|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
80-655 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 826.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 159
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 LITSvellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrPTPSDMAIVMYTSG 239
Cdd:cd17639 81 IFTD--------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 240 STGRPKGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqssKIKKGS 318
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 319 KGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMM 398
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 399 LSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYtVHDKPNPRGEI 478
Cdd:cd17639 256 LSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGY-STDKPPPRGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 479 VIGGQNISMGYFKNEEKTAEDYcvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLID 558
Cdd:cd17639 334 LIRGPNVFKGYYKNPEKTKEAF----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 559 NICAFAKSDQSYVISFVVPNQKKLTLLAQQKGV-EGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPW 637
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 75992927 638 TPETGLVTDAFKLKRKEL 655
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
24-667 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 809.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 24 FDSLavIDIP--GADTLDKLFDHAVAKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGL 101
Cdd:PLN02387 46 FPEL--VETPweGATTLAALFEQSCKKYSDKRLLGTRKLISREFETSSDGRKFEKLHLGEYEWITYGQVFERVCNFASGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 102 TALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLEsKLKAALVDINCV 181
Cdd:PLN02387 124 VALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLK-KLIDISSQLETV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 182 KHIIYVDNKTINRAEYPEGLE---IHSMQSVEELGakpENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGM 258
Cdd:PLN02387 203 KRVIYMDDEGVDSDSSLSGSSnwtVSSFSEVEKLG---KENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 259 TGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMD 338
Cdd:PLN02387 280 AGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTLMTAVPAILD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 339 RIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKK------GYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRF 412
Cdd:PLN02387 360 RVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGswfgawGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRF 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 413 MNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKN 492
Cdd:PLN02387 440 INICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKN 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 493 EEKTAEDYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVI 572
Cdd:PLN02387 520 QEKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCV 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 573 SFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLK 651
Cdd:PLN02387 600 ALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLK 679
|
650
....*....|....*.
gi 75992927 652 RKELKNHYLKDIERMY 667
Cdd:PLN02387 680 REQIRKKFKDDLKKLY 695
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
80-667 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 535.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNT--IAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEA 157
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 158 SylitsvellesklkaalvdincvkhIIYVDnktinraeypEGLEIHSMQSVEELGAKPEnlsVPPSRPTPSDMAIVMYT 237
Cdd:cd05927 81 S-------------------------IVFCD----------AGVKVYSLEEFEKLGKKNK---VPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 238 SGSTGRPKGVMMHHSNLIAGMTGQC---ERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSS--PLTLSDqss 312
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 313 kikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKG--YDAPLCNLILFKKVKAL 390
Cdd:cd05927 200 --------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 391 LGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVhD 470
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDA-K 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 471 KPNPRGEIVIGGQNISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAA 550
Cdd:cd05927 351 DPNPRGEVCIRGPNVFSGYYKDPEKTAEA--LDEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 551 LKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQK-GVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIK 629
Cdd:cd05927 427 YARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKA 506
|
570 580 590
....*....|....*....|....*....|....*...
gi 75992927 630 VRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 667
Cdd:cd05927 507 IHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
31-670 |
4.16e-152 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 453.40 E-value: 4.16e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 31 DIPGADTLDKLFDHAVAKFGKKDSLGTREilseenemqpngkvfkkliLGNYKWINYLEVNCRVNNFGSGLTALGLKPKN 110
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKE-------------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 111 TIAIFCETRAEWMIA--------AQTcfkynfplVTLYATLGREAVVHGLNESEASYLITSVELLESKLKAALVDINCVK 182
Cdd:COG1022 67 RVAILSDNRPEWVIAdlailaagAVT--------VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 183 HIIYVDNKTInraeyPEGLEIHSMQSVEELGAK---PENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT 259
Cdd:COG1022 139 HIVVLDPRGL-----RDDPRLLSLDELLALGREvadPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 260 GQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYS-SPLTLSDqsskikkgskgDCTVLKPTLMAAVPEIMD 338
Cdd:COG1022 214 ALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------DLREVKPTFMLAVPRVWE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 339 RIYKNVMSKVQEMNYVQKTLF----KIGYDYKlEQIKKGYDAP--------LCNLILFKKVKALLGGNVRMMLSGGAPLS 406
Cdd:COG1022 282 KVYAGIQAKAEEAGGLKRKLFrwalAVGRRYA-RARLAGKSPSlllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 407 PQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLkdwqeggytvhdkpNPRGEIVIGGQ 483
Cdd:COG1022 361 PELARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI--------------AEDGEILVRGP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 484 NISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAF 563
Cdd:COG1022 423 NVMKGYYKNPEATAEA--FDADG--WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVV 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 564 AkSDQSYVISFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEPWTPETG 642
Cdd:COG1022 499 G-DGRPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEV-DRANA-GLSRAEQIKRFRLLPKEFTIENG 575
|
650 660
....*....|....*....|....*...
gi 75992927 643 LVTDAFKLKRKELKNHYLKDIERMYGGK 670
Cdd:COG1022 576 ELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
15-667 |
1.30e-151 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 453.79 E-value: 1.30e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 15 GSPYRSVTHFDslaviDIPGADTLDKLFDHAVAKFGKKDSLGTReilseeneMQPNGKVfkklilGNYKWINYLEVNCRV 94
Cdd:PLN02736 28 RSPLKLVSRFP-----DHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 95 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESKLkAA 174
Cdd:PLN02736 89 TAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLL-SC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 175 LVDINCVKHIIYVDNKTINRAEYPE--GLEIHSMQSVEELGAKPenlSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 252
Cdd:PLN02736 168 LSEIPSVRLIVVVGGADEPLPSLPSgtGVEIVTYSKLLAQGRSS---PQPFRPPKPEDVATICYTSGTTGTPKGVVLTHG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 253 NLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSP--LTLSDqsskikkgskgDCTVLKPTLM 330
Cdd:PLN02736 245 NLIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGdnLKLMD-----------DLAALRPTIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 331 AAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD-APLCNLILFKKVKALLGGNVRMMLSGGAPLSPQT 409
Cdd:PLN02736 313 CSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 410 HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGY 489
Cdd:PLN02736 393 MEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 490 FKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS 569
Cdd:PLN02736 473 YKDEVQTRE--VIDEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 570 YVISFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAF 648
Cdd:PLN02736 549 SLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTF 628
|
650
....*....|....*....
gi 75992927 649 KLKRKELKNHYLKDIERMY 667
Cdd:PLN02736 629 KVKRPQAKAYFAKAISDMY 647
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
83-667 |
8.53e-145 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 437.87 E-value: 8.53e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 83 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLIT 162
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 163 S---VELLESKLKAALVDiNCVkhIIYVDnktinraEYPEGLEIHSMQ-----SVEELGAKPENlSVPPSRPTPSD-MAI 233
Cdd:PTZ00216 200 NgknVPNLLRLMKSGGMP-NTT--IIYLD-------SLPASVDTEGCRlvawtDVVAKGHSAGS-HHPLNIPENNDdLAL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 234 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGL-GPK---DTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSD 309
Cdd:PTZ00216 269 IMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGPPeedETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 310 QSSKikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKA 389
Cdd:PTZ00216 349 TFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 390 LLGGNVRMMLSGGAPLSPQTHRFMNVCFcCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvh 469
Cdd:PTZ00216 425 VLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHT-- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 470 DKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEA 549
Cdd:PTZ00216 502 DTPEPRGEILLRGPFLFKGYYKQEELTRE--VLDEDG--WFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 550 ALKNCPLIDN--ICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIP 627
Cdd:PTZ00216 578 LYGQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIV 657
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 75992927 628 IKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 667
Cdd:PTZ00216 658 RHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
80-655 |
7.92e-135 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 403.51 E-value: 7.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 159
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 LITSvellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrpTPSDMAIVMYTSG 239
Cdd:cd05907 81 LFVE---------------------------------------------------------------DPDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 240 STGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRIGYSSPL-TLSDQSSKIkkg 317
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAeTLLDDLSEV--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 318 skgdctvlKPTLMAAVPEIMDRIYKNVmsKVQEMNYVQKTLFKIGydykleqikkgydaplcnlilfkkvkalLGGNVRM 397
Cdd:cd05907 174 --------RPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLA----------------------------VGGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 398 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytvhdkpnpRGE 477
Cdd:cd05907 216 AASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--------------DGE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 478 IVIGGQNISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 557
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAEA--LDADG--WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLI 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 558 DNICAFAkSDQSYVISFVVPNQKKLTLLAQQKGVEG-SWVDICNNPAMEAEILKEIrEAANAmKLERFEIPIKVRLSPEP 636
Cdd:cd05907 357 SQAVVIG-DGRPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAV-EAANA-RLSRYEQIKKFLLLPEP 433
|
570
....*....|....*....
gi 75992927 637 WTPETGLVTDAFKLKRKEL 655
Cdd:cd05907 434 FTIENGELTPTLKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
3-667 |
4.94e-123 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 380.31 E-value: 4.94e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 3 KRIKAKPTSdkpGSPYRSVTHFDSLAVIDiPGADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGNY 82
Cdd:PLN02430 13 KGKDGKPSV---GPVYRNLLSKKGFPPID-SDITTAWDIFSKSVEKYPDNKMLGWRRIV--------DGKV------GPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 83 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEasylIT 162
Cdd:PLN02430 75 MWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAE----ID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 163 SVELLESKLKAaLVDINC-----VKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGAKPENLSvPPSRPTPSDMAIVMYT 237
Cdd:PLN02430 151 FVFVQDKKIKE-LLEPDCksakrLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPS-ETNPPKPLDICTIMYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 238 SGSTGRPKGVMMHHSNLIAGMTG------QCEriPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQS 311
Cdd:PLN02430 229 SGTSGDPKGVVLTHEAVATFVRGvdlfmeQFE--DKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYH----GDLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 312 SKikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD----APLCNLILFKKV 387
Cdd:PLN02430 303 AL-----RDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLAFRKV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 388 KALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPLICCEIKLKDWQEGGY 466
Cdd:PLN02430 378 KAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 467 TVHDKPnPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGK 546
Cdd:PLN02430 458 DPLGEP-PRGEICVRGKCLFSGYYKNPELTEE---VMKDG--WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEY 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 547 VEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEI 626
Cdd:PLN02430 532 LENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEY 611
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 75992927 627 PIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 667
Cdd:PLN02430 612 IKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
6-667 |
8.65e-115 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 358.77 E-value: 8.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 6 KAKPTSD-KP--GSPYRSVTHFDSLavIDIP-GADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGN 81
Cdd:PLN02861 11 ESRPATGgKPsaGPVYRSIYAKDGL--LDLPaDIDSPWQFFSDAVKKYPNNQMLGRRQVT--------DSKV------GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 82 YKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASylI 161
Cdd:PLN02861 75 YVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 162 TSVEllESKLKAAL-VDINCVKHIIYV----DNKTINRAEYPE-GLEIHSMQSVEELGAKPENLsvPPSRPTpsDMAIVM 235
Cdd:PLN02861 153 AFVQ--ESKISSILsCLPKCSSNLKTIvsfgDVSSEQKEEAEElGVSCFSWEEFSLMGSLDCEL--PPKQKT--DICTIM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 236 YTSGSTGRPKGVMMHHSNLIAG------MTGQCERIpgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSD 309
Cdd:PLN02861 227 YTSGTTGEPKGVILTNRAIIAEvlstdhLLKVTDRV--ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQ----GD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 310 QSSKIKkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD----APLCNLILFK 385
Cdd:PLN02861 301 IRYLME-----DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRLVFD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 386 KVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGaGTVTEVTDY--TTGRVGAPLICCEIKLKDWQE 463
Cdd:PLN02861 376 KIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANVfsMVGTVGVPMTTIEARLESVPE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 464 GGYTVHDKPnPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVS 543
Cdd:PLN02861 455 MGYDALSDV-PRGEICLRGNTLFSGYHKRQDLTEE---VLIDG--WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 544 LGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLER 623
Cdd:PLN02861 529 VENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 75992927 624 FEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 667
Cdd:PLN02861 609 FEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
77-537 |
4.58e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.22 E-value: 4.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 77 LILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESE 156
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 157 ASYLITSVELLESKLKAALVDINCVKHIIYVDNKTINRAEypegleihsmqSVEELGAKPENLSVPPSRPTPSDMAIVMY 236
Cdd:pfam00501 94 AKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 237 TSGSTGRPKGVMMHHSNLIAGMTGQ---CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSPLTLSDQss 312
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALDP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 313 kikKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmskvqemnyvqktlfkigydykleqikkgydaplcnlilfKKVKALLG 392
Cdd:pfam00501 241 ---AALLELIERYKVTVLYGVPTLLNMLLEA-----------------------------------------GAPKRALL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 393 GNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDWQEGGYTVH 469
Cdd:pfam00501 277 SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPlplDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPP 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 470 DKPnprGEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQ 537
Cdd:pfam00501 357 GEP---GELCVRGPGVMKGYLNDPELTAEAFDED----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
7-667 |
1.19e-112 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 353.56 E-value: 1.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 7 AKPTSD-KP--GSPYRSVTHFDSLAViDIPGADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGNYK 83
Cdd:PLN02614 14 GKEGSDgRPsvGPVYRSIFAKDGFPN-PIEGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 84 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITS 163
Cdd:PLN02614 79 WQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 164 VELLESKLKAALVDINCVKHIIYVDNKTINRAEYPE--GLEIHSMQSVEELGaKPENLSVPPSRPtpSDMAIVMYTSGST 241
Cdd:PLN02614 159 EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLG-EGKQYDLPIKKK--SDICTIMYTSGTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 242 GRPKGVMMHHSNLIAGMTGQCERI----PGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQSSKIKkg 317
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAGVIRLLksanAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR----GDVKLLIE-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 318 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIKKGYD----APLCNLILFKKVKALLGG 393
Cdd:PLN02614 310 ---DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 394 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCgAGTVTEVTDY--TTGRVGAPLICCEIKLKDWQEGGYTVHDK 471
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVDIRLESVPEMEYDALAS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 472 pNPRGEIVIGGQNISMGYFKNEEKTAEDYcVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAAL 551
Cdd:PLN02614 466 -TPRGEICIRGKTLFSGYYKREDLTKEVL-IDG----WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIY 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 552 KNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVR 631
Cdd:PLN02614 540 GEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIH 619
|
650 660 670
....*....|....*....|....*....|....*.
