDELAQRAARAAGGLAALGVRPGDCVALlmrndfaFFEAAY----AAMRLGAYAVP-VNWHFK--PEEIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 150 YGLNESGASYLITSVELLEsklkPALSEIPGLKHIIYVdkktinkseyPEGLEIHSMQTVEELGAKPENLDI-------- 221
Cdd:PRK12406 77 YILEDSGARVLIAHADLLH----GLASALPAGVTVLSV----------PTPPEIAAAYRISPALLTPPAGAIdwegwlaq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 222 -----PPSKPVPTDLaliMYTSGSTGRPKGVmmihknliagmtgqcERIPELgPKDTYVGYLPLAHVLELTAEISCVTYG 296
Cdd:PRK12406 143 qepydGPPVPQPQSM---IYTSGTTGHPKGV---------------RRAAPT-PEQAAAAEQMRALIYGLKPGIRALLTG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 297 cRIGYSSPltlsdQSSKIKKGSKGDCTVLKPTLMA-AVPEIMDRIYKNVMSKVQEMnYIqRTLfkigydyKL-EQIKRGY 374
Cdd:PRK12406 204 -PLYHSAP-----NAYGLRAGRLGGVLVLQPRFDPeELLQLIERHRITHMHMVPTM-FI-RLL-------KLpEEVRAKY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 375 DaplcnillfkkVKALlggnvRMMLSGGAPLSPQTQRFMnICFCCPV-GQGYGLTETcGAGTITEVSDY--STGRVGAPL 451
Cdd:PRK12406 269 D-----------VSSL-----RHVIHAAAPCPADVKRAM-IEWWGPViYEYYGSTES-GAVTFATSEDAlsHPGTVGKAA 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 452 ICCEIKLRDwQEGgytcrdKPNPRGEI------IIGGPNVSmgYFKNEEKTEdfSVDENGqrWFCTGDIGEFHPDGCLQI 525
Cdd:PRK12406 331 PGAELRFVD-EDG------RPLPQGEIgeiysrIAGNPDFT--YHNKPEKRA--EIDRGG--FITSGDVGYLDADGYLFL 397
|
490 500
....*....|....*....|....*....
gi 1935119612 526 IDRKKDLVkLQAGEYVSLGKVETALKNCP 554
Cdd:PRK12406 398 CDRKRDMV-ISGGVNIYPAEIEAVLHAVP 425
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-577 |
2.38e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.96 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITsv 164
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT-- 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellESKLKPALSEIPGLKhIIYVDKKTINKSEYPEgleihsmqtveelgakpENldiPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:PRK12467 1678 ---QSHLQARLPLPDGLR-SLVLDQEDDWLEGYSD-----------------SN---PAVNLAPQNLAYVIYTSGSTGRP 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLA---HVLELTAeiscvtygcrigyssPLTlsdqsskikkgsKGD 321
Cdd:PRK12467 1734 KGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAfdvSVWELFW---------------PLI------------NGA 1785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 322 CTVLKPTLMAAVPE-IMDRIYKN-VMSKVQEMNYIQrtlfkigydyKLEQIKRGYDAPLcnillfkkvkallggNVRMML 399
Cdd:PRK12467 1786 RLVIAPPGAHRDPEqLIQLIERQqVTTLHFVPSMLQ----------QLLQMDEQVEHPL---------------SLRRVV 1840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 400 SGGAPLSPQTQRFMNICFcCPVG--QGYGLTETC---GAGTITEVSDysTGRVGAPlICCEIKLRDWqeggYTCRDKPNP 474
Cdd:PRK12467 1841 CGGEALEVEALRPWLERL-PDTGlfNLYGPTETAvdvTHWTCRRKDL--EGRDSVP-IGQPIANLST----YILDASLNP 1912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 475 R-----GEIIIGGPNVSMGYFKNEEKT-EDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 545
Cdd:PRK12467 1913 VpigvaGELYLGGVGLARGYLNRPALTaERFVADpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGE 1991
|
490 500 510
....*....|....*....|....*....|....
gi 1935119612 546 VETALKNCPFIDN--ICAYAKSDQSYVISFVVPN 577
Cdd:PRK12467 1992 IEARLREQGGVREavVIAQDGANGKQLVAYVVPT 2025
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
236-550 |
3.07e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 69.66 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 236 YTSGSTGRPKGVMMIHK-------NLIAGMtgqceripELGPKDTYVGYLPLAHvleltaeiscvtygCRiGYSSPLTLS 308
Cdd:PLN03102 193 YTSGTTADPKGVVISHRgaylstlSAIIGW--------EMGTCPVYLWTLPMFH--------------CN-GWTFTWGTA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 309 dqsskikkgSKGDCTVLKPTLMAavPEImdriYKNV-MSKVQEMNYIQrTLFKIGYD-YKLEQIKRGydaplcnillfkk 386
Cdd:PLN03102 250 ---------ARGGTSVCMRHVTA--PEI----YKNIeMHNVTHMCCVP-TVFNILLKgNSLDLSPRS------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 387 vkallgGNVRMMLSGGAPLSPQTQRFMNICFccPVGQGYGLTETCGAGTITEVSDYST-----------GRVGAP-LICC 454
Cdd:PLN03102 301 ------GPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEWQDEWNrlpenqqmelkARQGVSiLGLA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 455 EIKLRDWQEGGYTCRDKPNpRGEIIIGGPNVSMGYFKNEEKTedFSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 534
Cdd:PLN03102 373 DVDVKNKETQESVPRDGKT-MGEIVIKGSSIMKGYLKNPKAT--SEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDII- 446
|
330
....*....|....*.
gi 1935119612 535 LQAGEYVSLGKVETAL 550
Cdd:PLN03102 447 ISGGENISSVEVENVL 462
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
85-533 |
3.12e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 69.33 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRA---EWMIAAQTCFKYnFPLVTLYATLGEEAvtYGLNESGASYLI 161
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAA--YIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 162 TSVELLESkLKPALSEIPGLKHIIYVDKKtiNKSEYPEGLEihsmQTVEELGAKPEnldipPSKPVPTDLaliMYTSGST 241
Cdd:PRK13391 102 TSAAKLDV-ARALLKQCPGVRHRLVLDGD--GELEGFVGYA----EAVAGLPATPI-----ADESLGTDM---LYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 242 GRPKGVMmihknliagmtgqcERIPELGPKDTyvgyLPLAHVLELtaeiscvTYGCRIG--YSSPLTL---SDQSSKIKK 316
Cdd:PRK13391 167 GRPKGIK--------------RPLPEQPPDTP----LPLTAFLQR-------LWGFRSDmvYLSPAPLyhsAPQRAVMLV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 317 GSKGDCTVlkptlmaavpeIMDRiyknvMSKVQEMNYIQRtlFKIGYD----------YKL-EQIKRGYDaplcnillfk 385
Cdd:PRK13391 222 IRLGGTVI-----------VMEH-----FDAEQYLALIEE--YGVTHTqlvptmfsrmLKLpEEVRDKYD---------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 386 kVKALlggnvRMMLSGGAPLSPQTQRFMnICFCCPV-GQGYGLTETCGAGTI-TEVSDYSTGRVGAPLIcCEIKLRDwqE 463
Cdd:PRK13391 274 -LSSL-----EVAIHAAAPCPPQVKEQM-IDWWGPIiHEYYAATEGLGFTACdSEEWLAHPGTVGRAMF-GDLHILD--D 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935119612 464 GGYTCrdkpnPRGEI--IIGGPNVSMGYFKNEEKTEDfSVDENGQrWFCTGDIGEFHPDGCLQIIDRKKDLV 533
Cdd:PRK13391 344 DGAEL-----PPGEPgtIWFEGGRPFEYLNDPAKTAE-ARHPDGT-WSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
85-576 |
6.23e-12 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 67.96 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSv 164
Cdd:cd17645 24 LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTN- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellesklkpalseipglkhiiyvdkktinkseypegleihsmqtveelgakpenldippskpvPTDLALIMYTSGSTGRP 244
Cdd:cd17645 103 ---------------------------------------------------------------PDDLAYVIYTSGSTGLP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIagmtGQCEripelgpkdtyvGYLPlahVLELTAEiscvtygcrigysspltlsDQSSKIKkGSKGDCTV 324
Cdd:cd17645 120 KGVMIEHHNLV----NLCE------------WHRP---YFGVTPA-------------------DKSLVYA-SFSFDASA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 325 LK--PTLMA-AVPEIMDRIYKNVMSKVQEmnYIQRTLFKIGYdykleqikrgYDAPLCnillfKKVKALLGGNVRMMLSG 401
Cdd:cd17645 161 WEifPHLTAgAALHVVPSERRLDLDALND--YFNQEGITISF----------LPTGAA-----EQFMQLDNQSLRVLLTG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 402 GAPLSPQTQRFMNICfccpvgQGYGLTETCGAGTITEV-SDYSTGRVGAPLICCEIKLRDwqEGGYTCRDkpNPRGEIII 480
Cdd:cd17645 224 GDKLKKIERKGYKLV------NNYGPTENTVVATSFEIdKPYANIPIGKPIDNTRVYILD--EALQLQPI--GVAGELCI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 481 GGPNVSMGYFKNEEKT-EDFSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCPFID 557
Cdd:cd17645 294 AGEGLARGYLNRPELTaEKFIVHpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR-GYRIEPGEIEPFLMNHPLIE 372
|
490 500
....*....|....*....|..
gi 1935119612 558 NICAYAKSD---QSYVISFVVP 576
Cdd:cd17645 373 LAAVLAKEDadgRKYLVAYVTA 394
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
31-577 |
6.57e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 68.56 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 31 DIPGADTLDKLFDHAVAKFGKKDCLGTREILSEENEMqpngkvfkklilgNYRWLNyEDINQRVNHFgrglAAQGLKPKS 110
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVYGHKTALIFESSGGVVRRY-------------SYLELN-EEINRTANLF----YSLGIRKGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 111 AIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSVELLesklkPALSEIPG-----LKHII 185
Cdd:PRK08008 64 KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFY-----PMYRQIQQedatpLRHIC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 186 YVDkktinkSEYPEGLEIHSMQtvEELGAKPENLDIPPskPVPT-DLALIMYTSGSTGRPKGVMMIHKNLI-AGMTG--Q 261
Cdd:PRK08008 139 LTR------VALPADDGVSSFT--QLKAQQPATLCYAP--PLSTdDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSawQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 262 CeripELGPKDTYVGYLPLAHV-LELTAEISCVTYGCRI----GYSSPlTLSDQSSKIKkgskgdctvlkptlmAAVPEI 336
Cdd:PRK08008 209 C----ALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFvlleKYSAR-AFWGQVCKYR---------------ATITEC 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 337 MDRIYKNVMSKVQEMNYIQRTLFKIGYDYKL-EQIKRGYDAPLcnillfkkvkallggNVRMMLSggaplspqtqrfmni 415
Cdd:PRK08008 269 IPMMIRTLMVQPPSANDRQHCLREVMFYLNLsDQEKDAFEERF---------------GVRLLTS--------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 416 cfccpvgqgYGLTETCGaGTITEV-SDY----STGRVGaplICCEIKLRDwqEGGYTCrdKPNPRGEIIIGG-PNVSM-- 487
Cdd:PRK08008 319 ---------YGMTETIV-GIIGDRpGDKrrwpSIGRPG---FCYEAEIRD--DHNRPL--PAGEIGEICIKGvPGKTIfk 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 488 GYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCPFIDNICAYAKSD- 566
Cdd:PRK08008 382 EYYLDPKATAK-VLEADG--WLHTGDTGYVDEEGFFYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVGIKDs 457
|
570
....*....|...