gi 75992927 632 LSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMY 667
Cdd:PLN02614 620 LDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
80-652 |
2.21e-70 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 236.49 E-value: 2.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFkynfplvtlyaTLGREAVVHGLNES--EA 157
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIM-----------ALGAVDVVRGSDSSveEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 158 SYLITSVEllesklkaalvdinCVkhIIYVDNktinraeypegleihsmqsveelgakpenlsvppsrpTPSDMAIVMYT 237
Cdd:cd17640 70 LYILNHSE--------------SV--ALVVEN-------------------------------------DSDDLATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 238 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGlGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkg 317
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPP-QPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKD-------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 318 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIgydykleqikkgydaplcnlilfkkvkALLGGNVRM 397
Cdd:cd17640 168 ---DLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF---------------------------FLSGGIFKF 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 398 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvhdKPNPRGE 477
Cdd:cd17640 218 GISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVL---PPGEKGI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 478 IVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLI 557
Cdd:cd17640 294 VWVRGPQVMKGYYKNPEATSK--VLDSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFI 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 558 DNICAFAKsDQSYVISFVVPNQKKLTLLAQQKGV---EGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSP 634
Cdd:cd17640 370 EQIMVVGQ-DQKRLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLE 448
|
570
....*....|....*...
gi 75992927 635 EPWTpETGLVTDAFKLKR 652
Cdd:cd17640 449 EPFI-ENGEMTQTMKIKR 465
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
85-662 |
1.63e-63 |
|
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: 217.37 E-value: 1.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 164
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptpsdmAIVMYTSGSTGRP 244
Cdd:COG0318 103 -------------------------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI---GYSSPLTLSDQsskIKKGskg 320
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAAL-GLTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLvllPRFDPERVLEL---IERE--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 321 dctvlKPTLMAAVPEIMDRIyknvmskvqeMNYVQKTlfkigydykleqikkGYDAPlcnlilfkkvkallggNVRMMLS 400
Cdd:COG0318 189 -----RVTVLFGVPTMLARL----------LRHPEFA---------------RYDLS----------------SLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 401 GGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDwqEGGYTVhdKPNPRGE 477
Cdd:COG0318 223 GGAPLPPELlERFEER-FGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVD--EDGREL--PPGEVGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 478 IVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 557
Cdd:COG0318 298 IVVRGPNVMKGYWNDPEATAE---AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAHPGV 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 558 DNICAFAKSDQSY---VISFVVPNqkkltllaqqkgvEGSWVDicnnpamEAEILKEIREaanamKLERFEIPIKVRLSP 634
Cdd:COG0318 372 AEAAVVGVPDEKWgerVVAFVVLR-------------PGAELD-------AEELRAFLRE-----RLARYKVPRRVEFVD 426
|
570 580
....*....|....*....|....*....
gi 75992927 635 E-PWTPeTGlvtdafKLKRKELKNHYLKD 662
Cdd:COG0318 427 ElPRTA-SG------KIDRRALRERYAAG 448
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
84-624 |
8.87e-60 |
|
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: 210.36 E-value: 8.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 84 WINYLEvncRVNNFGSGLTALGLKPKNTIAIFCETRAEW---MIAAQTCFKYNFPLvtlYATLGREAVVHGLNESEASYL 160
Cdd:cd17641 14 WADYAD---RVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALSLGI---YQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ITSVELLESKLKAALVDINCVKHIIYVDNKTINRAEYPEgleIHSMQSVEELG-----AKPENLSVPPSRPTPSDMAIVM 235
Cdd:cd17641 88 IAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPR---LISFEDVVALGraldrRDPGLYEREVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 236 YTSGSTGRPKGVMMHHSNLIaGMTGQCERIPGLGPKDTYIGYLPLAHVLELT-----AEISCFTYGCrigYSSPLTLsdq 310
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFL-GHCAAYLAADPLGPGDEYVSVLPLPWIGEQMysvgqALVCGFIVNF---PEEPETM--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 311 sskikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYD--YK-LEQIKKGYDAP--------LC 379
Cdd:cd17641 238 --------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKlgLRaLDRGKRGRPVSlwlrlaswLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 380 NLILFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCE 455
Cdd:cd17641 310 DALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 456 IKLKDwqeggytvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 535
Cdd:cd17641 386 VRIDE--------------VGEILVRSPGVFVGYYKNPEATAED--FDEDG--WLHTGDAGYFKENGHLVVIDRAKDVGT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 536 LQAGEYVSLGKVEAALKNCPLIDNICAFAKsDQSYVISFVVPNQKKLTLLAQQKGVE-GSWVDICNNPAMEAEILKEIRE 614
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAEAVVLGA-GRPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEK 526
|
570
....*....|....
gi 75992927 615 A----ANAMKLERF 624
Cdd:cd17641 527 VnaslPEAQRIRRF 540
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
80-659 |
1.28e-55 |
|
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: 197.69 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 159
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 LITsvellesklkAALVDINCVKHIIyvdnktinraeyPEGLEIHSMQSVEELGAKPE--------NLSVPPSRPTPSDM 231
Cdd:cd05932 82 LFV----------GKLDDWKAMAPGV------------PEGLISISLPPPSAANCQYQwddliaqhPPLEERPTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 232 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTA-EISCFTYGCRIGYSSPLTLSDQ 310
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 311 sskikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKV--QEMNyvqkTLFKIgydykleqikkgydaPLCNLILFKKVK 388
Cdd:cd05932 219 ----------DVQRARPTLFFSVPRLWTKFQQGVQDKIpqQKLN----LLLKI---------------PVVNSLVKRKVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 389 ALLGGN-VRMMLSGGAPLSPQT-HRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggy 466
Cdd:cd05932 270 KGLGLDqCRLAGCGSAPVPPALlEWYRSLGL--NILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 467 tvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDYcvDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGK 546
Cdd:cd05932 342 --------DGEILVRSPALMMGYYKDPEATAEAF--TADG--FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAP 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 547 VEAALKNCPLIDNICAFAkSDQSYVISFVVPNQ--KKLTLLAQQKGVEGSwvdicnnpameaeiLKEIREAANAmKLERF 624
Cdd:cd05932 410 IENKLAEHDRVEMVCVIG-SGLPAPLALVVLSEeaRLRADAFARAELEAS--------------LRAHLARVNS-TLDSH 473
|
570 580 590
....*....|....*....|....*....|....*
gi 75992927 625 EIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHY 659
Cdd:cd05932 474 EQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
230-579 |
1.56e-53 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 187.11 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI---GYSSPLT 306
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LSDqssKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQIK-KGYDAPlcnlilfk 385
Cdd:cd04433 80 ALE---LIER--------EKVTILLGVPTLLARL--------------------------LKAPEsAGYDLS-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 386 kvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwQE 463
Cdd:cd04433 115 --------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPVPGVEVRIVD-PD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 464 GGytvHDKPNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVS 543
Cdd:cd04433 186 GG---ELPPGEIGELVVRGPSVMKGYWNNPEATAA---VDEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVY 256
|
330 340 350
....*....|....*....|....*....|....*....
gi 75992927 544 LGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 579
Cdd:cd04433 257 PAEVEAVLLGHPGVAEAAVVGVPDPEWgerVVAVVVLRP 295
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
85-567 |
3.43e-52 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 187.42 E-value: 3.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsKLKAALVDINCVKHIIYVDNKtinrAEYPEGLEihsmQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:cd05911 91 DGLE-KVKEAAKELGPKDKIIVLDDK----PDGVLSIE----DLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVleltaeiscftYGCRIGYSSPLtlsdqsskikkgsKGdCT 323
Cdd:cd05911 162 KGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHI-----------YGLFTTLASLL-------------NG-AT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 324 VLkptlmaavpeIMDRIYKNVMskvqeMNYVQKtlfkigydYKleqIKKGYDAPLCNLILFK---KVKALLGgNVRMMLS 400
Cdd:cd05911 217 VI----------IMPKFDSELF-----LDLIEK--------YK---ITFLYLVPPIAAALAKsplLDKYDLS-SLRVILS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 401 GGAPLSPQTHRFMNVCFC-CPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvhdKPNPRGEIV 479
Cdd:cd05911 270 GGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSL---GPNEPGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 480 IGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDN 559
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKE--TFDEDG--WLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHPGVAD 421
|
....*...
gi 75992927 560 ICAFAKSD 567
Cdd:cd05911 422 AAVIGIPD 429
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
37-555 |
6.22e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 187.70 E-value: 6.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 37 TLDKLFDHAVAKFGKKdslgtrEILSEEnemqpnGKVFkklilgnykwiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFC 116
Cdd:PRK06187 7 TIGRILRHGARKHPDK------EAVYFD------GRRT-----------TYAELDERVNRLANALRALGVKKGDRVAVFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 117 ETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESkLKAALVDINCVKHIIYVDnktinraE 196
Cdd:PRK06187 64 WNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPL-LAAILPQLPTVRTVIVEG-------D 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 197 YPEGLEIHSMQSVEE-LGAKPENLSVPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYI 275
Cdd:PRK06187 136 GPAAPLAPEVGEYEElLAAASDTFDFPD--IDENDAAAMLYTSGTTGHPKGVVLSHRNLFL-HSLAVCAWLKLSRDDVYL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 276 GYLPLAHVLELTAEISCFTYGCRIGYS---SPLTLSDQsskIKKgskgdctvLKPTLMAAVPEIMdriyknvmskvqemN 352
Cdd:PRK06187 213 VIVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPTIW--------------Q 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 353 YVQKTLFKIGYDYkleqikkgydaplcnlilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESC 431
Cdd:PRK06187 268 MLLKAPRAYFVDF---------------------------SSLRLVIYGGAALPPALlREFKEK-FGIDLVQGYGMTETS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 432 GAGTVTEVTDYTTGR------VGAPLICCEIKLKD--WQE---GGYTVhdkpnprGEIVIGGQNISMGYFKNEEKTAEDY 500
Cdd:PRK06187 320 PVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVDddGDElppDGGEV-------GEIIVRGPWLMQGYWNRPEATAETI 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 501 cvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCP 555
Cdd:PRK06187 393 ---DGG--WLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELEDALYGHP 441
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
38-645 |
2.09e-51 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 187.66 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 38 LDKLFDHAVAKFGKKDSLGTREilSEENEMQPNGKVFKKLiLGNYKWINYLEVNCRVNNFGSGL-TALGLKPKNTIAIFC 116
Cdd:cd17632 24 LAQIIATVMTGYADRPALGQRA--TELVTDPATGRTTLRL-LPRFETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 117 ETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESKLKAALvDINCVKHIIYVDNK---TIN 193
Cdd:cd17632 101 FTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVL-EGGTPPRLVVFDHRpevDAH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 194 R----------AEYPEGLEIHSMQSVEELGAKPenlsVPPSRPTPSDMAIVM--YTSGSTGRPKGVMMHHSNLIAGMTGQ 261
Cdd:cd17632 180 RaalesarerlAAVGIPVTTLTLIAVRGRDLPP----APLFRPEPDDDPLALliYTSGSTGTPKGAMYTERLVATFWLKV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 262 CERIPGLGPKDTYIGYLPLAHVLeltAEISCFTYGCRIGYSSPLTLSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIY 341
Cdd:cd17632 256 SSIQDIRPPASITLNFMPMSHIA---GRISLYGTLARGGTAYFAAASDMSTLFD-----DLALVRPTELFLVPRVCDMLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 342 KNVMSKVqemnyvqktlfkigyDYKLEQikkGYDAplcnLILFKKVKA-----LLGGNVRMMLSGGAPLSPQTHRFMNVC 416
Cdd:cd17632 328 QRYQAEL---------------DRRSVA---GADA----ETLAERVKAelrerVLGGRLLAAVCGSAPLSAEMKAFMESL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 417 FCCPIGQGYGLTEscgAGTVT--------EVTDYttgrvgaplicceiKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMG 488
Cdd:cd17632 386 LDLDLHDGYGSTE---AGAVIldgvivrpPVLDY--------------KLVDVPELGYFRTDRPHPRGELLVKTDTLFPG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 489 YFKNEEKTAEDYcvDENGqrWFCTGDI-GEFHPDGcLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:cd17632 449 YYKRPEVTAEVF--DEDG--FYRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSE 523
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 568 QSYVISFVVPNQKKLTLLAQQkgvegswvdicnnpAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVT 645
Cdd:cd17632 524 RAYLLAVVVPTQDALAGEDTA--------------RLRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
85-652 |
4.90e-51 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 183.80 E-value: 4.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSv 164
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrpTPSDMAIVMYTSGSTGRP 244
Cdd:cd05914 87 --------------------------------------------------------------DEDDVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVLELtaeisCFTYGCRIGYSSPLTLSDQ--SSKIKKGSKGDc 322
Cdd:cd05914 105 KGVMLTYRNIVSNVDG-VKEVVLLGKGDKILSILPLHHIYPL-----TFTLLLPLLNGAHVVFLDKipSAKIIALAFAQ- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 323 tvLKPTLMAAVPEIMDRIYKNVmskVQEMNYVQKTLFKIGYDYKLEQIKKgydaplcnlILFKKVKALLGGNVRMMLSGG 402
Cdd:cd05914 178 --VTPTLGVPVPLVIEKIFKMD---IIPKLTLKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 403 APLSPQTHRF---MNVCFCcpigQGYGLTES----CGAGTVTEVTDyttgRVGAPLICCEIKLkdwqeggytvhDKPNPR 475
Cdd:cd05914 244 AKINPDVEEFlrtIGFPYT----IGYGMTETapiiSYSPPNRIRLG----SAGKVIDGVEVRI-----------DSPDPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 476 ---GEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALK 552
Cdd:cd05914 305 tgeGEIIVRGPNVMKGYYKNPEATAE--AFDKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKIN 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 553 NCPLIdnicafaksdqsyVISFVVPNQKKLTLLA-------QQKGVegswvdicNNPAMEAEILKEIREAANaMKLERFE 625
Cdd:cd05914 381 NMPFV-------------LESLVVVQEKKLVALAyidpdflDVKAL--------KQRNIIDAIKWEVRDKVN-QKVPNYK 438
|
570 580
....*....|....*....|....*..
gi 75992927 626 IPIKVRLSPEPWtPETGLvtdaFKLKR 652
Cdd:cd05914 439 KISKVKIVKEEF-EKTPK----GKIKR 460
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
80-667 |
2.03e-46 |
|
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: 173.70 E-value: 2.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKW--INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAA-QTCFKYNFpLVTLYATLGREAVVHGLNESE 156
Cdd:cd05933 2 RGDKWhtLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAvGAIFAGGI-AVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 157 ASYLITSVELLESKLKAALVDINCVKHIIyvdnktINRAEYPEGL-EIHSMQSVEELGakpenLSVPP-------SRPTP 228
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAII------QYKEPLKEKEpNLYSWDEFMELG-----RSIPDeqldaiiSSQKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 229 SDMAIVMYTSGSTGRPKGVMMHHSNL--IAGMTGQ-CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSP 304
Cdd:cd05933 150 NQCCTLIYTSGTTGMPKGVMLSHDNItwTAKAASQhMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFAQP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 305 LTLsdqsskikKGSKGDcTV--LKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLF----KIGYDYKLEQIKKGYDAPL 378
Cdd:cd05933 230 DAL--------KGTLVK-TLreVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLMGGESPSPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 379 C----NLILFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVGAP 450
Cdd:cd05933 301 FyrlaKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAYRLLSCGKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 451 LICCEIKLkdwqeggytvhDKPNPR--GEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIID 528
Cdd:cd05933 377 LPGCKTKI-----------HNPDADgiGEICFWGRHVFMGYLNMEDKTEE--AIDEDG--WLHSGDLGKLDEDGFLYITG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 529 RKKDLVKLQAGEYVSLGKVEAALKN-CPLIDNicAFAKSDQSYVISFVVP-----NQK------KLTLLA----QQKGVE 592
Cdd:cd05933 442 RIKELIITAGGENVPPVPIEDAVKKeLPIISN--AMLIGDKRKFLSMLLTlkcevNPEtgepldELTEEAiefcRKLGSQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 593 GSWVDICNN---PAMEAEILKEIREA-----ANAMKLERFEIpikvrlSPEPWTPETGLVTDAFKLKRKELKNHYLKDIE 664
Cdd:cd05933 520 ATRVSEIAGgkdPKVYEAIEEGIKRVnkkaiSNAQKIQKWVI------LEKDFSVPGGELGPTMKLKRPVVAKKYKDEID 593
|
...
gi 75992927 665 RMY 667
Cdd:cd05933 594 KLY 596
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
83-534 |
1.15e-42 |
|
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: 160.42 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 83 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLIT 162
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 163 SVELlesklkaalvdincvkhiiyvdnktinraeypegleihsmqsvEELGAKPENLSVPPSRpTPSDMAIVMYTSGSTG 242
Cdd:cd05936 103 AVSF-------------------------------------------TDLLAAGAPLGERVAL-TPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 243 RPKGVMMHHSNLIAGMTgQCERI--PGLGPKDTYIGYLPLAHVLELTAeisCFTYGCRIGYS-------SPLTLSDQssk 313
Cdd:cd05936 139 VPKGAMLTHRNLVANAL-QIKAWleDLLEGDDVVLAALPLFHVFGLTV---ALLLPLALGATivliprfRPIGVLKE--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 314 IKKGskgdctvlKPTLMAAVPeimdriyknvmskvqemnyvqkTLFkIGydykleqikkgydaplcnLILFKKVKALLGG 393
Cdd:cd05936 212 IRKH--------RVTIFPGVP----------------------TMY-IA------------------LLNAPEFKKRDFS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 394 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKDwqeggytVHDKP 472
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-------DDGEE 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 473 NPR---GEIVIGGQNISMGYFKNEEKTAEDYcVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:cd05936 316 LPPgevGELWVRGPQVMKGYWNRPEETAEAF-VDG----WLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
85-535 |
1.86e-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: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwmiaaqtcfkynFPLVTLyATLGREAVVHGLN----------- 153
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIE------------FPVAFL-AVLSLGAVVTTANplstpaeiakq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 154 --ESEASYLITSVELLEsKLKAALVDINCVkhiiyvdnktinraeypEGLEIHSMQSVEELGAKPENlSVPPSRPTPSDM 231
Cdd:cd05904 100 vkDSGAKLAFTTAELAE-KLASLALPVVLL-----------------DSAEFDSLSFSDLLFEADEA-EPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 232 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERI-PGLGPKDTYIGYLPLAHVLELTAeiscFTYGcrigyssplTLSdq 310
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSS----FALG---------LLR-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 311 sskikkgskgdctvLKPTLMaavpeimdriyknVMSK---VQEMNYVQKtlFKIGYdykleqikkgydAPLCNLILFKKV 387
Cdd:cd05904 226 --------------LGATVV-------------VMPRfdlEELLAAIER--YKVTH------------LPVVPPIVLALV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 388 KALLGGN-----VRMMLSGGAPLSPQT-----HRFMNVcfccPIGQGYGLTESCGAGTVTEVTDYTTGRVG-----APLI 452
Cdd:cd05904 265 KSPIVDKydlssLRQIMSGAAPLGKELieafrAKFPNV----DLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 453 ccEIKLKDWQEGGytvHDKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:cd05904 341 --EAKIVDPETGE---SLPPNQTGELWIRGPSIMKGYLNNPEATAA--TIDKEG--WLHTGDLCYIDEDGYLFIVDRLKE 411
|
...