gi 1935119612 567 --QSYVISFVVPN 577
Cdd:PRK08008 458 irDEAIKAFVVLN 470
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
81-540 |
7.71e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.39 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 81 NYRWLNYEDINQRVNHFGRGLAAQGLKPKsaiaifceTRAEWMIAAQTCFkynFPLVtlYATLGEEAVTYgLNESGASY- 159
Cdd:PRK09274 38 AYDELSFAELDARSDAIAHGLNAAGIGRG--------MRAVLMVTPSLEF---FALT--FALFKAGAVPV-LVDPGMGIk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 -LITSVEllESKLKpALSEIP--------------GLKHIIYVDkktinkseypeGLEIHSMQTVEELGAKPENLDIPPS 224
Cdd:PRK09274 104 nLKQCLA--EAQPD-AFIGIPkahlarrlfgwgkpSVRRLVTVG-----------GRLLWGGTTLATLLRDGAAAPFPMA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 225 KPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAgmtgQCERIpelgpKDTYvgylPLAHvleltAEISCVTYgcrigyssP 304
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA----QIEAL-----REDY----GIEP-----GEIDLPTF--------P 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 305 LTLsdqsskikkgskgdctVLKPTL-MAAV-PEiMDriyknvMSKVQEMN--YIQRTLFKigydyklEQIKRGYDAP-LC 379
Cdd:PRK09274 224 LFA----------------LFGPALgMTSViPD-MD------PTRPATVDpaKLFAAIER-------YGVTNLFGSPaLL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 380 NILL-FKKVKALLGGNVRMMLSGGAPLSPQT-QRF---MNicfccPVGQ---GYGLTET--------------------C 431
Cdd:PRK09274 274 ERLGrYGEANGIKLPSLRRVISAGAPVPIAViERFramLP-----PDAEiltPYGATEAlpissiesreilfatraatdN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 432 GAGTItevsdystgrVGAPLICCEIKLRD--------WQEggyTCRDKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSV-D 502
Cdd:PRK09274 349 GAGIC----------VGRPVDGVEVRIIAisdapipeWDD---ALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIpD 415
|
490 500 510
....*....|....*....|....*....|....*...
gi 1935119612 503 ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEY 540
Cdd:PRK09274 416 GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
228-576 |
1.19e-11 |
|
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: 67.39 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKnliagmtgqceripelgpkdtyvgylPLAHVLELTAEISCVTYGCRIGYSSPLTL 307
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHG--------------------------PLAAHCQATAERYGLTPGDRELQFASFNF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 308 SDQSSKIKKG-SKGDCTVLKP-TLMAAVPEIMDRIYKNVMSKVQemnyiqrtlFKIGYDYKL-EQIKRGYDAPlcnillf 384
Cdd:cd17649 147 DGAHEQLLPPlICGACVVLRPdELWASADELAEMVRELGVTVLD---------LPPAYLQQLaEEADRTGDGR------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 385 kkvkallGGNVRMMLSGGAPLSPQTQR--FMNICFCCpvgQGYGLTETCGAGTITEVSDYsTGRVGA------PLiccei 456
Cdd:cd17649 211 -------PPSLRLYIFGGEALSPELLRrwLKAPVRLF---NAYGPTEATVTPLVWKCEAG-AARAGAsmpigrPL----- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 457 klrdwqeGGYTCR--DK------PNPRGEIIIGGPNVSMGYFKNEEKT-EDFSVD---ENGQRWFCTGDIGEFHPDGCLQ 524
Cdd:cd17649 275 -------GGRSAYilDAdlnpvpVGVTGELYIGGEGLARGYLGRPELTaERFVPDpfgAPGSRLYRTGDLARWRDDGVIE 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 525 IIDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICAYAKSDQS--YVISFVVP 576
Cdd:cd17649 348 YLGRVDHQVKIR-GFRIELGEIEAALLEHPGVREAAVVALDGAGgkQLVAYVVL 400
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
395-654 |
3.00e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 66.41 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 395 VRMMLSGGAP----LSPQTQRFMNicfccpVGQGYGLTETCGAGTI-----------TEVSDYSTGRVGAPLICCE-IKL 458
Cdd:PLN02479 313 VHVMTAGAAPppsvLFAMSEKGFR------VTHTYGLSETYGPSTVcawkpewdslpPEEQARLNARQGVRYIGLEgLDV 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 459 RDWQEGgytcrdKPNPR-----GEIIIGGPNVSMGYFKNEEKTED-FsvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDL 532
Cdd:PLN02479 387 VDTKTM------KPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEaF---ANG--WFHSGDLGVKHPDGYIEIKDRSKDI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 533 VkLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSYVIS---FVVPNQKkltvlaeqkgvkgtwVEICNNPIMEAEILK 609
Cdd:PLN02479 456 I-ISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESpcaFVTLKPG---------------VDKSDEAALAEDIMK 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1935119612 610 EIKEvadkmKLERFETPIKVRLSPEPWTPETGLVTDAFKLKRKEL 654
Cdd:PLN02479 520 FCRE-----RLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEM 559
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
77-577 |
3.23e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNyRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESG 156
Cdd:PRK12467 3114 LVFGD-QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLEsKLKpalseIPGLKHIIYVDKKTINkSEYPEGLEIHSMqtveelgakPENLdippskpvptdlALIMY 236
Cdd:PRK12467 3193 VKLLLTQAHLLE-QLP-----APAGDTALTLDRLDLN-GYSENNPSTRVM---------GENL------------AYVIY 3244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 237 TSGSTGRPKGVMMIHKNLiAGMTGQCERIPELGPKDTYVGYLPLAhvLELTAEiscvtygcriGYSSPLTlsdqsskikk 316
Cdd:PRK12467 3245 TSGSTGKPKGVGVRHGAL-ANHLCWIAEAYELDANDRVLLFMSFS--FDGAQE----------RFLWTLI---------- 3301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 317 gsKGDCTVLKPTLMAAvPEimdriyknvmSKVQEMNYiqrtlfkigydyklEQIKRGYDAP--LCNILLFKKVKAllGGN 394
Cdd:PRK12467 3302 --CGGCLVVRDNDLWD-PE----------ELWQAIHA--------------HRISIACFPPayLQQFAEDAGGAD--CAS 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 395 VRMMLSGGAPLSPQTQRFMNICFcCPVG--QGYGLTET--------CGAGTITEVSDYSTGRVGAPLICceiklrdwqeg 464
Cdd:PRK12467 3353 LDIYVFGGEAVPPAAFEQVKRKL-KPRGltNGYGPTEAvvtvtlwkCGGDAVCEAPYAPIGRPVAGRSI----------- 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 465 gYTCRDKPNP-----RGEIIIGGPNVSMGYFKNEEKT-EDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 535
Cdd:PRK12467 3421 -YVLDGQLNPvpvgvAGELYIGGVGLARGYHQRPSLTaERFVADpfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKI 3499
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1935119612 536 QaGEYVSLGKVETALKNCPFIDNICAYAKSDQS--YVISFVVPN 577
Cdd:PRK12467 3500 R-GFRIELGEIEARLLQHPSVREAVVLARDGAGgkQLVAYVVPA 3542
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
230-585 |
8.37e-11 |
|
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: 64.66 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTgQCERIPELGPKDTYVGYLPLAHVLELtaeiscvtygcrigySSPLTLsd 309
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVR-ASAEVCGLDQDTVYLAVLPAAHNFPL---------------ACPGVL-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 qsskikkGS--KGDCTVLKPTlmaAVPE----IMDRIYKNVMSKVQE--MNYIQrtlfkigydyklEQIKRGYDAplcni 381
Cdd:cd05920 202 -------GTllAGGRVVLAPD---PSPDaafpLIEREGVTVTALVPAlvSLWLD------------AAASRRADL----- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 382 llfkkvkallgGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTEtcGAGTITEVSD------YSTGRVGAPLIccE 455
Cdd:cd05920 255 -----------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTRLDDpdeviiHTQGRPMSPDD--E 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 456 IKLRDwQEGgytcRD-KPNPRGEIIIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 534
Cdd:cd05920 320 IRVVD-EEG----NPvPPGEEGELLTRGPYTIRGYYRAPEHNAR-AFTPDG--FYRTGDLVRRTPDGYLVVEGRIKDQIN 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 535 lQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSY---VISFVVPNQKKLTVLA 585
Cdd:cd05920 392 -RGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLgerSCAFVVLRDPPPSAAQ 444
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
223-586 |
1.31e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 63.53 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 223 PSKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERipeLGPKDTYVGYLPLAHVLELTAEISCVTYGcrigyS 302
Cdd:PRK07824 29 VGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDR---LGGPGQWLLALPAHHIAGLQVLVRSVIAG-----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 303 SPLTLsDQSSKIKKgskgdctvlkPTLMAAVPEI-MDRIYKNvMSKVQemnyiqrtLFKIGYDYKLEQIKRGYDAplcnI 381
Cdd:PRK07824 101 EPVEL-DVSAGFDP----------TALPRAVAELgGGRRYTS-LVPMQ--------LAKALDDPAATAALAELDA----V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 382 LLfkkvkallggnvrmmlsGGAPLSPQTQRF---MNIcfccPVGQGYGLTETCGAGtiteVSDystgrvGAPLICCEIKL 458
Cdd:PRK07824 157 LV-----------------GGGPAPAPVLDAaaaAGI----NVVRTYGMSETSGGC----VYD------GVPLDGVRVRV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 459 RDwqeggytcrdkpnprGEIIIGGPNVSMGYfKNEEKTEDFSvdENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVKlQAG 538
Cdd:PRK07824 206 ED---------------GRIALGGPTLAKGY-RNPVDPDPFA--EPG--WFRTDDLGALD-DGVLTVLGRADDAIS-TGG 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1935119612 539 EYVSLGKVETALKNCPFIDNICAYAKSDQSY---VISFVVPNQKKLTVLAE 586