gi 75992927 533 LVK 535
Cdd:cd05904 412 LIK 414
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
228-542 |
1.74e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 155.26 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCER--IPGLGPKdTYIGYLPLAHVLELTAEISCFTYGCRIgysspl 305
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsiFKKYNPK-THLSYLPISHIYERVIAYLSFMLGGTI------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 306 tlsDQSSK-IKKGSKgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKigydyKLEQIKKG-YDAPLCNLI- 382
Cdd:PTZ00342 376 ---NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVK-----KILSLRKSnNNGGFSKFLe 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 383 ----LFKKVKALLGGNVRMMLSGGAPLSPQTHR----FMNVCFCcpigQGYGLTESCGAGTVTEVTDYTTGRVGAPlIC- 453
Cdd:PTZ00342 447 githISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYGLTETTGPIFVQHADDNNTESIGGP-ISp 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 454 -CEIKLKDWQEggYTVHDKPnPRGEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PTZ00342 522 nTKYKVRTWET--YKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTED----GYFKTGDIVQINKNGSLTFLDRSKG 594
|
330
....*....|
gi 75992927 533 LVKLQAGEYV 542
Cdd:PTZ00342 595 LVKLSQGEYI 604
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
80-657 |
1.01e-38 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 149.77 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAaqtcfkynfplvtLYATLGREAVVHGLN----ES 155
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVA-------------FLAAARAGAVVAPLNpaykKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 156 EASYLitsveLLESKLKAALVDincvkhiiYVDNKTINRAEYPEGLEI----------HSMQSVEELGAKPENLSVPPSR 225
Cdd:cd05926 77 EFEFY-----LADLGSKLVLTP--------KGELGPASRAASKLGLAIlelaldvgvlIRAPSAESLSNLLADKKNAKSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 226 --PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEI--SCFTYGCrigy 301
Cdd:cd05926 144 gvPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNIT-NTYKLTPDDRTLVVMPLFHVHGLVASLlsTLAAGGS---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 302 sspLTLSDQSSkikkGSK--GDCTVLKPTLMAAVPEIMDRIYKNVMSKvqemnyvqktlfkigydykleqikkgydaplc 379
Cdd:cd05926 219 ---VVLPPRFS----ASTfwPDVRDYNATWYTAVPTIHQILLNRPEPN-------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 380 nlilFKKVKALLggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--EVTDYTTGRVGAPLiccEIK 457
Cdd:cd05926 260 ----PESPPPKL----RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPV---GVE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 458 LKDWQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQ 537
Cdd:cd05926 329 VRILDEDGEIL--PPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD----GWFRTGDLGYLDADGYLFLTGRIKELIN-R 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 538 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKltllaqqkgvegswvdicnnPAMEAEILKEIRE 614
Cdd:cd05926 402 GGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLREGA--------------------SVTEEELRAFCRK 461
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 75992927 615 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKN 657
Cdd:cd05926 462 -----HLAAFKVPKKVYFVDElPKTA-TG------KIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
85-534 |
8.60e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 138.88 E-value: 8.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGREAVVHGLNE----SEASY- 159
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAA-------------LGALKAGAVVVPLNTrytaDEAAYi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 -------LITSVELLESKLKAALVDINCVKHIIYVDNktinRAEYPEGLEIHSMQSVEELGAKPEnlsVPPSRpTPSDMA 232
Cdd:PRK07656 98 largdakALFVLGLFLGVDYSATTRLPALEHVVICET----EEDDPHTEKMKTFTDFLAAGDPAE---RAPEV-DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 233 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGcrigysspltlsdqs 311
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKAGVnAPLMRG--------------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 312 skikkgskgdCTVLkPTLMAAVPEIMDRIYK---NVMSKVQEMnyvqktlfkigYDYkLEQIKKGYDAPLCNLilfkkvk 388
Cdd:PRK07656 234 ----------ATIL-PLPVFDPDEVFRLIETeriTVLPGPPTM-----------YNS-LLQHPDRSAEDLSSL------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 389 allggnvRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD---YTTGRVGAPLICCEIKLKDWQEG 464
Cdd:PRK07656 284 -------RLAVTGAASMPVAlLERFESELGVDIVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVNELGE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 465 GYTVHDKpnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK07656 357 EVPVGEV----GELLVRGPNVMKGYYDDPEATAA--AIDADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
77-576 |
2.37e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 137.02 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 77 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESE 156
Cdd:PRK03640 21 IEFEEKKV-TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 157 ASYLITSvellesklkaalvdincvkhiiyvdnktinrAEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTPSDMAIVMY 236
Cdd:PRK03640 100 VKCLITD-------------------------------DDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 237 TSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLSDQ--SSKI 314
Cdd:PRK03640 149 TSGTTGKPKGVIQTYGNHWWSAVGSALNL-GLTEDDCWLAAVPIFHISGLSILMRSVIYGMRV------VLVEKfdAEKI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 315 KKGSKGDctvlKPTLMAAVPEIMDRIyknvMSKVQEMNYvqktlfkigydykleqikkgydaplcnlilfkkvkallGGN 394
Cdd:PRK03640 222 NKLLQTG----GVTIISVVSTMLQRL----LERLGEGTY--------------------------------------PSS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 395 VRMMLSGGAPLSPQT------HRFmnvcfccPIGQGYGLTESCgAGTVTEVTDYTT---GRVGAPLICCEIKL-KDWQEG 464
Cdd:PRK03640 256 FRCMLLGGGPAPKPLleqckeKGI-------PVYQSYGMTETA-SQIVTLSPEDALtklGSAGKPLFPCELKIeKDGVVV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 465 gytvhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSL 544
Cdd:PRK03640 328 ------PPFEEGEIVVKGPNVTKGYLNREDATRE---TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYP 395
|
490 500 510
....*....|....*....|....*....|....*
gi 75992927 545 GKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 576
Cdd:PRK03640 396 AEIEEVLLSHPGVAEAGVVGVPDDKWgqvPVAFVV 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
87-577 |
5.28e-33 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 132.12 E-value: 5.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 87 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsvel 166
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 167 lesklkaalvdincvkhiiyvdnktinraeyPEGLEIHSMQsveelgakpenlsvppsrPTPSDMAIVMYTSGSTGRPKG 246
Cdd:cd05903 80 -------------------------------PERFRQFDPA------------------AMPDAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 247 VMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaeISCFTYGcrigysspltlsdqsskikkgskgdctVLK 326
Cdd:cd05903 111 VMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAH-------QTGFVYG---------------------------FTL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 327 PTLMAAvPEIMDRIYkNVMSKVQEMNyVQKTLFKIGYDYKLEQIKKGYD---APLCNLilfkkvkallggnvRMMLSGGA 403
Cdd:cd05903 156 PLLLGA-PVVLQDIW-DPDKALALMR-EHGVTFMMGATPFLTDLLNAVEeagEPLSRL--------------RTFVCGGA 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 404 PLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD-----YTTGRVGAPLiccEIKLKDwqEGGYTVhdKPNPRGEI 478
Cdd:cd05903 219 TVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrlYTDGRPLPGV---EIKVVD--DTGATL--APGVEGEL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 479 VIGGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLID 558
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAA-----PEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVI 365
|
490 500
....*....|....*....|..
gi 75992927 559 NICAFAKSDQ---SYVISFVVP 577
Cdd:cd05903 366 EAAVVALPDErlgERACAVVVT 387
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
85-567 |
3.34e-31 |
|
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: 127.98 E-value: 3.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIA------AQTCFKYNFPLvtlyatLGREAVVHGLNESEAS 158
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAmfgaalAGGVFVPINPL------LKAEQVAHILADCNVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 159 YLITSVELLEsKLKAALVDINCVKHIIYVDNKTINRAEYPeGLEIHSMQSVEELGAkpenlSVPPSRPTPSDMAIVMYTS 238
Cdd:TIGR03098 100 LLVTSSERLD-LLHPALPGCHDLRTLIIVGDPAHASEGHP-GEEPASWPKLLALGD-----ADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 239 GSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGs 318
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATYLE-NRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDVLKALEKH- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 319 kgdctvlKPTLMAAVPEImdriyknvmskvqemnYVQktLFKIgyDYKLEqikkgyDAPLCNLIlfkkvkALLGGNV-RM 397
Cdd:TIGR03098 251 -------GITGLAAVPPL----------------WAQ--LAQL--DWPES------AAPSLRYL------TNSGGAMpRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 398 MLSGGAPLSPQTHRFMNvcfccpigqgYGLTESCGAGTV-TEVTDYTTGRVGAPLICCEIklkdwqeggYTVHDK----- 471
Cdd:TIGR03098 292 TLSRLRSFLPNARLFLM----------YGLTEAFRSTYLpPEEVDRRPDSIGKAIPNAEV---------LVLREDgseca 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 472 PNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGQR-----------WfcTGDIGEFHPDGCLQIIDRKKDLVKlQAGE 540
Cdd:TIGR03098 353 PGEEGELVHRGALVAMGYWNDPEKTAE--RFRPLPPFpgelhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIK-TSGY 427
|
490 500
....*....|....*....|....*..
gi 75992927 541 YVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:TIGR03098 428 RVSPTEVEEVAYATGLVAEAVAFGVPD 454
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
87-551 |
8.42e-31 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 125.80 E-value: 8.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 87 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLItsvel 166
Cdd:cd17631 23 YAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 167 lesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptpSDMAIVMYTSGSTGRPKG 246
Cdd:cd17631 98 --------------------------------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 247 VMMHHSNL-----IAGMTGqceripGLGPKDTYIGYLPLAHVleltAEISCFTygcrigysSPLTLSDQSSKIKKGSKGD 321
Cdd:cd17631 116 AMLTHRNLlwnavNALAAL------DLGPDDVLLVVAPLFHI----GGLGVFT--------LPTLLRGGTVVILRKFDPE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 322 cTVL------KPTLMAAVPEIMDRIyknvmskvqemnyVQKTLFKigydykleqikkGYDAPlcnlilfkkvkallggNV 395
Cdd:cd17631 178 -TVLdlierhRVTSFFLVPTMIQAL-------------LQHPRFA------------TTDLS----------------SL 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 396 RMMLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEVTDYTT--GRVGAPLICCEIKLKDwqEGGYTVhdKPN 473
Cdd:cd17631 216 RAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD--PDGREV--PPG 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 474 PRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 551
Cdd:cd17631 291 EVGEIVVRGPHVMAGYWNRPEATAAAF---RDG--WFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVL 362
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
229-580 |
2.25e-29 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 120.91 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLS 308
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNL-GLTEDDNWLCALPLFHISGLSILMRSVIYGMTV------YLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 309 DQ--SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQIKKGYDAplcnlilfkk 386
Cdd:cd05912 150 DKfdAEQVLHLINSG----KVTIISVVPTMLQRL--------------------------LEILGEGYPN---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 387 vkallggNVRMMLSGGAPLSPQThrfMNVC--FCCPIGQGYGLTESCgAGTVTEVTDYT---TGRVGAPLICCEIKLKDW 461
Cdd:cd05912 190 -------NLRCILLGGGPAPKPL---LEQCkeKGIPVYQSYGMTETC-SQIVTLSPEDAlnkIGSAGKPLFPVELKIEDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 462 QEGGYTVhdkpnprGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEY 541
Cdd:cd05912 259 GQPPYEV-------GEILLKGPNVTKGYLNRPDATEE---SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGEN 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 75992927 542 VSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQK 580
Cdd:cd05912 326 IYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvPVAFVVSERP 367
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
81-557 |
2.89e-29 |
|
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: 122.64 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 81 NYKWINYLEVNCRVnnfGSGLTALGLKPKNTIAIFCETRAEW---MIAAQTCFKYNFPLVTLYATlgREaVVHGLNESEA 157
Cdd:cd17642 44 NYSYAEYLEMSVRL---AEALKKYGLKQNDRIAVCSENSLQFflpVIAGLFIGVGVAPTNDIYNE--RE-LDHSLNISKP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 158 SYLITSVELLESKLKAAlVDINCVKHIIYVDNKTinraEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTPSDMAIVMYT 237
Cdd:cd17642 118 TIVFCSKKGLQKVLNVQ-KKLKIIKTIIILDSKE----DYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 238 SGSTGRPKGVMMHHSNLIAGMTGQCERIPG--LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGY----SSPLTLSD-Q 310
Cdd:cd17642 193 SGSTGLPKGVQLTHKNIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykfEEELFLRSlQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 311 SSKIKKgskgdcTVLKPTLMAAVPeimdriyknvmskvqemnyvqktlfkigydyKLEQIKKgYDapLCNLIlfkkvkal 390
Cdd:cd17642 273 DYKVQS------ALLVPTLFAFFA-------------------------------KSTLVDK-YD--LSNLH-------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 391 lggnvrMMLSGGAPLSPQTHRFMNVCFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTvh 469
Cdd:cd17642 305 ------EIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTL-- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 470 dKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEA 549
Cdd:cd17642 377 -GPNERGELCVKGPMIMKGYVNNPEATKA--LIDKDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GYQVPPAELES 450
|
....*...