Cdd:PRK07824 264 LTVLPQVVEAALATHPAVADCAVFGLPDDRLgqrVVAAVVGDGGPAPTLEA 314
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
85-656 |
1.40e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 64.13 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAqtcfkynFPLVTLYATLG-------EEAVTYGLNESGA 157
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAW-------LGLAKLGAVVAllntqqrGAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 158 SYLITSVELLEsklkpALSEIPG---LKHIIYVDKKTINKSEypegleihsmQTVEELGAKPENLdiPPSKPVPT----- 229
Cdd:PRK08279 136 KHLIVGEELVE-----AFEEARAdlaRPPRLWVAGGDTLDDP----------EGYEDLAAAAAGA--PTTNPASRsgvta 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 -DLALIMYTSGSTGRPKGVMMIHKNLI---AGMTGQCeripELGPKDTYVGYLPLAHVlelTAEISCVtygcrigysspl 305
Cdd:PRK08279 199 kDTAFYIYTSGTTGLPKAAVMSHMRWLkamGGFGGLL----RLTPDDVLYCCLPLYHN---TGGTVAW------------ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 tlsdqSSKIKKGSkgdCTVLKPTLMAAvpEIMDRIYKNvmskvqemnyiQRTLFkigydykleqikrGYDAPLCNILLFK 385
Cdd:PRK08279 260 -----SSVLAAGA---TLALRRKFSAS--RFWDDVRRY-----------RATAF-------------QYIGELCRYLLNQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 386 KVKALLGGN-VRMMLsgGAPLSPQ-----TQRF--MNICfccpvgQGYGLTEtcgaGTITEVS----DYSTGRV------ 447
Cdd:PRK08279 306 PPKPTDRDHrLRLMI--GNGLRPDiwdefQQRFgiPRIL------EFYAASE----GNVGFINvfnfDGTVGRVplwlah 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 448 -----------GAPlicceikLRDwqEGGYTCRDKPNPRGEII--IGGPNVSMGYfKNEEKTE-----DfsVDENGQRWF 509
Cdd:PRK08279 374 pyaivkydvdtGEP-------VRD--ADGRCIKVKPGEVGLLIgrITDRGPFDGY-TDPEASEkkilrD--VFKKGDAWF 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 510 CTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICAYAKSdqsyvisfvVPNqkkltvlAEqkG 589
Cdd:PRK08279 442 NTGDLMRDDGFGHAQFVDRLGDTFRWK-GENVATTEVENALSGFPGVEEAVVYGVE---------VPG-------TD--G 502
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935119612 590 VKGtwveicnnpiMEAEILKE-----IKEVADKM--KLERFETPIKVRLSPEPWTPETglvtdaFKLKRKELKN 656
Cdd:PRK08279 503 RAG----------MAAIVLADgaefdLAALAAHLyeRLPAYAVPLFVRLVPELETTGT------FKYRKVDLRK 560
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
83-556 |
2.11e-10 |
|
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: 63.75 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 83 RWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 SVELLES----KLKPALSE-----IPGLKHIIyVDKKTINKSEYPEGLEIHSMQTVEElgAKPENldiPPSKPVPTDLAL 233
Cdd:cd17634 163 ADGGVRAgrsvPLKKNVDDalnpnVTSVEHVI-VLKRTGSDIDWQEGRDLWWRDLIAK--ASPEH---QPEAMNAEDPLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 234 IMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVgylplahvleLTAEISCVTYGCRIGYsSPLTLsdqssk 313
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYW----------CTADVGWVTGHSYLLY-GPLAC------ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 314 ikkgskGDCTVL---KPTLMAAvPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYkleqiKRGYDAplcnillfkkvkal 390
Cdd:cd17634 300 ------GATTLLyegVPNWPTP-ARMWQVVDKHGVNILYTAPTAIRALMAAGDDA-----IEGTDR-------------- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 391 lgGNVRMMLSGGAPLSPQTQRFMNICFC---CPVGQGYGLTETcGAGTITEVSDYSTGRVGA---PLICCEIKLRDwqEG 464
Cdd:cd17634 354 --SSLRILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTET-GGFMITPLPGAIELKAGSatrPVFGVQPAVVD--NE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 465 GYTCrdKPNPRGEIIIGG--PNVSMGYFKNEEKTED--FSVDENgqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEY 540
Cdd:cd17634 429 GHPQ--PGGTEGNLVITDpwPGQTRTLFGDHERFEQtyFSTFKG---MYFSGDGARRDEDGYYWITGRSDDVINV-AGHR 502
|
490
....*....|....*.
gi 1935119612 541 VSLGKVETALKNCPFI 556
Cdd:cd17634 503 LGTAEIESVLVAHPKV 518
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
85-550 |
3.19e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLEsklkpALSEIPGLKHIIYVDKKTINKSEYPEGLEIHSmqtveelgakpenldippskpvpTDLALIMYTSGSTGRP 244
Cdd:PRK05691 1237 HLLE-----RLPQAEGVSAIALDSLHLDSWPSQAPGLHLHG-----------------------DNLAYVIYTSGSTGQP 1288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLIagmtgqcERIPELgpKDTYVgyLPLAHVLELTAEIS-------C---VTYGCRIGYSSPLTLSDQSSKI 314
Cdd:PRK05691 1289 KGVGNTHAALA-------ERLQWM--QATYA--LDDSDVLMQKAPISfdvsvweCfwpLITGCRLVLAGPGEHRDPQRIA 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 315 KKGSKGDCTVLKptlmaAVPEIMDriyknvmskvqemnyiqrtLFkigydykleqikrgYDAPL---CNILlfkkvkall 391
Cdd:PRK05691 1358 ELVQQYGVTTLH-----FVPPLLQ-------------------LF--------------IDEPLaaaCTSL--------- 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 392 ggnvRMMLSGGAPLSPQTQ-RFMNICFCCPVGQGYGLTETcgAGTIT----EVSDYSTGRVGAPL--ICCEIKLRDWQeg 464
Cdd:PRK05691 1391 ----RRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTET--AINVThwqcQAEDGERSPIGRPLgnVLCRVLDAELN-- 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 465 gytcrdkPNPRG---EIIIGGPNVSMGYFKNEEKT-EDFSVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQa 537
Cdd:PRK05691 1463 -------LLPPGvagELCIGGAGLARGYLGRPALTaERFVPDplgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLR- 1534
|
490
....*....|...
gi 1935119612 538 GEYVSLGKVETAL 550
Cdd:PRK05691 1535 GFRVEPEEIQARL 1547
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
228-533 |
3.62e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.65 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAG--MTGQCERIpELGPKDTYVGYLPLAHVLELtaeiscvtygcrIGysspl 305
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGI-DLNPDDVIVSWLPLYHDMGL------------IG----- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 tlsdqsskikkgskgdcTVLKPtLMAAVPEIMdriyknvMSKVQEMNYIQRTLFKIG-----------YDYKLEQiKRGY 374
Cdd:PRK05691 227 -----------------GLLQP-IFSGVPCVL-------MSPAYFLERPLRWLEAISeyggtisggpdFAYRLCS-ERVS 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 375 DAPLCNILLfkkvkallgGNVRMMLSGGAPLSPQT-QRFMNICFCCPVGQ-----GYGLTETC--------GAG-TITEV 439
Cdd:PRK05691 281 ESALERLDL---------SRWRVAYSGSEPIRQDSlERFAEKFAACGFDPdsffaSYGLAEATlfvsggrrGQGiPALEL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 440 SDYSTGR------VGAPLICC-------EIKLRDWQEGGYTcrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDENGQ 506
Cdd:PRK05691 352 DAEALARnraepgTGSVLMSCgrsqpghAVLIVDPQSLEVL---GDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHDGR 428
|
330 340
....*....|....*....|....*..
gi 1935119612 507 RWFCTGDIGeFHPDGCLQIIDRKKDLV 533
Cdd:PRK05691 429 TWLRTGDLG-FLRDGELFVTGRLKDML 454
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
85-533 |
4.59e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 62.72 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCfKYN----FPLvTLYATLGEEAVtY------GLNE 154
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFAC-QYAglvpVPL-PLPMGFGGRES-YiaqlrgMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 155 SGASYLITSVELLEsklkpalseipglkhiiYVDKKTINKSEypegleIHSMqTVEELGAKPENlDIPPSKPVPTDLALI 234
Cdd:PRK09192 127 AQPAAIITPDELLP-----------------WVNEATHGNPL------LHVL-SHAWFKALPEA-DVALPRPTPDDIAYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 235 MYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVGYLPLAHVLELTaeiscvtyGCRIgysSPLTlsDQSSki 314
Cdd:PRK09192 182 QYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGLV--------GFLL---TPVA--TQLS-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 315 kkgskgdcTVLKPTlmaavpeimdRIYknVMSKVQEMNYIQRTLFKIGYD----YKLEQiKRGYDAPLCNILLfkkvkal 390
Cdd:PRK09192 247 --------VDYLPT----------RDF--ARRPLQWLDLISRNRGTISYSppfgYELCA-RRVNSKDLAELDL------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 391 lgGNVRMMLSGGAPLSPQT-QRFMNiCFCcPVG-------QGYGLTETC--------GAGTITEVSDYS----------- 443
Cdd:PRK09192 299 --SCWRVAGIGADMIRPDVlHQFAE-AFA-PAGfddkafmPSYGLAEATlavsfsplGSGIVVEEVDRDrleyqgkavap 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 444 ---TGRV------GAPLICCEIKLRDwqEGGytcRDKPNPR-GEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGD 513
Cdd:PRK09192 375 gaeTRRVrtfvncGKALPGHEIEIRN--EAG---MPLPERVvGHICVRGPSLMSGYFRDEESQDVLAADG----WLDTGD 445
|
490 500
....*....|....*....|
gi 1935119612 514 IGeFHPDGCLQIIDRKKDLV 533
Cdd:PRK09192 446 LG-YLLDGYLYITGRAKDLI 464
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
80-248 |
5.26e-10 |
|
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: 62.65 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASY 159
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 LITSVELLE----SKLKP----ALSEIPG-LKHIIyVDKKTinkseypeGLEIHSMQT-----VEELGAKpENLDIPPSK 225
Cdd:TIGR02188 164 VITADEGLRggkvIPLKAivdeALEKCPVsVEHVL-VVRRT--------GNPVVPWVEgrdvwWHDLMAK-ASAYCEPEP 233
|
170 180
....*....|....*....|...
gi 1935119612 226 PVPTDLALIMYTSGSTGRPKGVM 248
Cdd:TIGR02188 234 MDSEDPLFILYTSGSTGKPKGVL 256
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
393-591 |
5.85e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.93 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 393 GNVRMMLSGGAPLSP---QTQRFMNIcfccPVGQGYGLTETcgAGTITEV--SDYSTGR--VGAPLICCEIKLRdwqegg 465
Cdd:PRK07445 230 AQFRTILLGGAPAWPsllEQARQLQL----RLAPTYGMTET--ASQIATLkpDDFLAGNnsSGQVLPHAQITIP------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 466 ytcrdkPNPRGEIIIGGPNVSMGYFKNEEktedfsvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGK 545
Cdd:PRK07445 298 ------ANQTGNITIQAQSLALGYYPQIL---------DSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAE 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1935119612 546 VETALKNCPFIDNICAYAKSDQSY---VISFVVPNQKKLTVLAEQKGVK 591
Cdd:PRK07445 362 VEAAILATGLVQDVCVLGLPDPHWgevVTAIYVPKDPSISLEELKTAIK 410
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
37-542 |
6.81e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 37 TLDKLFDHAVAKFGKkdclgtREILSEENEmqpngkvfkklilGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFC 116
Cdd:PRK06018 11 LCHRIIDHAARIHGN------REVVTRSVE-------------GPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 117 ETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITS---VELLEsKLKPALSEIPglKHIIYVDKKTIN 193
Cdd:PRK06018 72 WNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDltfVPILE-KIADKLPSVE--RYVVLTDAAHMP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 194 KSEYPEGLEIHSMqtVEELGAKPEnldippSKPVPTDLALIM-YTSGSTGRPKGVMMIHK-NLIAGMTGQCERIPELGPK 271
Cdd:PRK06018 149 QTTLKNAVAYEEW--IAEADGDFA------WKTFDENTAAGMcYTSGTTGDPKGVLYSHRsNVLHALMANNGDALGTSAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 272 DTYVGYLPLAHVLELTAEISC-------VTYGCRIGYSSPLTLSDQSskikkgskgdctvlKPTLMAAVPEIMDRIyknv 344
Cdd:PRK06018 221 DTMLPVVPLFHANSWGIAFSApsmgtklVMPGAKLDGASVYELLDTE--------------KVTFTAGVPTVWLML---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 345 mskvqeMNYIQRTlfkigyDYKLEQIKrgydaplcnillfkkvKALLGGNV--RMMLsggaplspqtQRFMNicFCCPVG 422
Cdd:PRK06018 283 ------LQYMEKE------GLKLPHLK----------------MVVCGGSAmpRSMI----------KAFED--MGVEVR 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 423 QGYGLTETCGAGTITEVSDYSTG-----------RVGAPLICCEIKLRDwQEGGYTCRDKPNPrGEIIIGGPNVSMGYFK 491
Cdd:PRK06018 323 HAWGMTEMSPLGTLAALKPPFSKlpgdarldvlqKQGYPPFGVEMKITD-DAGKELPWDGKTF-GRLKVRGPAVAAAYYR 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1935119612 492 NEEKTedfsVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVS 542
Cdd:PRK06018 401 VDGEI----LDDDG--FFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWIS 444
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
85-533 |
7.90e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.95 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCfkynfplvtlyATLGEEAVtyglnesgasylitsv 164
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLAC-----------AKLGAIAV---------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 eLLESKLKPA----LSEIPGLKHIIYVDKKTINKSEYPEGLEIHSMQTVE---ELGAKPENLDI--PPSKP-VPTDLALI 234
Cdd:PRK05857 95 -MADGNLPIAaierFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDiaaVTRESEHSLDAasLAGNAdQGSEDPLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 235 M-YTSGSTGRPKGVMMIHKNLIAgmtgqcerIPEL-----------GPKDTYVGYLPLAHVLELTAEISCVTYG--CRIG 300
Cdd:PRK05857 174 MiFTSGTTGEPKAVLLANRTFFA--------VPDIlqkeglnwvtwVVGETTYSPLPATHIGGLWWILTCLMHGglCVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 301 YSSPLTLSDqsskIKKGSKGDCTVLKPTLMAavpeimdriyknvmskvqemnyiqrtlfKIGYDYKLEqikrGYDAPLCN 380
Cdd:PRK05857 246 GENTTSLLE----ILTTNAVATTCLVPTLLS----------------------------KLVSELKSA----NATVPSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 ILLFKKVKALlGGNVRMMLSGGAPlspqtqrfmnicfccpVGQGYGLTET-CGA-------GTITEVSdysTGRVGAPLI 452
Cdd:PRK05857 290 LVGYGGSRAI-AADVRFIEATGVR----------------TAQVYGLSETgCTAlclptddGSIVKIE---AGAVGRPYP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 453 CCEIKLRDWQEGGYTCRDKPNPR--GEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKK 530
Cdd:PRK05857 350 GVDVYLAATDGIGPTAPGAGPSAsfGTLWIKSPANMLGYWNNPERTAEVLIDG----WVNTGDLLERREDGFFYIKGRSS 425
|
...
gi 1935119612 531 DLV 533
Cdd:PRK05857 426 EMI 428
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
85-562 |
8.55e-10 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 61.54 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQ-GLKPKSAIAIFC--ETRAEWM---IAAQTCfkynfPLVTLYATLGEEAVTYGLNESGAS 158
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLgnEPAFLWIwlgLAKLGC-----PVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 159 YLITSVELLEsklkpALSEI-PGLK----HIIYVDKKTInkseyPEGleihsmqtVEELGAKpenLDIPPSKPVPTDL-- 231
Cdd:cd05938 81 VLVVAPELQE-----AVEEVlPALRadgvSVWYLSHTSN-----TEG--------VISLLDK---VDAASDEPVPASLra 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 232 -------ALIMYTSGSTGRPKGVMMIHKNLIA--GMTGQCeripelGPKDTYVGY--LPLAHVLELTAEIScvtyGCrig 300
Cdd:cd05938 140 hvtikspALYIYTSGTTGLPKAARISHLRVLQcsGFLSLC------GVTADDVIYitLPLYHSSGFLLGIG----GC--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 301 ysspltlsdqsskIKKGSKgdcTVLKPTLMAAvpEIMDRIYKNVMSKVQemnYIQRTLfkigyDYkleqikrgydapLCN 380
Cdd:cd05938 207 -------------IELGAT---CVLKPKFSAS--QFWDDCRKHNVTVIQ---YIGELL-----RY------------LCN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 IllfKKVKALLGGNVRMMLSGGapLSPQT-----QRFMNICFCcpvgQGYGLTEtcgaGTITEVsDYsTGRVGA------ 449
Cdd:cd05938 249 Q---PQSPNDRDHKVRLAIGNG--LRADVwreflRRFGPIRIR----EFYGSTE----GNIGFF-NY-TGKIGAvgrvsy 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 450 --------PLICCEIK----LRDWQegGYTCRDKPNPRGEIIigGPNVSM----GYFKNEEKTED---FSVDENGQRWFC 510
Cdd:cd05938 314 lykllfpfELIKFDVEkeepVRDAQ--GFCIPVAKGEPGLLV--AKITQQspflGYAGDKEQTEKkllRDVFKKGDVYFN 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1935119612 511 TGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICAY 562
Cdd:cd05938 390 TGDLLVQDQQNFLYFHDRVGDTFRWK-GENVATTEVADVLGLLDFLQEVNVY 440
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-576 |
1.74e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 60.53 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 79 LGNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGAS 158
Cdd:PRK06164 30 IDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 159 YLIT-----SVELLESKLKPALSEIPGLKHIIYVDKKTinkSEYPEGLEIHSMQTVE-ELGAKPENLDIPPSkpVPTDLA 232
Cdd:PRK06164 110 WLVVwpgfkGIDFAAILAAVPPDALPPLRAIAVVDDAA---DATPAPAPGARVQLFAlPDPAPPAAAGERAA--DPDAGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 233 LIMYTSGSTGRPKGVMMIHKNLIAgMTGQCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYG----CRIGYSSPLTLS 308
Cdd:PRK06164 185 LLFTTSGTTSGPKLVLHRQATLLR-HARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGaplvCEPVFDAARTAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 309 D-QSSKIKKGSKGDctvlkptlmaavpEIMDRIYKnvmSKVQEMNYIQRTLFKIGyDY-----KLEQIKRGYDAPLCNIL 382
Cdd:PRK06164 264 AlRRHRVTHTFGND-------------EMLRRILD---TAGERADFPSARLFGFA-SFapalgELAALARARGVPLTGLY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 LFKKVKALLGG-------NVRMmLSGGAPLSPQTqrfmnicfccpvgqgygltetcgagtitevsdystgrvgapliccE 455
Cdd:PRK06164 327 GSSEVQALVALqpatdpvSVRI-EGGGRPASPEA---------------------------------------------R 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 456 IKLRDWQEGGYTcrdKPNPRGEIIIGGPNVSMGYFKNEEKTED-FSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 534
Cdd:PRK06164 361 VRARDPQDGALL---PDGESGEIEIRAPSLMRGYLDNPDATARaLTDDG----YFRTGDLGYTRGDGQFVYQTRMGDSLR 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1935119612 535 LqAGEYVSLGKVETALKNCPFIDN--ICAYAKSDQSYVISFVVP 576
Cdd:PRK06164 434 L-GGFLVNPAEIEHALEALPGVAAaqVVGATRDGKTVPVAFVIP 476
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
218-533 |
1.98e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 60.73 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 218 NLDIPP-SKPVPTDL---ALIMYTSGSTGRPKGVMMIHKNLIA----GMTGQCERIPELGPKD-TYVGYLPLAH----VL 284
Cdd:PRK05850 145 DLDSPRgSDARPRDLpstAYLQYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYFGDTGGVPPPDtTVVSWLPFYHdmglVL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 285 ELTAEISCvtyGCRIGYSSPLTLsdqsskikkgskgdctVLKPT----LMAAVPEImdriyknvmskvqemnyiqrtlFK 360
Cdd:PRK05850 225 GVCAPILG---GCPAVLTSPVAF----------------LQRPArwmqLLASNPHA----------------------FS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 361 IGYDYKLE-QIKRGYDAPLCNILLfkkvkallgGNVRMMLSGGAPLSPQT-----QRFMNICFCCPVGQ-GYGLTE---- 429
Cdd:PRK05850 264 AAPNFAFElAVRKTSDDDMAGLDL---------GGVLGIISGSERVHPATlkrfaDRFAPFNLRETAIRpSYGLAEatvy 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 430 --TCGAGTITEVSDY-----STGRV-------GAPLICC------EIKLRDWQeggyTCRDKPNPR-GEIIIGGPNVSMG 488
Cdd:PRK05850 335 vaTREPGQPPESVRFdyeklSAGHAkrcetggGTPLVSYgsprspTVRIVDPD----TCIECPAGTvGEIWVHGDNVAAG 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1935119612 489 YFKNEEKTE--------DFSVDENGQRWFCTGDIGEFHpDGCLQIIDRKKDLV 533
Cdd:PRK05850 411 YWQKPEETErtfgatlvDPSPGTPEGPWLRTGDLGFIS-EGELFIVGRIKDLL 462
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
80-248 |
2.94e-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: 60.27 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASY 159
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 LITSVELLESK----LKP----ALSEIPGLKHIIyVDKKTINKSEYPEGLEI--HSMQTVEELGAKPENLDippskpvPT 229
Cdd:cd05966 160 VITADGGYRGGkvipLKEivdeALEKCPSVEKVL-VVKRTGGEVPMTEGRDLwwHDLMAKQSPECEPEWMD-------SE 231
|
170
....*....|....*....