gi 75992927 550 ALKNCPLI 557
Cdd:cd17642 451 ILLQHPKI 458
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
221-559 |
1.63e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 117.41 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 221 VPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA-GMTGQCeRIPGLGPKD-TYIGYLPLAHVLELTAeisCFTYGCR 298
Cdd:PRK05605 211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKA-WVPGLGDGPeRVLAALPMFHAYGLTL---CLTLAVS 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IG--------YSSPLTLsdqsSKIKKGskgdctvlKPTLMAAVPEimdrIYKNVMSKVQEmnyvqktlfkigydykleqi 370
Cdd:PRK05605 287 IGgelvllpaPDIDLIL----DAMKKH--------PPTWLPGVPP----LYEKIAEAAEE-------------------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 371 kKGYDaplcnlilfkkvkalLGGnVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY-TTGRVGA 449
Cdd:PRK05605 331 -RGVD---------------LSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDrRPGYVGV 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 450 PLICCEIKLKDWQEGGYTVHDkpNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDR 529
Cdd:PRK05605 394 PFPDTEVRIVDPEDPDETMPD--GEEGELLVRGPQVFKGYWNRPEETAK---SFLDG--WFRTGDVVVMEEDGFIRIVDR 466
|
330 340 350
....*....|....*....|....*....|
gi 75992927 530 KKDLVkLQAGEYVSLGKVEAALKNCPLIDN 559
Cdd:PRK05605 467 IKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
85-660 |
1.99e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 117.13 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLE--------SKLKAALVDINCVKHIIYVDNkTINRAEYPEGLEIHsmqsvEELGAKPENLsvpPSRPTPS-DMAIVM 235
Cdd:COG0365 120 GGLRggkvidlkEKVDEALEELPSLEHVIVVGR-TGADVPMEGDLDWD-----ELLAAASAEF---EPEPTDAdDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 236 YTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY-----IG---------YLPLAHvleltaEISCFTYGCRIGY 301
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFwctadIGwatghsyivYGPLLN------GATVVLYEGRPDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 302 SSPLTLSDQSSKikkgskgdctvLKPTLMAAVPeimdRIYKNVMskvqemnyvqktlfKIGydyklEQIKKGYDapLCNL 381
Cdd:COG0365 265 PDPGRLWELIEK-----------YGVTVFFTAP----TAIRALM--------------KAG-----DEPLKKYD--LSSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 382 ilfkkvkallggnvRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGA-GTVTEVTDYTTGRVGAPLICCEIKLk 459
Cdd:COG0365 309 --------------RLLGSAGEPLNPEVwEWWYEA-VGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAV- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 460 dWQEGGYTVhdKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLq 537
Cdd:COG0365 373 -VDEDGNPV--PPGEEGELVIKGPWPGMfrGYWNDPERYRETYFGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINV- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 538 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNqkkltllaqqKGVEGSwvdicnnPAMEAEILKEIRE 614
Cdd:COG0365 447 SGHRIGTAEIESALVSHPAVAEAAVVGVPDEirgQVVKAFVVLK----------PGVEPS-------DELAKELQAHVRE 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 75992927 615 aanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKNHYL 660
Cdd:COG0365 510 -----ELGPYAYPREIEFVDElPKTR-SG------KIMRRLLRKIAE 544
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
87-562 |
8.44e-27 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 113.13 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 87 YLEVNCRVNNFGSGL-TALGLKPKNTIAIFCEtRAEWMIAAQ-TCFK----YnFPLVTLYATLGREAVvhgLNESEASYL 160
Cdd:TIGR01733 2 YRELDERANRLARHLrAAGGVGPGDRVAVLLE-RSAELVVAIlAVLKagaaY-VPLDPAYPAERLAFI---LEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ITSVELLESKLKAALVDINCVkhiiyvdnktinraeypegleihsmQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGS 240
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLD-------------------------PLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 241 TGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAH---VLELTAeiscftygcrigyssPLTLsdqsskikkg 317
Cdd:TIGR01733 132 TGRPKGVVVTHRSLVN-LLAWLARRYGLDPDDRVLQFASLSFdasVEEIFG---------------ALLA---------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 318 skGDCTVLKPTLMAAVPEIMDRIYKNVMsKVQEMNYVqKTLFKigydykleqikkgydaplcnliLFKKVKALLGGNVRM 397
Cdd:TIGR01733 186 --GATLVVPPEDEERDDAALLAALIAEH-PVTVLNLT-PSLLA----------------------LLAAALPPALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 398 MLSGGAPLSPQTH-RFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIKLKDwqeggytVHDK 471
Cdd:TIGR01733 240 VILGGEALTPALVdRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRLYVLD-------DDLR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 472 PNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 544
Cdd:TIGR01733 313 PVPVgvvGELYIGGPGVARGYLNRPELTAERFVPDpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYRIEL 391
|
490
....*....|....*...
gi 75992927 545 GKVEAALKNCPLIDNICA 562
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
227-588 |
9.09e-27 |
|
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: 113.88 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPkdtyigylplahvleltaeiscftyGCRIGYSSPLT 306
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGP-------------------------GDVFLNQAPFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LsdqsskikkgskgDCTV--LKPTLMA-----AVPEIMDRIYKNVMSKVQEMnyvqktlfkigydykleQIKKGYDAP-- 377
Cdd:cd05945 149 F-------------DLSVmdLYPALASgatlvPVPRDATADPKQLFRFLAEH-----------------GITVWVSTPsf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 378 --LCnlILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVT-----DYTTGRVGA 449
Cdd:cd05945 199 aaMC--LLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTpevldGYDRLPIGY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 450 PLICCEIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdYCVDENGQRWFCTGDIGEFHPDGCLQIIDR 529
Cdd:cd05945 277 AKPGAKLVILD--EDGRPV--PPGEKGELVISGPSVSKGYLNNPEKTAA-AFFPDEGQRAYRTGDLVRLEADGLLFYRGR 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992927 530 KKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP----NQKKLTLLAQQ 588
Cdd:cd05945 352 LDFQVKLN-GYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVtelIAFVVPkpgaEAGLTKAIKAE 416
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
230-568 |
1.13e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 113.16 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIgysspl 305
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRF-GLGEDDVYLTVLPLFHinaqAVSVLAALSV---GATL------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 306 tlsdqsskikkgskgdctVLKPTLMAAvpeimdriykNVMSKVQE-----MNYVQKTLfkigyDYKLEQIKKGYDAplcn 380
Cdd:cd05934 152 ------------------VLLPRFSAS----------RFWSDVRRygatvTNYLGAML-----SYLLAQPPSPDDR---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 381 lilfkkvkallGGNVRmmLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKD 460
Cdd:cd05934 195 -----------AHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 461 wqeggytVHDKPNPR---GEIVI---GGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:cd05934 262 -------DDGQELPAgepGELVIrglRGWGFFKGYYNMPEATAE---AMRNG--WFHTGDLGYRDADGFFYFVDRKKDMI 329
|
330 340 350
....*....|....*....|....*....|....
gi 75992927 535 KlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:cd05934 330 R-RRGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
85-588 |
2.62e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 115.34 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCEtRAEWMIAAqtcfkynfplvtLYATL--G-----------REAVVHG 151
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLE-RSLEMVVA------------LLAVLkaGaayvpldpaypAERLAYM 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 152 LNESEASYLITsvellESKLKAALVDINCvkHIIYVDNKTInrAEYPEgleihsmqsveelgakpenlSVPPSRPTPSDM 231
Cdd:COG1020 569 LEDAGARLVLT-----QSALAARLPELGV--PVLALDALAL--AAEPA--------------------TNPPVPVTPDDL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 232 AIVMYTSGSTGRPKGVMMHH---SNLIAGMTGQCeripGLGPKDTYIGYLPLAH---VLELtaeISCFTYGCRIGYSSPL 305
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMVEHralVNLLAWMQRRY----GLGPGDRVLQFASLSFdasVWEI---FGALLSGATLVLAPPE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 306 TLSD--------QSSKIkkgskgdcTVLK--PTLMAAVPEimdriyknvmskvqemnyvqktlfkigydykleqikkgYD 375
Cdd:COG1020 693 ARRDpaalaellARHRV--------TVLNltPSLLRALLD--------------------------------------AA 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 376 APLCnlilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAP 450
Cdd:COG1020 727 PEAL-------------PSLRLVLVGGEALPPELvRRWRARLPGARLVNLYGPTETTVDSTYYEVTppDADGGSVpiGRP 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 451 LicceiklkdwqeGGYTV-----HDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFH 519
Cdd:COG1020 794 I------------ANTRVyvldaHLQPVPvgvPGELYIGGAGLARGYLNRPELTAERFVADpfgFPGARLYRTGDLARWL 861
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992927 520 PDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKKLTLLAQQ 588
Cdd:COG1020 862 PDGNLEFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAREDAPgdkRLVAYVVPEAGAAAAAALL 932
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
142-569 |
2.89e-26 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 112.81 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 142 TLGREAVVHGLNESEASYLITSVELLEsKLKAA-LVDINCVKHIIYVDN--KTINRAEYPEGLeIHSMQSVEELgakpen 218
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQFIE-KLKLHhLFDVEYDARIVYLEDlrAKISKADKCKAF-LAGKFPPKWL------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 219 LSVPPSRPT-PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELT-AEISCFTYG 296
Cdd:cd05909 136 LRIFGVAPVqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 297 CRIG-YSSPLTLSDQSSKIKKGSkgdCTVL--KPTLMaavpeimdRIYknvmskvqeMNYVQKTLFKigydykleqikkg 373
Cdd:cd05909 215 IKVVfHPNPLDYKKIPELIYDKK---ATILlgTPTFL--------RGY---------ARAAHPEDFS------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 374 ydaplcnlilfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV-TEVTDYTTGRVGAPLI 452
Cdd:cd05909 262 --------------------SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 453 CCEIKLKDwQEGGytvhdKPNPRGE---IVIGGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQIIDR 529
Cdd:cd05909 322 GMEVKIVS-VETH-----EEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF-----GDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 75992927 530 KKDLVKLqAGEYVSLGKVE-AALKNCPLIDNICAFAKSDQS 569
Cdd:cd05909 391 LSRFAKI-AGEMVSLEAIEdILSEILPEDNEVAVVSVPDGR 430
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
86-555 |
2.98e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 113.11 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 86 NYLEVNCRVNNFGSGLTALGLKPKNTIAIFCetraeWmiaaqTCFKYnfpLVTLYATLGREAVVHGLN------------ 153
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLA-----W-----NTHRH---LELYYAVPGMGAVLHTINprlfpeqiayii 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 154 -ESEASYLITSVELLeSKLKAALVDINCVKHIIYVDNKTINRAEYPEGLE-----IHSMQSVEELGAKPENlsvppsrpt 227
Cdd:cd12119 94 nHAEDRVVFVDRDFL-PLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLayeelLAAESPEYDWPDFDEN--------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 psDMAIVMYTSGSTGRPKGVMM-HHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLT 306
Cdd:cd12119 164 --TAAAICYTSGTTGNPKGVVYsHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LSDQSSKIKKGSKgdctvlkPTLMAAVPEImdriYKNVMSKVQEMNYVQKTLfkigydykleqikkgydaplcnlilfkk 386
Cdd:cd12119 242 DPASLAELIEREG-------VTFAAGVPTV----WQGLLDHLEANGRDLSSL---------------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 387 vkallggnvRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTESCGAGTVTEVTDY--------------TTGRVgA 449
Cdd:cd12119 283 ---------RRVVIGGSAVPRsliEAFEERGV----RVIHAWGMTETSPLGTVARPPSEhsnlsedeqlalraKQGRP-V 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 450 PLIccEIKLKDwQEGGYTVHDkPNPRGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDR 529
Cdd:cd12119 349 PGV--ELRIVD-DDGRELPWD-GKAVGELQVRGPWVTKSYYKNDEESEA---LTEDG--WLRTGDVATIDEDGYLTITDR 419
|
490 500
....*....|....*....|....*.
gi 75992927 530 KKDLVKlQAGEYVSLGKVEAALKNCP 555
Cdd:cd12119 420 SKDVIK-SGGEWISSVELENAIMAHP 444
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
230-635 |
6.92e-26 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 111.23 E-value: 6.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIP---GLGPKDTYIGYLPLAHVLELTAEISCFTYgCRigySSPLT 306
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAA----NVRALVdawRWTEDDVLLHVLPLHHVHGLVNALLCPLF-AG---ASVEF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LSDQSSKIKKGSKGDCTVlkpTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKigydykleqikkgydaplcnlilfkk 386
Cdd:cd05941 162 LPKFDPKEVAISRLMPSI---TVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAE-------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 387 vkallggNVRMMLSGGAPLSPQTHRFmnvcFCCPIGQG----YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQ 462
Cdd:cd05941 213 -------RLRLMVSGSAALPVPTLEE----WEAITGHTllerYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVD-E 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 463 EGGytvhdKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVDengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAG 539
Cdd:cd05941 281 ETG-----EPLPRgevGEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGVVDEDGYYWILGRSSVDIIKSGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 540 EYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkkltllaqQKGVegswvdicnnPAMEAEILKEireaA 616
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVL----------RAGA----------AALSLEELKE----W 407
|
410
....*....|....*....