gi 1935119612 230 DLALIMYTSGSTGRPKGVM 248
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVV 250
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
230-587 |
3.22e-09 |
|
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: 59.41 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 230 DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVGYLPLAhvleltaeiscVTYGCRIGYSSPLtlsd 309
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLA-----------FTFGLGGVLLFPF---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 310 qsskikkgSKGDCTVLKPtlmAAVPEimdriykNVMSKVQEmnYIQRTLFkigydykleQIKRGYDAplcnILLFKKVKA 389
Cdd:cd05958 163 --------GVGASGVLLE---EATPD-------LLLSAIAR--YKPTVLF---------TAPTAYRA----MLAHPDAAG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 390 LLGGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDwQEGgytcr 469
Cdd:cd05958 210 PDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEG----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 470 dKPNPRGEI---IIGGPNvsmGYFKNEEKTEDFSVDENgqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKV 546
Cdd:cd05958 284 -NPVPDGTIgrlAVRGPT---GCRYLADKRQRTYVQGG---WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEV 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1935119612 547 ETALKNCPFIDNICAYAKSDQS---YVISFVV--PNQKKLTVLAEQ 587
Cdd:cd05958 356 EDVLLQHPAVAECAVVGHPDESrgvVVKAFVVlrPGVIPGPVLARE 401
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
150-550 |
3.26e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 60.05 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 150 YGLNESGASYLITSVELLESkLKPALSEIPgLKHIIYV-------DKKTInksEYPEGLEIHSMQT--VEELGAKPENLD 220
Cdd:PRK06178 124 YELNDAGAEVLLALDQLAPV-VEQVRAETS-LRHVIVTsladvlpAEPTL---PLPDSLRAPRLAAagAIDLLPALRACT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 221 IPPSKPVPT--DLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVGYLPLahvLELTAEISCVTYgcr 298
Cdd:PRK06178 199 APVPLPPPAldALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPE---FWIAGENFGLLF--- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 299 igyssPLTLsdqsskikkgskGDCTVL-----KPTLMAAVPEImdRIYKNVM---SKVQEMNYIQrtlFKigyDYKLEQI 370
Cdd:PRK06178 273 -----PLFS------------GATLVLlarwdAVAFMAAVERY--RVTRTVMlvdNAVELMDHPR---FA---EYDLSSL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 371 KrgydaplcnillfkkvkallggNVRMMlSGGAPLSPQT-QRFMNICFCCPVGQGYGLTETCGAGTIT---EVSDYS-TG 445
Cdd:PRK06178 328 R----------------------QVRVV-SFVKKLNPDYrQRWRALTGSVLAEAAWGMTETHTCDTFTagfQDDDFDlLS 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 446 R---VGAPLICCEIKLRDWQEGgytcrdKPNP---RGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHP 519
Cdd:PRK06178 385 QpvfVGLPVPGTEFKICDFETG------ELLPlgaEGEIVVRTPSLLKGYWNKPEATAEALRDG----WLHTGDIGKIDE 454
|
410 420 430
....*....|....*....|....*....|.
gi 1935119612 520 DGCLQIIDRKKDLVKLQaGEYVSLGKVETAL 550
Cdd:PRK06178 455 QGFLHYLGRRKEMLKVN-GMSVFPSEVEALL 484
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
143-657 |
3.40e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 59.80 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 143 LGEEAVTYGLNESGASYLITSVELLEsKLKPALSEIPGLKHIIYV--DKKTINKSEYPEGLEIHSMQTveELGAKPENLD 220
Cdd:PRK05620 98 LMNDQIVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIgpSDADSAAAHMPEGIKVYSYEA--LLDGRSTVYD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 221 IPPskpVP-TDLALIMYTSGSTGRPKGVMMIHKNL-IAGMTGQCERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGcr 298
Cdd:PRK05620 175 WPE---LDeTTAAAICYSTGTTGAPKGVVYSHRSLyLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSG-- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 299 igysSPLTLSDQSskikkgskgdctVLKPTLMAAVPEIMDRIYKNVMSK-VQEMNYIQRTLFKigydykleqikrgydap 377
Cdd:PRK05620 250 ----TPLVFPGPD------------LSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPPE----------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 378 lcnillfkkvkallggnvRMML----SGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTITE----VSD-------Y 442
Cdd:PRK05620 297 ------------------RMSLqeiyVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARppsgVSGearwayrV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 443 STGRVGAPLiccEIKL-RDWQEGGYTCRDKpnprGEIIIGGPNVSMGYFKNEEKTED--------FSVDENGQR-----W 508
Cdd:PRK05620 359 SQGRFPASL---EYRIvNDGQVMESTDRNE----GEIQVRGNWVTASYYHSPTEEGGgaastfrgEDVEDANDRftadgW 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 509 FCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVslgkVETALKNcpfidNICAYAKSDQSYVISFvvPNQKkltvlaeqk 588
Cdd:PRK05620 432 LRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWI----YSAQLEN-----YIMAAPEVVECAVIGY--PDDK--------- 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 589 gvkgtWVEICNNPIMEAEILKEIKEVADKMKlERFETPIKVRLSPEPWT-PETGLVTDAFKLKRKELKNH 657
Cdd:PRK05620 491 -----WGERPLAVTVLAPGIEPTRETAERLR-DQLRDRLPNWMLPEYWTfVDEIDKTSVGKFDKKDLRQH 554
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
85-562 |
3.60e-09 |
|
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: 59.29 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMiaaqtcfkynfplvtlyatlgeeAVTYGLNESGAsylitsv 164
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYV-----------------------LLWLGLVKIGA------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ellesklkpalseIPGLkhiiyvdkktINKSEYPEGLeIHSmqtveelgakpenLDIPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:cd05940 54 -------------VAAL----------INYNLRGESL-AHC-------------LNVSSAKHLVVDAALYIYTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 245 KGVMMIHKNLI------AGMTGqceripeLGPKDTYVGYLPLAHVlelTAEISCVTYGCRIGYSspltlsdqsskikkgs 318
Cdd:cd05940 97 KAAIISHRRAWrggaffAGSGG-------ALPSDVLYTCLPLYHS---TALIVGWSACLASGAT---------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 319 kgdcTVLKPTLMAavpeimdriyKNVMSKVQEMNYiqrTLFkigydykleqikrGYDAPLCNILLFKKVKAL-LGGNVRM 397
Cdd:cd05940 151 ----LVIRKKFSA----------SNFWDDIRKYQA---TIF-------------QYIGELCRYLLNQPPKPTeRKHKVRM 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 398 MLSGGapLSPQTQRFMNICFCCP-VGQGYGLTE-TCG-------AGTITEVSDYSTGRVGAPLICCEIK----LRDwqEG 464
Cdd:cd05940 201 IFGNG--LRPDIWEEFKERFGVPrIAEFYAATEgNSGfinffgkPGAIGRNPSLLRKVAPLALVKYDLEsgepIRD--AE 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 465 GYTCRDKPNPRGEII--IGGPNVSMGYFKNEEKTEDFSVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEY 540
Cdd:cd05940 277 GRCIKVPRGEPGLLIsrINPLEPFDGYTDPAATEKKILRDvfKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK-GEN 355
|
490 500
....*....|....*....|..
gi 1935119612 541 VSLGKVETALKNCPFIDNICAY 562
Cdd:cd05940 356 VSTTEVAAVLGAFPGVEEANVY 377
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
77-528 |
4.62e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 59.11 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWlNYEDINQRVNHFGRGLAAQGLKPKSAIAIfcetraewmiaaqtCFKYNFPLVTLY-ATLgeeavtyglnES 155
Cdd:PRK09029 22 LRLNDEVL-TWQQLCARIDQLAAGFAQQGVVEGSGVAL--------------RGKNSPETLLAYlALL----------QC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 156 GASYLITSVELLES---KLKPALseipGLKHIIYvdkktINKSEYPEGLEIHSMQTVEElgakpenldIPPSKPVPTDLA 232
Cdd:PRK09029 77 GARVLPLNPQLPQPlleELLPSL----TLDFALV-----LEGENTFSALTSLHLQLVEG---------AHAVAWQPQRLA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 233 LIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPeLGPKDTYVGYLPLAHVLE-------LTAeiscvtyGCRIGYSSPL 305
Cdd:PRK09029 139 TMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMP-FTAQDSWLLSLPLFHVSGqgivwrwLYA-------GATLVVRDKQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 TLSDqsskikkgSKGDCT--VLKPTlmaavpeimdriyknvmskvQemnyIQRTLfkigyDYKLEQikrgydaplcniLL 383
Cdd:PRK09029 211 PLEQ--------ALAGCThaSLVPT--------------------Q----LWRLL-----DNRSEP------------LS 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 384 FKKVkaLLGGNvrmMLSggAPLSPQTQRfMNI-CFCcpvgqGYGLTETcgAGTITEV-SDYSTGrVGAPLICCEIKLRDw 461
Cdd:PRK09029 242 LKAV--LLGGA---AIP--VELTEQAEQ-QGIrCWC-----GYGLTEM--ASTVCAKrADGLAG-VGSPLPGREVKLVD- 304
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1935119612 462 qeggytcrdkpnprGEIIIGGPNVSMGYFKNEEKTEdfSVDENGqrWFCTGDIGEFHpDGCLQIIDR 528
Cdd:PRK09029 305 --------------GEIWLRGASLALGYWRQGQLVP--LVNDEG--WFATRDRGEWQ-NGELTILGR 352
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
80-251 |
1.85e-08 |
|
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: 57.50 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASY 159
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 160 LITS---------VELLESkLKPALSEIPGLKHIIyVDKKTINKSEYPEGLEIHSMQTVEELGAKPENLDippskpvPTD 230
Cdd:cd05968 167 LITAdgftrrgreVNLKEE-ADKACAQCPTVEKVV-VVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTE-------SED 237
|
170 180
....*....|....*....|.