gi 75992927 617 NAMKLERFEIPIKVRLSPE 635
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDE 426
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
227-579 |
2.06e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 109.54 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI------G 300
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLvvlpeeV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 301 YSSPLTLSD--QSSKIkkgskgdcTVLK--PTLMAAVpeimdriyknvmskvqeMNYVQKTLFKigydykleqikkgyda 376
Cdd:cd05930 170 RKDPEALADllAEEGI--------TVLHltPSLLRLL-----------------LQELELAALP---------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 377 plcnlilfkkvkallggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPL 451
Cdd:cd05930 209 -----------------SLRLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATYYRVPpdDEEDGRVpiGRPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 452 ICCEIklkdwqeggYTVHDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCL 524
Cdd:cd05930 272 PNTRV---------YVLDENLRPVppgvpGELYIGGAGLARGYLNRPELTAERFVPNpfGPGERMYRTGDLVRWLPDGNL 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 525 QIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 579
Cdd:cd05930 343 EFLGRIDDQVKI-RGYRIELGEIEAALLAHPGVREAAVVAREDgdgEKRLVAYVVPDE 399
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
85-578 |
5.19e-25 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 108.95 E-value: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 164
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ellESKLKAALVDIncvKHIIYVDNKTInrAEYPEgleihsmqsveelgakpENLSvPPSRPtpSDMAIVMYTSGSTGRP 244
Cdd:cd17655 101 ---QSHLQPPIAFI---GLIDLLDEDTI--YHEES-----------------ENLE-PVSKS--DDLAYVIYTSGSTGKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTLSDQSSKIKKGSKGDctv 324
Cdd:cd17655 153 KGVMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIS--FDASVT-EIFA---------SLLSGNTLYIVRKETVLD--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 lkptlmaaVPEIMDRIYKNVMSKVqemnyvqktlfkigydykleqikkgyDAPLCNLILFKKVKALLGGNVRMMLSGGAP 404
Cdd:cd17655 217 --------GQALTQYIRQNRITII--------------------------DLTPAHLKLLDAADDSEGLSLKHLIVGGEA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 405 LSPQT-----HRFMNvcfCCPIGQGYGLTESC-GAGT-VTEVTDYTTGRV--GAPLICCEIKLKDwQEGgytvhdKPNP- 474
Cdd:cd17655 263 LSTELakkiiELFGT---NPTITNAYGPTETTvDASIyQYEPETDQQVSVpiGKPLGNTRIYILD-QYG------RPQPv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 475 --RGEIVIGGQNISMGYFKNEEKTAEDYCVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAA 550
Cdd:cd17655 333 gvAGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR-GYRIELGEIEAR 411
|
490 500 510
....*....|....*....|....*....|.
gi 75992927 551 LKNCPLIDNICAFAKSDQS---YVISFVVPN 578
Cdd:cd17655 412 LLQHPDIKEAVVIARKDEQgqnYLCAYIVSE 442
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
160-534 |
5.74e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.39 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 LITSVELLESKLKAALVDiNCVKHIiyvdNKTINRAEYPEGLEIHSMQSveelgaKPENLSVPPSRPTPSDMAIVMYTSG 239
Cdd:PRK05677 149 IVTEVADMLPPLKRLLIN-AVVKHV----KKMVPAYHLPQAVKFNDALA------KGAGQPVTEANPQADDVAVLQYTGG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 240 STGRPKGVMMHHSNLIAGMTgQCERIPG--LGP-KDTYIGYLPLAHvleltaeISCFTYGCRIgysspLTLSdqsskikk 316
Cdd:PRK05677 218 TTGVAKGAMLTHRNLVANML-QCRALMGsnLNEgCEILIAPLPLYH-------IYAFTFHCMA-----MMLI-------- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 317 gskGDCTVLKPTlmaavPEIMDRIYKnVMSKVQEMNYVQ-KTLFkigydykleqikkgydAPLCNLILFKKV--KALlgg 393
Cdd:PRK05677 277 ---GNHNILISN-----PRDLPAMVK-ELGKWKFSGFVGlNTLF----------------VALCNNEAFRKLdfSAL--- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 394 nvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGGYTVHDKPn 473
Cdd:PRK05677 329 --KLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEV- 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75992927 474 prGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK05677 405 --GELCVKGPQVMKGYWQRPEATDE--ILDSDG--WLKTGDIALIQEDGYMRIVDRKKDMI 459
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
85-568 |
6.04e-24 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 105.25 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELlesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptpSDMAIVMYTSGSTGRP 244
Cdd:cd05935 82 EL--------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCriGYSSPLTLSDQSSKIKKGSKGDCTV 324
Cdd:cd05935 100 KGCMHTHFSAAANALQSA-VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG--GTYVLMARWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LkptlMAAVPEIMDriyknVMSKVQEMNYVQKTLfkigydykleqikkgydaplcnlilfkkvkallggnvRMMLSGGAP 404
Cdd:cd05935 177 W----TNIPTMLVD-----LLATPEFKTRDLSSL-------------------------------------KVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 405 LSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGgytVHDKPNPRGEIVIGGQN 484
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETG---RELPPNEVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 485 ISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFA 564
Cdd:cd05935 288 IFKGYWNRPEETEESF-IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
....
gi 75992927 565 KSDQ 568
Cdd:cd05935 366 VPDE 369
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
230-659 |
1.97e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 101.64 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysSPLTLSD 309
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVGGLAILVRSLLAG------AELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 310 QSSKIKKgskgDCTVLKPTLMAAVPEimdriyknvmskvqemnyvqktlfkigydykleQIKKGYDAPLCNLILFkkvka 389
Cdd:cd17630 74 RNQALAE----DLAPPGVTHVSLVPT---------------------------------QLQRLLDSGQGPAALK----- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 390 llggNVRMMLSGGAPLSPQ-THRFMnvCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytv 468
Cdd:cd17630 112 ----SLRAVLLGGAPIPPElLERAA--DRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 469 hdkpnpRGEIVIGGQNISMGYFKNEEKTAedycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVE 548
Cdd:cd17630 178 ------DGEIWVGGASLAMGYLRGQLVPE----FNEDG--WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 549 AALKNCPLIDNICAFAKSDQSY---VISFVVPnqkkltllaqqkgvegswvdicNNPAMEAEILKEIREaanamKLERFE 625
Cdd:cd17630 245 AALAAHPAVRDAFVVGVPDEELgqrPVAVIVG----------------------RGPADPAELRAWLKD-----KLARFK 297
|
410 420 430
....*....|....*....|....*....|....
gi 75992927 626 IPIkvRLSPEPWTPETGLVtdafKLKRKELKNHY 659
Cdd:cd17630 298 LPK--RIYPVPELPRTGGG----KVDRRALRAWL 325
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
87-584 |
7.54e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 102.90 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 87 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLI----- 161
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 162 --TSVELLESKLKAalvDINCVKHIIYVDNktinraEYPEgleiHSMQSVEELGAKPENLSVPPsrPTPSD-MAIVMYTS 238
Cdd:PRK06087 132 kqTRPVDLILPLQN---QLPQLQQIVGVDK------LAPA----TSSLSLSQIIADYEPLTTAI--TTHGDeLAAVLFTS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 239 GSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRigySSPLTLSDQSSKIKKG 317
Cdd:PRK06087 197 GTEGLPKGVMLTHNNILASERAYCARL-NLTWQDVFMMPAPLGHATGfLHGVTAPFLIGAR---SVLLDIFTPDACLALL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 318 SKGDCTvlkpTLMAAVPEIMDriyknVMSKVQEMNYVQKTLfkigydykleqikkgydaplcnlilfkkvkallggnvRM 397
Cdd:PRK06087 273 EQQRCT----CMLGATPFIYD-----LLNLLEKQPADLSAL-------------------------------------RF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 398 MLSGGAP----LSPQTHRFmNVCFCcpigQGYGLTESCGAGTVT--EVTDYTTGRVGAPLICCEIKLKDwqeggytVHDK 471
Cdd:PRK06087 307 FLCGGTTipkkVARECQQR-GIKLL----SVYGSTESSPHAVVNldDPLSRFMHTDGYAAAGVEIKVVD-------EARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 472 PNPRG---EIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVE 548
Cdd:PRK06087 375 TLPPGcegEEASRGPNVFMGYLDEPELTAR--ALDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVE 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 75992927 549 AALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLTL 584
Cdd:PRK06087 450 DILLQHPKIHDACVVAMPDERLgerSCAYVVLKAPHHSL 488
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
85-577 |
1.25e-22 |
|
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: 101.58 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynfpLVTLYAtlgreavvhGlneseASYLITSV 164
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAV---------LGILAA---------G-----AAYVPVDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLESKLKAALVD--INCVkhiiyvdnktINRAEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGSTG 242
Cdd:cd12114 70 DQPAARREAILADagARLV----------LTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 243 RPKGVMMHH---SNLIAGMTgqcERIpGLGPKDTYIGYLPLAH---VLELTAEIScftygcrIGYSspLTLSDQsskikk 316
Cdd:cd12114 140 TPKGVMISHraaLNTILDIN---RRF-AVGPDDRVLALSSLSFdlsVYDIFGALS-------AGAT--LVLPDE------ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 317 GSKGDCTVLKP-------TLMAAVPEIMDRIyknvmskvqeMNYVQKTlfkigydykleqikkgyDAPLCNLilfkkvka 389
Cdd:cd12114 201 ARRRDPAHWAElierhgvTLWNSVPALLEML----------LDVLEAA-----------------QALLPSL-------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 390 llggnvRM-MLSG---GAPLSPQTHRFmnVCFCCPIGQGyGLTESCGAGTVTEVTDYTTGRV----GAPLI--CCEIkLK 459
Cdd:cd12114 246 ------RLvLLSGdwiPLDLPARLRAL--APDARLISLG-GATEASIWSIYHPIDEVPPDWRsipyGRPLAnqRYRV-LD 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 460 DWQEggytvhDKPN-PRGEIVIGGQNISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQa 538
Cdd:cd12114 316 PRGR------DCPDwVPGELWIGGRGVALGYLGDPELTAARFVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR- 388
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 75992927 539 GEYVSLGKVEAALKNCPLIDNICAFAKSD--QSYVISFVVP 577
Cdd:cd12114 389 GYRIELGEIEAALQAHPGVARAVVVVLGDpgGKRLAAFVVP 429
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
84-568 |
3.66e-22 |
|
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: 100.06 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 84 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITS 163
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 164 VELLESklkaalvdincvkhiiyvdnktinraeYPEGLEIhSMQSVEELGAKPENLSVPPSrptPSDMAIVMYTSGSTGR 243
Cdd:cd12116 92 DALPDR---------------------------LPAGLPV-LLLALAAAAAAPAAPRTPVS---PDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 244 PKGVMMHHSNLIAGMTGQCERiPGLGPKDTYIG-------------YLPL---AHVLELTAEIScftygcrigySSPLTL 307
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAvttyafdisllelLLPLlagARVVIAPRETQ----------RDPEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 308 SDQSSKIkkgskgdctvlKPTLMAAVPEimdriyknvmskvqemnyVQKTLFKIGYdykleQIKKGYDApLCnlilfkkv 387
Cdd:cd12116 210 ARLIEAH-----------SITVMQATPA------------------TWRMLLDAGW-----QGRAGLTA-LC-------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 388 kallggnvrmmlsGGAPLSPQTHRFmnvcFCCPIGQG---YGLTESCGAGTVTEVTDYTTG-RVGAPLicceiklkdwqe 463
Cdd:cd12116 247 -------------GGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAAAGPiPIGRPL------------ 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 464 GGYTVH--D---KPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:cd12116 298 ANTQVYvlDaalRPVPPgvpGELYIGGDGVAQGYLGRPALTAERFVPDpfaGPGSRLYRTGDLVRRRADGRLEYLGRADG 377
|
490 500 510
....*....|....*....|....*....|....*.