gi 1935119612 231 LALIMYTSGSTGRPKGVMMIH 251
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
77-544 |
3.34e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 56.59 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWlNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESG 156
Cdd:PRK07470 26 LVWGDRSW-TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 157 ASYLITSVELLEsKLKPALSEIPGLKHIIyvdkkTINKSEYPEGLEihsMQTVEELGAKPENLDIPPSKPvptdlALIMY 236
Cdd:PRK07470 105 ARAMICHADFPE-HAAAVRAASPDLTHVV-----AIGGARAGLDYE---ALVARHLGARVANAAVDHDDP-----CWFFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 237 TSGSTGRPKGVMMIHKNLIAGMTGQ-CERIPELGPKDTYVGYLPLAHvleltaeiscvtyGCRIgysspltlsDQSSKIK 315
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQMAFVITNHlADLMPGTTEQDASLVVAPLSH-------------GAGI---------HQLCQVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 316 KGSKgdcTVLKPTLMAAVPEIMDRIYKNvmsKVQEMnYIQRTLFKI--------GYDYkleqikrgydaplcnillfkkv 387
Cdd:PRK07470 229 RGAA---TVLLPSERFDPAEVWALVERH---RVTNL-FTVPTILKMlvehpavdRYDH---------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 388 kallgGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTETCGAGTIT-----EVSDYSTGRVGapliCC-------E 455
Cdd:PRK07470 280 -----SSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLppalhDAEDGPDARIG----TCgfertgmE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 456 IKLRDwqEGGYTCrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLvkl 535
Cdd:PRK07470 351 VQIQD--DEGREL--PPGETGEICVIGPAVFAGYYNNPEANAKAFRDG----WFRTGDLGHLDARGFLYITGRASDM--- 419
|
....*....
gi 1935119612 536 qageYVSLG 544
Cdd:PRK07470 420 ----YISGG 424
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
85-251 |
1.23e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 55.05 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYN---FPLVTLYAtlgEEAVTYGLNESGASYLI 161
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGaawLPLDTGYP---DDRLKMMLEDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 162 TSVELLesklkPALSEIPGLKHIIYvdkktinkseypegleihsmqtvEELGAKPENLDIPPSKpvPTDLALIMYTSGST 241
Cdd:PRK10252 561 TTADQL-----PRFADVPDLTSLCY-----------------------NAPLAPQGAAPLQLSQ--PHHTAYIIFTSGST 610
|
170
....*....|
gi 1935119612 242 GRPKGVMMIH 251
Cdd:PRK10252 611 GRPKGVMVGQ 620
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
476-547 |
1.64e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 54.33 E-value: 1.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935119612 476 GEIIIGGPNVSMGYFKNEEkteDFSVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 547
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDA---SPLVD----GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
223-533 |
4.02e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.19 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 223 PSKPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIpELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYS 302
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDAL-EGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFM 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 303 SPLTLsdqsskikkgskgdctVLKP----TLMAAVPEIMDRIYKNVMSKVQEmNYIQRTLFKIGydykleqikrgyDAPL 378
Cdd:PRK07769 253 SPAAF----------------VRRPgrwiRELARKPGGTGGTFSAAPNFAFE-HAAARGLPKDG------------EPPL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 379 cnillfkkvkALlgGNVRMMLSGGAPLSPQTQRFMNICFCcPVG-------QGYGLTETC-------------------- 431
Cdd:PRK07769 304 ----------DL--SNVKGLLNGSEPVSPASMRKFNEAFA-PYGlpptaikPSYGMAEATlfvsttpmdeeptviyvdrd 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 432 --GAGTITEVSDYSTGRVgAPLICCEIKLRDWQE--GGYTCRDKPNPR-GEIIIGGPNVSMGYF-KNEEKTEDF------ 499
Cdd:PRK07769 371 elNAGRFVEVPADAPNAV-AQVSAGKVGVSEWAVivDPETASELPDGQiGEIWLHGNNIGTGYWgKPEETAATFqnilks 449
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1935119612 500 --------SVDENGqRWFCTGDIGEFHpDGCLQIIDRKKDLV 533
Cdd:PRK07769 450 rlseshaeGAPDDA-LWVRTGDYGVYF-DGELYITGRVKDLV 489
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-554 |
4.94e-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: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 226 PVPTDLaLIMYTSGSTGRPKGVMMIHKNLIAGMTGqceripelGPKDTYVGYLPLAHVLELTAEIScvtyGCRIGYSSPL 305
Cdd:cd05924 1 RSADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMG--------GADFGTGEFTPSEDAHKAAAAAA----GTVMFPAPPL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 306 TLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYK---NVMSKVQEMnyIQRTLfkigydykLEQIKRGYDAPLCNIl 382
Cdd:cd05924 68 MHGTGSWTAFGGLLGGQTVVLPDDRFDPEEVWRTIEKhkvTSMTIVGDA--MARPL--------IDALRDAGPYDLSSL- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 lfkkvkallggnvRMMLSGGAPLSPQT-QRFMNICFCCPVGQGYGLTETCGAGT-ITEVSDYSTG---RVGAPLICCEIK 457
Cdd:cd05924 137 -------------FAISSGGALLSPEVkQGLLELVPNITLVDAFGSSETGFTGSgHSAGSGPETGpftRANPDTVVLDDD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 458 LRDWQEGgytcrdkPNPRGEIIIGGpNVSMGYFKNEEKTEDFSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQA 537
Cdd:cd05924 204 GRVVPPG-------SGGVGWIARRG-HIPLGYYGDEAKTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-TG 274
|
330
....*....|....*..
gi 1935119612 538 GEYVSLGKVETALKNCP 554
Cdd:cd05924 275 GEKVFPEEVEEALKSHP 291
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
80-248 |
7.38e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 52.45 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 80 GNYRWLNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCfkynfplvtlyATLG-----------EEAV 148
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC-----------ARIGavhsvvfggfsAEAL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 149 TYGLNESGASYLITSVELLE----SKLKP----ALSEIPGLKHIIYVdKKTINKSEYPEGLEI--HSMQtveelgaKPEN 218
Cdd:PRK00174 163 ADRIIDAGAKLVITADEGVRggkpIPLKAnvdeALANCPSVEKVIVV-RRTGGDVDWVEGRDLwwHELV-------AGAS 234
|
170 180 190
....*....|....*....|....*....|.
gi 1935119612 219 LDIPPsKPVPT-DLALIMYTSGSTGRPKGVM 248
Cdd:PRK00174 235 DECEP-EPMDAeDPLFILYTSGSTGKPKGVL 264
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
234-618 |
8.56e-07 |
|
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: 51.25 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 234 IMYTSGSTGRPKGVMMIHKNLIAGMTGQcERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIGYSSPLTLSDQSSK 313
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 314 IKKGSKgdctvlkpTLMAAVPEIMDRIYKnvmskvqemnyIQRTLFKIgydykleqikrgydaplcnillfkkvkallgg 393
Cdd:cd17633 84 INQYNA--------TVIYLVPTMLQALAR-----------TLEPESKI-------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 394 nvRMMLSGGAPLSPQT----QRFMN----ICFccpvgqgYGLTEtcgAGTITEVSDYS---TGRVGAPLICCEIKLRDwQ 462
Cdd:cd17633 113 --KSIFSSGQKLFESTkkklKNIFPkanlIEF-------YGTSE---LSFITYNFNQEsrpPNSVGRPFPNVEIEIRN-A 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 463 EGGYTcrdkpnprGEIIIGGPNVSMGYFKNEEKTEDfsvdengqRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVS 542
Cdd:cd17633 180 DGGEI--------GKIFVKSEMVFSGYVRGGFSNPD--------GWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIF 242
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935119612 543 LGKVETALKNCPFIDNICAYAKSDQSYvisfvvpNQKKLTVLAEQKGVKGTWVEICNNPIMEAEILKEIKEVaDKM 618
Cdd:cd17633 243 PTEIESVLKAIPGIEEAIVVGIPDARF-------GEIAVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFV-DSL 310
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
77-582 |
8.58e-07 |
|
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: 52.07 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 77 LILGNYRWlNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYN-FPLVTLYATLGEEaVTYGLNES 155
Cdd:COG1021 44 VVDGERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGaIPVFALPAHRRAE-ISHFAEQS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 156 GASYLITS--------VELLESklkpALSEIPGLKHIIYVDkktinkseypEGLEIHSMqtvEELGAKPENLDIPPskPV 227
Cdd:COG1021 122 EAVAYIIPdrhrgfdyRALARE----LQAEVPSLRHVLVVG----------DAGEFTSL---DALLAAPADLSEPR--PD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHK----NLIAgmtgqCERIPELGPKDTYVGYLPLAHVLELtaeiscvtygcrigySS 303
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPKLIPRTHDdylySVRA-----SAEICGLDADTVYLAALPAAHNFPL---------------SS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 304 PLTLsdqsskikkG--SKGDCTVLKP----------------TLMAAVPEIMDRIyknvmskvqeMNYIQRtlfkigYDY 365
Cdd:COG1021 243 PGVL---------GvlYAGGTVVLAPdpspdtafplierervTVTALVPPLALLW----------LDAAER------SRY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 366 KLeqikrgydaplcnillfkkvkallgGNVRMMLSGGAPLSPQTQRFMNICFCCPVGQGYGLTEtcGAGTITEVSD---- 441
Cdd:COG1021 298 DL-------------------------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLVNYTRLDDpeev 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 442 -YSTgrVGAPlICC--EIKLRDWQeggytcrDKPNPRGEI---IIGGPNVSMGYFKNEEKTEDfSVDENGqrWFCTGDIG 515
Cdd:COG1021 351 iLTT--QGRP-ISPddEVRIVDED-------GNPVPPGEVgelLTRGPYTIRGYYRAPEHNAR-AFTPDG--FYRTGDLV 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 516 EFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSY---VISFVVPNQKKLT 582
Cdd:COG1021 418 RRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgerSCAFVVPRGEPLT 486
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
22-396 |
8.69e-07 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 52.55 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 22 THLESLAtidipGADTLDKLFDHAVAKFGKKDCLGtreilsEENEmqpngkvfkkliLGNYRWLNYEDINQRVNHFGRGL 101
Cdd:PTZ00297 418 REYNPLA-----GVRSLGEMWERSVTRHSTFRCLG------QTSE------------SGESEWLTYGTVDARARELGSGL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 102 AAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTL------YATLGEE---AVTYGLNESGASYLITSVELLESKLK 172
Cdd:PTZ00297 475 LALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPLvgkgstMRTLIDEhkiKVVFADRNSVAAILTCRSRKLETVVY 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 173 PAlSEIPGLKHIIYVDKktinkseypeGLEIHSMQTVEELGakpeNLDIPPSKPVPTDLALIMY-----TSGSTGRPKGV 247
Cdd:PTZ00297 555 TH-SFYDEDDHAVARDL----------NITLIPYEFVEQKG----RLCPVPLKEHVTTDTVFTYvvdntTSASGDGLAVV 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 248 MMIHKNLIAG-----MTGQcerIPELGPKDTYVGYLPLAHVLELTaeisCVtygcrigysspLTLSDQSSKIKKGSKGDC 322
Cdd:PTZ00297 620 RVTHADVLRDistlvMTGV---LPSSFKKHLMVHFTPFAMLFNRV----FV-----------LGLFAHGSAVATVDAAHL 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 323 ----TVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKIGYDYK--LEQIKRgYDAPLCNILLFKKVKALLGGNVR 396
Cdd:PTZ00297 682 qrafVKFQPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRsrLINIHR-RDSSLLRFIFFRATQELLGGCVE 760
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
228-550 |
1.18e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 51.74 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGqCERIPELGPKDTYVGYLPLAHvleltaeiscvTYGCrigysspltl 307
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRA-CLKFFSPKEDDVMMSFLPPFH-----------AYGF---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 308 sdqsskikkgskgDCTVLKPtLMAAVPEIMDriYKNVMSK--VQEMNYIQRTLF---KIGYDYKLEQIKRGyDAPLCNIL 382
Cdd:PRK06334 240 -------------NSCTLFP-LLSGVPVVFA--YNPLYPKkiVEMIDEAKVTFLgstPVFFDYILKTAKKQ-ESCLPSLR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 383 LfkkvkALLGGNV--RMMLSGGAPLSPQTQRFmnicfccpvgQGYGLTETCGAGTI-TEVSDYSTGRVGAPLICCEIKLR 459
Cdd:PRK06334 303 F-----VVIGGDAfkDSLYQEALKTFPHIQLR----------QGYGTTECSPVITInTVNSPKHESCVGMPIRGMDVLIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 460 dwQEGGYTcrdkPNPRGE---IIIGGPNVSMGYFKNEEkTEDFsVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLq 536
Cdd:PRK06334 368 --SEETKV----PVSSGEtglVLTRGTSLFSGYLGEDF-GQGF-VELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI- 438
|
330
....*....|....
gi 1935119612 537 AGEYVSLGKVETAL 550
Cdd:PRK06334 439 GAEMVSLEALESIL 452
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
228-655 |
1.87e-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: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 228 PTDLALIMYTSGSTGRPKGVMMihknliagMTGQCeripelgpkdtYVGYLPLAHVLELTAEIScvTYGCRIGYSSPLTL 307
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAI--------SWRRT-----------LVTSNLLSHDLNLKNGDR--TYTCMPLYHGTAAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 308 SDQSSKIKKGSkgdCTVLKPTLMAAvpeimdRIYKNVMSkvQEMNYIQrtlfkigydykleqikrgYDAPLCNILLF--- 384
Cdd:cd05937 145 LGACNCLMSGG---TLALSRKFSAS------QFWKDVRD--SGATIIQ------------------YVGELCRYLLStpp 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 385 -KKVKAllgGNVRMMLSGGapLSPQT-QRFMNIcFCCP-VGQGYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDW 461
Cdd:cd05937 196 sPYDRD---HKVRVAWGNG--LRPDIwERFRER-FNVPeIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 462 Q----------------EGGYTCRDKPNPRGEII--IGGPNVSM--GYFKNEEKTED---FSVDENGQRWFCTGDIGEFH 518
Cdd:cd05937 270 VvlvkmdpetddpirdpKTGFCVRAPVGEPGEMLgrVPFKNREAfqGYLHNEDATESklvRDVFRKGDIYFRTGDLLRQD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 519 PDGCLQIIDRKKDLVKLQaGEYVSLGKVEtalkncpfiDNICAYAKSDQSYVISFVVPNQKKltvlaeQKGVKGtwVEIC 598
Cdd:cd05937 350 ADGRWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHPDIAEANVYGVKVPGHDG------RAGCAA--ITLE 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1935119612 599 NNPIMEAEILKEIKEVADKMKLERFETPIKVRLSPEpwtpetGLVTDAFKLKRKELK 655
Cdd:cd05937 412 ESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VATTDNHKQQKGVLR 462
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
424-577 |
2.35e-06 |
|
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: 49.99 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 424 GYGLTETCGAGTITEVSDYSTGRVGAPLICCEIKLRDwQEGgytcRDKPNPR-GEIIIGGPNVSMGYFKNEEktedfsvd 502
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDG----REVPDGEvGEIVARGPTVMAGYWNRPE-------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 503 ENGQR----WFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCPFIDNICAYAKSD----QSyVISFV 574
Cdd:cd17636 209 VNARRtrggWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAAVIGVPDprwaQS-VKAIV 286
|
...
gi 1935119612 575 VPN 577
Cdd:cd17636 287 VLK 289
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
198-549 |
3.59e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.15 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 198 PEGLEIHSMQTVeelGAKPENLDIPPskPVPTDLALIMYTSGSTGRPKGVMMIHKNLIAGMTGQCERIPELGPKDTYVGY 277
Cdd:PRK05851 126 DSSVTVHDLATA---AHTNRSASLTP--PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSW 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 278 LPLAHVLELTAEISCVTYGcrigysSPLTLSDQSSkikkgskgdctvlkptlMAAVPeimdriyknvMSKVQEMNYIQRT 357
Cdd:PRK05851 201 LPLYHDMGLAFLLTAALAG------APLWLAPTTA-----------------FSASP----------FRWLSWLSDSRAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 358 LFK---IGYDYKLEQIKRGYDAPLcnillfkkvkallgGNVRMMLSGGAPLSPQ-TQRFMNICfcCPVG-------QGYG 426
Cdd:PRK05851 248 LTAapnFAYNLIGKYARRVSDVDL--------------GALRVALNGGEPVDCDgFERFATAM--APFGfdagaaaPSYG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 427 LTE-TC-------GAG-TITEVSDYSTG------RVGAPLICCEIKLrdwqeggyTCRDKPNPR-----GEIIIGGPNVS 486
Cdd:PRK05851 312 LAEsTCavtvpvpGIGlRVDEVTTDDGSgarrhaVLGNPIPGMEVRI--------SPGDGAAGVagreiGEIEIRGASMM 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935119612 487 MGYFKNEektedfSVDEngQRWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAGEYVSLGKVETA 549
Cdd:PRK05851 384 SGYLGQA------PIDP--DDWFPTGDLGYL-VDGGLVVCGRAKELITV-AGRNIFPTEIERV 436
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
221-582 |
7.52e-06 |
|
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: 49.04 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 221 IPPSKPVPTDLALIMYTSGSTGRPKGVMMIHKNL---IAGMTGQCERipELGPKDTYVGYLPLAHVLE----LTAEISCV 293
Cdd:cd05923 142 IEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAesrVLFMSTQAGL--RHGRHNVVLGLMPLYHVIGffavLVAALALD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 294 TYGCRIGYSSPltlSDQSSKIKKgskgdctvLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQRTLFKigydykleqikrg 373
Cdd:cd05923 220 GTYVVVEEFDP---ADALKLIEQ--------ERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFA------------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 374 yDAPLCNILLfKKVKALLGGnvrmmlsggaplspqtqRFMNIcfccpvgqgYGLTEtcgAGTITEVSDYSTGRVGAPLIC 453
Cdd:cd05923 276 -GATMPDAVL-ERVNQHLPG-----------------EKVNI---------YGTTE---AMNSLYMRDARTGTEMRPGFF 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 454 CEIKLRdwQEGGYTCRDKPN-PRGEIII--GGPNVSMGYFKNEEKTEDFSVDengqRWFCTGDIGEFHPDGCLQIIDRKK 530
Cdd:cd05923 325 SEVRIV--RIGGSPDEALANgEEGELIVaaAADAAFTGYLNQPEATAKKLQD----GWYRTGDVGYVDPSGDVRILGRVD 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1935119612 531 DLVkLQAGEYVSLGKVETALKNCPFIDNICAYAKSDQSY---VISFVVPNQKKLT 582
Cdd:cd05923 399 DMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWgqsVTACVVPREGTLS 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
85-251 |
1.78e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.24 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDR 2293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLEsklkpALSEIPGLKHIIYVDKKTINKSEYPEgleihsmqtveelgakpenlDIPPSKPVPTDLALIMYTSGSTGRP 244
Cdd:PRK05691 2294 ALFE-----ALGELPAGVARWCLEDDAAALAAYSD--------------------APLPFLSLPQHQAYLIYTSGSTGKP 2348
|
....*..
gi 1935119612 245 KGVMMIH 251
Cdd:PRK05691 2349 KGVVVSH 2355
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
66-569 |
3.83e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 46.70 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 66 EMQPNgkvfKKLILGNYRWLNYEDINQRVNHFGRGLAAQGLKPKsAIAIFCETRAEWMIaaqtcfkynfpLVTLYATLGE 145
Cdd:PRK07638 12 SLQPN----KIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQ-----------LFAGAAMAGW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 146 EAVTYGLNESGAsylitsvELLEsklKPALSEiPGLkhiIYVDKKTINKSEYPEG--LEI-HSMQTVEElgakpeNLDIP 222
Cdd:PRK07638 76 TCVPLDIKWKQD-------ELKE---RLAISN-ADM---IVTERYKLNDLPDEEGrvIEIdEWKRMIEK------YLPTY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 223 PSKPVPTDLALIM-YTSGSTGRPKGVMMIHKNLIAGMtgQC-ERIPELGPKDTYVGYLPLAHVLELTAEISCVTYGCRIG 300
Cdd:PRK07638 136 APIENVQNAPFYMgFTSGSTGKPKAFLRAQQSWLHSF--DCnVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 301 YSSPLTLSDQSSKIKKGSKgdctvlkpTLMAAVPEIMDRIYKNVMSKVQEMNYIQRtlfkiGYDYKLEQIKRgydapLCN 380
Cdd:PRK07638 214 LMRKFIPNQVLDKLETENI--------SVMYTVPTMLESLYKENRVIENKMKIISS-----GAKWEAEAKEK-----IKN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 381 ILlfkkvkallggnvrmmlsggaplsPQTQRFmnicfccpvgQGYGLTETcgaGTITEVSDYSTGR----VGAPliCCEI 456
Cdd:PRK07638 276 IF------------------------PYAKLY----------EFYGASEL---SFVTALVDEESERrpnsVGRP--FHNV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 457 KLRDWQEGGYTCrdKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQ 536
Cdd:PRK07638 317 QVRICNEAGEEV--QKGEIGTVYVKSPQFFMGYIIGGVLARELNADG----WMTVRDVGYEDEEGFIYIVGREKNMI-LF 389
|
490 500 510
....*....|....*....|....*....|...