gi 75992927 533 LVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:cd12116 378 QVKIR-GHRIELGEIEAALAAHPGVAQAAVVVREDG 412
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
137-551 |
6.33e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 101.15 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 137 VTLYATLGREAVVHGLNESEASYLITSVELLEsKLKAALVDincvkhiiyvdnktinrAEYPEGLEIHSMqsvEELGAKP 216
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKFLE-KLKNKGFD-----------------LELPENVKVIYL---EDLKAKI 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 217 ENL---------SVPPSR---------PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYL 278
Cdd:PRK08633 752 SKVdkltallaaRLLPARllkrlygptFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSL 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 279 PLAHVLELTAE--------ISCftygcrIGYSSPLtlsdQSSKIKKgskgdcTVLK--PTLMAAVPEIMdRIY-KNvmsk 347
Cdd:PRK08633 831 PFFHSFGLTVTlwlpllegIKV------VYHPDPT----DALGIAK------LVAKhrATILLGTPTFL-RLYlRN---- 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 348 vqemnyvqktlfkigydykleqikkgydaplcnlilfKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGL 427
Cdd:PRK08633 890 -------------------------------------KKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGA 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 428 TESCGAGTV----TEVTDYTT------GRVGAPLICCEIKLKDwQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTA 497
Cdd:PRK08633 933 TETSPVASVnlpdVLAADFKRqtgskeGSVGMPLPGVAVRIVD-PETFEEL--PPGEDGLILIGGPQVMKGYLGDPEKTA 1009
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 75992927 498 EdYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAAL 551
Cdd:PRK08633 1010 E-VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
87-579 |
1.24e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 98.97 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 87 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK----YNfPLVTLYatlgRE-AVVHGLNESEASYLI 161
Cdd:PRK13295 58 YRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRigavLN-PLMPIF----RErELSFMLKHAESKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 162 T-------SVELLESKLKAALVDIncvKHIIYVDnktinrAEYPEGLEIHSMQSVEELGAKPENLSVPPsRPTPSDMAIV 234
Cdd:PRK13295 133 VpktfrgfDHAAMARRLRPELPAL---RHVVVVG------GDGADSFEALLITPAWEQEPDAPAILARL-RPGPDDVTQL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 235 MYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleLTAeiscFTYGCRIgyssPLTLsdqsski 314
Cdd:PRK13295 203 IYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASPMAH---QTG----FMYGLMM----PVML------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 315 kkgskGDCTVLK----PTL-------------MAAVPEIMDriyknvMSKVQEMNyvqktlfkigydykleqikkGYDAP 377
Cdd:PRK13295 264 -----GATAVLQdiwdPARaaelirtegvtftMASTPFLTD------LTRAVKES--------------------GRPVS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 378 lcnlilfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEsCGAGTVT------EVTDYTTGRvgaPL 451
Cdd:PRK13295 313 ----------------SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE-NGAVTLTklddpdERASTTDGC---PL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 452 ICCEIKLKDWQeggytvhDKPNPRGEI---VIGGQNISMGYFKNEEKTAEDycvdenGQRWFCTGDIGEFHPDGCLQIID 528
Cdd:PRK13295 373 PGVEVRVVDAD-------GAPLPAGQIgrlQVRGCSNFGGYLKRPQLNGTD------ADGWFDTGDLARIDADGYIRISG 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 75992927 529 RKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQ 579
Cdd:PRK13295 440 RSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDerlGERACAFVVPRP 492
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
94-570 |
2.13e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 98.31 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 94 VNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITS---------- 163
Cdd:PRK12583 55 VDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAdafktsdyha 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 164 --VELLESKLKAALVDINC-----VKHIIYVDnktinrAEYPEG-LEIHSMQSVEElGAKPENLSVPPSRPTPSDMAIVM 235
Cdd:PRK12583 135 mlQELLPGLAEGQPGALACerlpeLRGVVSLA------PAPPPGfLAWHELQARGE-TVSREALAERQASLDRDDPINIQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 236 YTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYssPLTLSDQSS 312
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNILnnGYFVA--ESL-GLTEHDRLCVPVPLYHCFGMVlANLGCMTVGACLVY--PNEAFDPLA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 313 KIKKGSKGDCTVLK--PTLMAAvpeimdriyknvmskvqEMNYVQKTLFKIGydykleqikkgydaplcnlilfkkvkal 390
Cdd:PRK12583 283 TLQAVEEERCTALYgvPTMFIA-----------------ELDHPQRGNFDLS---------------------------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 391 lggNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTD------YTTGRVGAPLiccEIKLKDwqE 463
Cdd:PRK12583 318 ---SLRTGIMAGAPCPIEVmRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADdlerrvETVGRTQPHL---EVKVVD--P 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 464 GGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVS 543
Cdd:PRK12583 390 DGATV--PRGEIGELCTRGYSVMKGYWNNPEATAE--SIDEDG--WMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIY 462
|
490 500
....*....|....*....|....*..
gi 75992927 544 LGKVEAALKNCPLIDNICAFAKSDQSY 570
Cdd:PRK12583 463 PREIEEFLFTHPAVADVQVFGVPDEKY 489
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
222-642 |
2.14e-21 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 97.75 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 222 PPSRPTPSDMAIVM-YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltAEISC 292
Cdd:cd12118 125 EWIPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylnalANILEW---------EMKQHPVYLWTLPMFH-----CNGWC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 293 FTYGcrigysspltlsdqsskikkgskgdctvlkptlMAAV------------PEIMDRIYKNvmsKVQEMNyvqktlfk 360
Cdd:cd12118 191 FPWT---------------------------------VAAVggtnvclrkvdaKAIYDLIEKH---KVTHFC-------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 361 igydykleqikkgyDAPLCNLILF---KKVKALLGGNVRMMlSGGAPLSPQTHRFMNvcfccPIG----QGYGLTESCGA 433
Cdd:cd12118 227 --------------GAPTVLNMLAnapPSDARPLPHRVHVM-TAGAPPPAAVLAKME-----ELGfdvtHVYGLTETYGP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 434 GTV-----------TEVTDYTTGRVGAPLICCEiklkdwqegGYTVHD----KPNPR-----GEIVIGGQNISMGYFKNE 493
Cdd:cd12118 287 ATVcawkpewdelpTEERARLKARQGVRYVGLE---------EVDVLDpetmKPVPRdgktiGEIVFRGNIVMKGYLKNP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 494 EKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS 573
Cdd:cd12118 358 EATAEAF---RGG--WFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEV 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992927 574 ---FVvpnqkklTLlaqQKGVEgswvdicnnpAMEAEILKEIREaanamKLERFEIPIKVRLSPEPWTPeTG 642
Cdd:cd12118 432 pcaFV-------EL---KEGAK----------VTEEEIIAFCRE-----HLAGFMVPKTVVFGELPKTS-TG 477
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
28-657 |
2.51e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 98.41 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 28 AVIDIPGADTLDKLFDHAVAKFGKKdslgtreilseenemqPNGKVFKKLIlgnykwiNYLEVNCRVNNFGSGLTA-LGL 106
Cdd:PRK08751 17 AEIDLEQFRTVAEVFATSVAKFADR----------------PAYHSFGKTI-------TYREADQLVEQFAAYLLGeLQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 107 KPKNTIAIFCETRAEWMIAAQTCFKYNFPLVT---LYATlgREaVVHGLNESEASYLI------TSVE----------LL 167
Cdd:PRK08751 74 KKGDRVALMMPNCLQYPIATFGVLRAGLTVVNvnpLYTP--RE-LKHQLIDSGASVLVvidnfgTTVQqviadtpvkqVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 168 ESKL-------KAALVDInCVKHII-YVDNKTINRA-EYPEGLEihsmqsveeLGAKPenlSVPPSRPTPSDMAIVMYTS 238
Cdd:PRK08751 151 TTGLgdmlgfpKAALVNF-VVKYVKkLVPEYRINGAiRFREALA---------LGRKH---SMPTLQIEPDDIAFLQYTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 239 GSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP----KDTYIGYLPLAHVLELTAEISCFTY--GCRIGYSSPltlSDQSS 312
Cdd:PRK08751 218 GTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTANGLVFMKigGCNHLISNP---RDMPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 313 KIKKgskgdctvLKPTLMAAVPEImdriyknvmskvqemnyvqKTLFkigydykleqiKKGYDAPLCNLILFKKVKALLG 392
Cdd:PRK08751 295 FVKE--------LKKTRFTAFTGV-------------------NTLF-----------NGLLNTPGFDQIDFSSLKMTLG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 393 GNVRMMLSGGAPLSPQTHrfmnvcfcCPIGQGYGLTESCGAGTVTEVT--DYtTGRVGAPLICCEIKLKDwqeggytVHD 470
Cdd:PRK08751 337 GGMAVQRSVAERWKQVTG--------LTLVEAYGLTETSPAACINPLTlkEY-NGSIGLPIPSTDACIKD-------DAG 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 471 KPNPRGEI---VIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKV 547
Cdd:PRK08751 401 TVLAIGEIgelCIKGPQVMKGYWKRPEETAK--VMDADG--WLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEI 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 548 EAALKNCPLIDNICAFAksdqsyvisfvVPNQKkltllaqqKGVEGSWVDICNNPAMEAEILKEiREAANamkLERFEIP 627
Cdd:PRK08751 476 EDVIAMMPGVLEVAAVG-----------VPDEK--------SGEIVKVVIVKKDPALTAEDVKA-HARAN---LTGYKQP 532
|
650 660 670
....*....|....*....|....*....|
gi 75992927 628 IKVRLSPEpwTPEtglvTDAFKLKRKELKN 657
Cdd:PRK08751 533 RIIEFRKE--LPK----TNVGKILRRELRD 556
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
78-577 |
4.41e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 97.24 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 78 ILGNYKWINYLEVNCRVNNFGSGLT-ALGLKPKNTIAIFcetraewmiaAQTCFKYnfpLVTLYATLGREAVVHGLN--- 153
Cdd:PRK06839 21 IITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAIL----------SQNSLEY---IVLLFAIAKVECIAVPLNirl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 154 -ESEASYLI----TSVELLESKLKAALVDIncvKHIIYVDNKTinRAEYPEGLEIHSMQSVEElgakpenlsvppsrPTP 228
Cdd:PRK06839 88 tENELIFQLkdsgTTVLFVEKTFQNMALSM---QKVSYVQRVI--SITSLKEIEDRKIDNFVE--------------KNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltAEISCFTY-----GCRIGYSS 303
Cdd:PRK06839 149 SASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHI----GGIGLFAFptlfaGGVIIVPR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 304 PLTLSDQSSKIKKGskgdctvlKPTLMAAVPEIMDRiyknvmskvqemnyvqktlfkigydykleqikkgydapLCNLIL 383
Cdd:PRK06839 224 KFEPTKALSMIEKH--------KVTVVMGVPTIHQA--------------------------------------LINCSK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 384 FKKVKAllgGNVRMMLSGGAPLS-PQTHRFMNVCFccPIGQGYGLTEScgAGTV----TEVTDYTTGRVGAPLICCEIKL 458
Cdd:PRK06839 258 FETTNL---QSVRWFYNGGAPCPeELMREFIDRGF--LFGQGFGMTET--SPTVfmlsEEDARRKVGSIGKPVLFCDYEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 459 KDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQA 538
Cdd:PRK06839 331 ID--ENKNKV--EVGEVGELLIRGPNVMKEYWNRPDATEETI---QDG--WLCTGDLARVDEDGFVYIVGRKKEMI-ISG 400
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 75992927 539 GEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 577
Cdd:PRK06839 401 GENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeiPIAFIVK 442
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
152-584 |
4.44e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.59 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 152 LNESEASYLI-TSVELLESKLKAALVDInCVKHIiyvdNKTINRAEYPEGLeihSMQSVEELGAkpeNLSVPPSRPTPSD 230
Cdd:PRK12492 140 LPDTGIEYLIeAKMGDLLPAAKGWLVNT-VVDKV----KKMVPAYHLPQAV---PFKQALRQGR---GLSLKPVPVGLDD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 231 MAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP---------KDTYIGYLPLAHVLELTAEISCFTYgcrigy 301
Cdd:PRK12492 209 IAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplmkegQEVMIAPLPLYHIYAFTANCMCMMV------ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 302 sspltlsdqsskikkgsKGDCTVLKpTLMAAVPEIMDRIYKNVMSKVQEMNyvqkTLFkigydykleqikkgydAPLCNL 381
Cdd:PRK12492 283 -----------------SGNHNVLI-TNPRDIPGFIKELGKWRFSALLGLN----TLF----------------VALMDH 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 382 ILFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVTDYTT----GRVGAPLICCEIK 457
Cdd:PRK12492 325 PGFKDLDF---SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTET---SPVASTNPYGElarlGTVGIPVPGTALK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 458 LKDwQEGgytVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQ 537
Cdd:PRK12492 399 VID-DDG---NELPLGERGELCIKGPQVMKGYWQQPEATAE--ALDAEG--WFKTGDIAVIDPDGFVRIVDRKKDLI-IV 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 75992927 538 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKKLTL 584
Cdd:PRK12492 470 SGFNVYPNEIEDVVMAHPKVANCAAIGVPDErsgEAVKLFVVARDPGLSV 519
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
230-567 |
7.99e-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: 94.26 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLI-AGMtgQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCR---IGYSSPL 305
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 306 TLSD--QSSKIkkgskgdctvlkpTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQIKK-GYDAPlcnli 382
Cdd:cd17637 79 EALEliEEEKV-------------TLMGSFPPILSNL--------------------------LDAAEKsGVDLS----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 383 lfkKVKALLGGNVrmmlsggaplsPQT----HRFMNVCFCCpigqGYGLTESCGAGTVTEVTDyTTGRVGAPLICCEIKL 458
Cdd:cd17637 115 ---SLRHVLGLDA-----------PETiqrfEETTGATFWS----LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 459 KDwqeggytVHDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRK--KDL 533
Cdd:cd17637 176 VD-------DNDRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTF---RNG--WHHTGDLGRFDEDGYLWYAGRKpeKEL 243
|
330 340 350
....*....|....*....|....*....|....