gi 1935119612 537 AGEYVSLGKVETALKNCPFIDNICAYAKSDqSY 569
Cdd:PRK07638 390 GGINIFPEEIESVLHEHPAVDEIVVIGVPD-SY 421
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
211-566 |
5.94e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.21 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 211 ELGAKPENLDIPPSKPVPTDLALIMYTSGSTGRPKGVMMIHKNL------IAGMTGqceripeLGPKDT-YVGyLPLAHV 283
Cdd:PRK07867 134 DELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVasagvmLAQRFG-------LGPDDVcYVS-MPLFHS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 284 LELTAeiscvtygcriGYSSPLtlsdqsskikkgSKGDCTVLKPTLMAA--VPEImdRIYknvmsKVQEMNYIQRTLfki 361
Cdd:PRK07867 206 NAVMA-----------GWAVAL------------AAGASIALRRKFSASgfLPDV--RRY-----GATYANYVGKPL--- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 362 gyDYKLEQIKRGYDA--PLcnillfkkvkallggnvRMMLSG-GAPlsPQTQRFMNIcFCCPVGQGYGLTEtcGAGTITE 438
Cdd:PRK07867 253 --SYVLATPERPDDAdnPL-----------------RIVYGNeGAP--GDIARFARR-FGCVVVDGFGSTE--GGVAITR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 439 VSDYSTGRVG--APliccEIKLRDwQEGGYTC---RDKPNPR-------GEII-IGGPNVSMGYFKNEEKTEDFSVDenG 505
Cdd:PRK07867 309 TPDTPPGALGplPP----GVAIVD-PDTGTECppaEDADGRLlnadeaiGELVnTAGPGGFEGYYNDPEADAERMRG--G 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935119612 506 QRWfcTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCPFIDNICAYAKSD 566
Cdd:PRK07867 382 VYW--SGDLAYRDADGYAYFAGRLGDWMRVD-GENLGTAPIERILLRYPDATEVAVYAVPD 439
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
478-568 |
8.12e-05 |
|
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: 45.88 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 478 IIIGGPNVSMGYFKNEEKTEDFSVDENgqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVETALKNCPFID 557
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDG---FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLENALMGHPKVK 438
|
90
....*....|.
gi 1935119612 558 NICAYAKSDQS 568
Cdd:cd05915 439 EAAVVAIPHPK 449
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-533 |
9.79e-05 |
|
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: 45.53 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 226 PVPTDLALIMYTSGSTGRPKGVMMIHKNLIAgmtgQCERIPEL-GPKDTYV---GYLPLA---HVLELTAEIScvtygcR 298
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAA----QIDALRQLyGIRPGEVdlaTFPLFAlfgPALGLTSVIP------D 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 299 IGYSSPLTLSDQS--SKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmskvqemnyiqrTLFKIGYDYKLEQIKR--GY 374
Cdd:cd05910 152 MDPTRPARADPQKlvGAIRQ--------YGVSIVFGSPALLERV----------------ARYCAQHGITLPSLRRvlSA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 375 DAPlcnillfkkVKALLGGNVRMMLSGGAP-LSPqtqrfmnicfccpvgqgYGLTETCGAGTI---------TEVSDYST 444
Cdd:cd05910 208 GAP---------VPIALAARLRKMLSDEAEiLTP-----------------YGATEALPVSSIgsrellattTAATSGGA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 445 GR-VGAPLICCEIKL-----RDWQEGGYTCRDKPNPRGEIIIGGPNVSMGYFKNEEKTEDFSVDENGQR-WFCTGDIGEF 517
Cdd:cd05910 262 GTcVGRPIPGVRVRIieiddEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGfWHRMGDLGYL 341
|
330
....*....|....*.
gi 1935119612 518 HPDGCLQIIDRKKDLV 533
Cdd:cd05910 342 DDEGRLWFCGRKAHRV 357
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
7-302 |
1.05e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 45.48 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 7 AKPISDKPGSPFRSVTHLESLATIDIPGADTLDKLFDHAVAKFGKkdclgtreILSEENEMQPNGKVFkkliLGNYRWLN 86
Cdd:PRK07868 407 ARGAADAAVAANRSVRTLAVETARTLPRLARLGQINDHTRISLGR--------IIAEQARDAPKGEFL----LFDGRVHT 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 87 YEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAaqtcfkynfplVTLYATLGEEAVTYG----LNES----GAS 158
Cdd:PRK07868 475 YEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVA-----------IAALSRLGAVAVLMPpdtdLAAAvrlgGVT 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 159 YLITSVELLEsklkpALSEIPGlkHIIYVDKKTINKSEYPEGLEIHSMQTVEelgakPENLDIP----PSKPVPTDLALI 234
Cdd:PRK07868 544 EIITDPTNLE-----AARQLPG--RVLVLGGGESRDLDLPDDADVIDMEKID-----PDAVELPgwyrPNPGLARDLAFI 611
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 235 MY-TSGSTGRPKGVMMIHKNLIAGMTGQCERipeLGPKDTYVGYLPLAHVLELTAEI-SCVTYGCRIGYS 302
Cdd:PRK07868 612 AFsTAGGELVAKQITNYRWALSAFGTASAAA---LDRRDTVYCLTPLHHESGLLVSLgGAVVGGSRIALS 678
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
209-554 |
5.19e-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: 43.13 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 209 VEELGAKPENldiPPSKPVPTDLalIMYTSGSTGRPKGVM------MIHKNLIAGMTGQCEripeLGPKDTYVGYLPLAH 282
Cdd:cd05929 110 EAAEGGSPET---PIEDEAAGWK--MLYSGGTTGRPKGIKrglpggPPDNDTLMAAALGFG----PGADSVYLSPAPLYH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 283 vleltaeiscvtygcrigySSPLTLSDQSSKIkkgskGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYI----QRTL 358
Cdd:cd05929 181 -------------------AAPFRWSMTALFM-----GGTLVLMEKFDPE--EFLRLIERY---RVTFAQFVptmfVRLL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 359 fkigydyKLEQIKRG-YDaplcnillfkkVKALlggnvRMMLSGGAPLSPQTQRFMnICFCCP-VGQGYGLTEtCGAGTI 436
Cdd:cd05929 232 -------KLPEAVRNaYD-----------LSSL-----KRVIHAAAPCPPWVKEQW-IDWGGPiIWEYYGGTE-GQGLTI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 437 TEVSDYST--GRVGAPLICcEIKLRDwqEGGYTCrdKPNPRGEIIIGGPNvSMGYFKNEEKTEDfSVDENGqrWFCTGDI 514
Cdd:cd05929 287 INGEEWLThpGSVGRAVLG-KVHILD--EDGNEV--PPGEIGEVYFANGP-GFEYTNDPEKTAA-ARNEGG--WSTLGDV 357
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1935119612 515 GEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVETALKNCP 554
Cdd:cd05929 358 GYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHP 396
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
85-269 |
7.88e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEW--MIAAQtcFKYNFPLVTLYATLGEEAVTYGLNESGASYLIT 162
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLlgMIVGS--FKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVC 3823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 163 SVELLES--KLKPALSEIPGLKHIIYVDKKTINKSEYPEGleIHSmqtveelgakpenldippskpVPTDLALIMYTSGS 240
Cdd:PRK05691 3824 SAACREQarALLDELGCANRPRLLVWEEVQAGEVASHNPG--IYS---------------------GPDNLAYVIYTSGS 3880
|
170 180 190
....*....|....*....|....*....|
gi 1935119612 241 TGRPKGVMMIHknliAGM-TGQCERIPELG 269
Cdd:PRK05691 3881 TGLPKGVMVEQ----RGMlNNQLSKVPYLA 3906
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
428-626 |
1.29e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 41.73 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 428 TETCGAGTITEV----SDYSTGRVGAPLICCEIKLRDW--QEGGYTCRDKpnprgeiiiggpnvsmgyfKNEEKTEDFSV 501
Cdd:cd17647 307 TQICGIGEVGEIyvraGGLAEGYRGLPELNKEKFVNNWfvEPDHWNYLDK-------------------DNNEPWRQFWL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 502 DENgQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVETALKNCPFI-DNICAYA--KSDQSYVISFVVPNQ 578
Cdd:cd17647 368 GPR-DRLYRTGDLGRYLPNGDCECCGRADDQVKIR-GFRIELGEIDTHISQHPLVrENITLVRrdKDEEPTLVSYIVPRF 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1935119612 579 KKLTVLAEQKGVKGTwvEICNNPIMEA-----EILKEIKEVAdKMKLERFETP 626
Cdd:cd17647 446 DKPDDESFAQEDVPK--EVSTDPIVKGligyrKLIKDIREFL-KKRLASYAIP 495
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
85-246 |
2.17e-03 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 41.28 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 85 LNYEDINQRVNHFGRGLAAQGLKPKSAIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGEEAVTYGLNESGASYLITSV 164
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 165 ELLESkLKPALSEIPGLKHIIyvdkktinksEYPEGLEIHsmqTVEELGAKPENLDIPPSkpvPTDLALIMYTSGSTGRP 244
Cdd:PRK13382 149 EFSAT-VDRALADCPQATRIV----------AWTDEDHDL---TVEVLIAAHAGQRPEPT---GRKGRVILLTSGTTGTP 211
|
..
gi 1935119612 245 KG 246
Cdd:PRK13382 212 KG 213
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
423-554 |
2.25e-03 |
|
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: 40.94 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935119612 423 QGYGLTETcgagTITEVS----DYSTGRVGAPLICCEIKLRDwqEGGYTCrdKPNPRGEIII----GGPnVSM--GYFKN 492
Cdd:cd05970 331 EGFGQTET----TLTIATfpwmEPKPGSMGKPAPGYEIDLID--REGRSC--EAGEEGEIVIrtskGKP-VGLfgGYYKD 401
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935119612 493 EEKTEdfSVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVETALKNCP 554
Cdd:cd05970 402 AEKTA--EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHP 458
|
|
| |