gi 75992927 534 VKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:cd17637 244 IK-PGGENVYPAEVEKVILEHPAIAEVCVIGVPD 276
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-655 |
1.31e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLEIHSMQSVEELGAKPENlsVPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 4657 HLLQ-------------------------RLPIPDGLASLALDRDEDWEGFPAH--DPAVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERiPGLGPKDTYIGYLPLAhvLELTAEiscftygcriGYSSPLTlsdqsskikkgsKGDCTV 324
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFS--FDGSHE----------GLYHPLI------------NGASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LKPTlMAAVPEimdRIYKNVM-SKVQEMNYVQKTLFKIgydykLEQIKKGYDAPLCNLILFKKvKALLGGNVRMMLSGGA 403
Cdd:PRK12316 4765 IRDD-SLWDPE---RLYAEIHeHRVTVLVFPPVYLQQL-----AEHAERDGEPPSLRVYCFGG-EAVAQASYDLAWRALK 4834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 404 PLSpqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTT-GRVGAPlicceIKLKDWQEGGYTVHDKPNPR-----GE 477
Cdd:PRK12316 4835 PVY--------------LFNGYGPTETTVTVLLWKARDGDAcGAAYMP-----IGTPLGNRSGYVLDGQLNPLpvgvaGE 4895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 478 IVIGGQNISMGYFKNEEKTAEDYC---VDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNC 554
Cdd:PRK12316 4896 LYLGGEGVARGYLERPALTAERFVpdpFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIR-GFRIELGEIEARLREH 4974
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 555 PLIDNICAFAK--SDQSYVISFVVPNQKKLTllaqqkgvegswvdicNNPAMEAEILKEIREAANAmKLERFEIPIK-VR 631
Cdd:PRK12316 4975 PAVREAVVIAQegAVGKQLVGYVVPQDPALA----------------DADEAQAELRDELKAALRE-RLPEYMVPAHlVF 5037
|
570 580
....*....|....*....|....
gi 75992927 632 LSPEPWTPETglvtdafKLKRKEL 655
Cdd:PRK12316 5038 LARMPLTPNG-------KLDRKAL 5054
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
84-551 |
1.35e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 95.78 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 84 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkYNFP-----LVTLYATLGREAVVHGLNESEAS 158
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA-MVEAH----FGVPmagavLNTLNTRLDAASIAFMLRHGEAK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 159 YLITSVELLESkLKAALVDINcVKHIIYVDnktINRAEYPEGLEIHSMqSVEELGAK--PEnlsVPPSRPTPSDMAIVM- 235
Cdd:PRK08162 118 VLIVDTEFAEV-AREALALLP-GPKPLVID---VDDPEYPGGRFIGAL-DYEAFLASgdPD---FAWTLPADEWDAIALn 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 236 YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAHvleltaeiscftygCRiGYSSPLTL 307
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHrgaylnalSNILAW---------GMPKHPVYLWTLPMFH--------------CN-GWCFPWTV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 308 sdqsskikkgskgdctvlkpTLMAAVpeimdriykNV-MSKVQEmnyvqKTLFKIGYDyklEQIKKGYDAP-----LCNL 381
Cdd:PRK08162 245 --------------------AARAGT---------NVcLRKVDP-----KLIFDLIRE---HGVTHYCGAPivlsaLINA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 382 IlfKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCcpIGQGYGLTESCGAGTV----TEVTDYTTGRvgapliccEIK 457
Cdd:PRK08162 288 P--AEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD--LTHVYGLTETYGPATVcawqPEWDALPLDE--------RAQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 458 LKDWQ------EGGYTVHD----KPNPR-----GEIVIGGqNISM-GYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPD 521
Cdd:PRK08162 356 LKARQgvryplQEGVTVLDpdtmQPVPAdgetiGEIMFRG-NIVMkGYLKNPKATEEAF---AGG--WFHTGDLAVLHPD 429
|
490 500 510
....*....|....*....|....*....|
gi 75992927 522 GCLQIIDRKKDLVkLQAGEYVSLGKVEAAL 551
Cdd:PRK08162 430 GYIKIKDRSKDII-ISGGENISSIEVEDVL 458
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
85-579 |
1.55e-20 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 95.51 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLESKLKAALVDINCVKHIIYVDnktinraeyPEGLEIHSMQSVEELGAKPENLsvPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIVSG---------GAGPEAGALLLAELVAAEAEQL--KPAATHADDPAFWLYSSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsdqsskikkgSKGDCTV 324
Cdd:cd05959 179 KGVVHLHADIYWTAELYARNVLGIREDDVC-----------FSAAKLFFAYGLGNSLTFPL------------SVGATTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LKPTLMAAvpeimDRIYKnvmskvqEMNYVQKTLFkigydYKLEQIkkgYDAPLCNlilfKKVKALLGGNVRMMLSGGAP 404
Cdd:cd05959 236 LMPERPTP-----AAVFK-------RIRRYRPTVF-----FGVPTL---YAAMLAA----PNLPSRDLSSLRLCVSAGEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 405 LSPQTHRFMNVCFCCPIGQGYGLTE------SCGAGTVtevtdyTTGRVGAPLICCEIKLKDwqEGGYTVHD-KPnprGE 477
Cdd:cd05959 292 LPAEVGERWKARFGLDILDGIGSTEmlhiflSNRPGRV------RYGTTGKPVPGYEVELRD--EDGGDVADgEP---GE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 478 IVIGGQNISMGYFKNEEKTAEDYcvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLI 557
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTF----QGE-WTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEVESALVQHPAV 434
|
490 500
....*....|....*....|....*
gi 75992927 558 DNICAFAKSDQSYVI---SFVVPNQ 579
Cdd:cd05959 435 LEAAVVGVEDEDGLTkpkAFVVLRP 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
211-576 |
2.73e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 95.05 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 211 ELGAKPENlSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCE-RIPGLG--PKDTYIGYLPLAHVLELT 287
Cdd:PLN02246 162 ELTQADEN-ELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLYfhSDDVILCVLPMFHIYSLN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 288 AEISCftyGCRIGysspltlsdqsSKIKKGSKGDCTVL-------KPTLMAAVPEIMDRIYKNVMSKvqemnyvqktlfk 360
Cdd:PLN02246 241 SVLLC---GLRVG-----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKSPVVE------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 361 igyDYKLEQIkkgydaplcnlilfkkvkallggnvRMMLSGGAPLSPQTH-----RFMNVCfccpIGQGYGLTEscgAGT 435
Cdd:PLN02246 294 ---KYDLSSI-------------------------RMVLSGAAPLGKELEdafraKLPNAV----LGQGYGMTE---AGP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 436 V--------TEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGq 507
Cdd:PLN02246 339 VlamclafaKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDPEATAN--TIDKDG- 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992927 508 rWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVV 576
Cdd:PLN02246 413 -WLHTGDIGYIDDDDELFIVDRLKELIKYK-GFQVAPAELEALLISHPSIADAAVVPMKDEVageVPVAFVV 482
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
228-580 |
3.86e-20 |
|
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: 93.69 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKdtyigylPLAHVleltaEISCFTYGCRIG-YSSPLT 306
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAHAWRREYELDSF-------PVRLL-----QMASFSFDVFAGdFARSLL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LSDQSSKIKKGSKGDCTVL-------KPTLMAAVPE----IMDRIYKNvmskvqEMNYVQKTLFKIGYDykleqikkgyd 375
Cdd:cd17650 159 NGGTLVICPDEVKLDPAALydlilksRITLMESTPAlirpVMAYVYRN------GLDLSAMRLLIVGSD----------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 376 apLCNLILFKKVKALLGGNVRMMLSggaplspqthrfmnvcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAP 450
Cdd:cd17650 222 --GCKAQDFKTLAARFGQGMRIINS------------------------YGVTEATIDSTYYEEGRDPLGDsanvpIGRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 451 LICCEIKLKDwqeggytVHDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQ 525
Cdd:cd17650 276 LPNTAMYVLD-------ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVENpfAPGERMYRTGDLARWRADGNVE 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 526 IIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 580
Cdd:cd17650 349 LLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVVAVREDkggEARLCAYVVAAAT 405
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-615 |
8.30e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 93.46 E-value: 8.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 84 WINYLEVNCRVNNFGSGLTALGlKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLN---ESEASYL 160
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAilaDAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ITSvelleSKLKAALVDIncvkhiiyvdnktinrAEYPEGLEIHSMQSVEELGAKPENLSVPPSrPTPSDMAIVMYTSGS 240
Cdd:cd05931 103 LTT-----AAALAAVRAF----------------AASRPAAGTPRLLVVDLLPDTSAADWPPPS-PDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 241 TGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH----VLELTAEISCftyGCRIGYSSPLT-LSDQSSKIK 315
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYHdmglIGGLLTPLYS---GGPSVLMSPAAfLRRPLRWLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 316 KGSKGDCTvlkptlMAAVPeimdriyknvmskvqemNYvqktlfkiGYDYkleQIKKGYDAPLCNLILfkkvkallgGNV 395
Cdd:cd05931 237 LISRYRAT------ISAAP-----------------NF--------AYDL---CVRRVRDEDLEGLDL---------SSW 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 396 RMMLSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTESCGAgtVtevtdyTTGRVGAPLICCEIkLKDWQEGG 465
Cdd:cd05931 274 RVALNGAEPVRPATlRRFAEAfapfgfrpeAFRP----SYGLAEATLF--V------SGGPPGTGPVVLRV-DRDALAGR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 466 YTVHDKPNPR--------------------------------GEIVIGGQNISMGYFKNEEKTAEDYCV----DENGqrW 509
Cdd:cd05931 341 AVAVAADDPAarelvscgrplpdqevrivdpetgrelpdgevGEIWVRGPSVASGYWGRPEATAETFGAlaatDEGG--W 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 510 FCTGDIGEFHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPlidnicafAKSDQSYVISFVVPNQKKLTLLAQQK 589
Cdd:cd05931 419 LRTGDLGFLH-DGELYITGRLKDLI-IVRGRNHYPQDIEATAEEAH--------PALRPGCVAAFSVPDDGEERLVVVAE 488
|
570 580
....*....|....*....|....*.
gi 75992927 590 gVEGSWVdicnnPAMEAEILKEIREA 615
Cdd:cd05931 489 -VERGAD-----PADLAAIAAAIRAA 508
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
227-578 |
1.09e-19 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 92.61 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLA---HVLE-LTAEISCftyGCRIGYS 302
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAL-GLTSESRVLQFASYTfdvSILEiFTTLAAG---GCLCIPS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 303 SPLTLSDQSSKIKKgSKGDCTVLKPTLMA-----AVPEImdriyknvmskvqemnyvqKTLFKIGydyklEQIKKgydap 377
Cdd:cd05918 180 EEDRLNDLAGFINR-LRVTWAFLTPSVARlldpeDVPSL-------------------RTLVLGG-----EALTQ----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 378 lcnlilfkKVKALLGGNVRMMlsggaplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVTDYTTGR-VGAPL--ICC 454
Cdd:cd05918 230 --------SDVDTWADRVRLI------------------------NAYGPAECTIAATVSPVVPSTDPRnIGRPLgaTCW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 455 EIKLKDwqeggytvHDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDY---------CVDENGQRWFCTGDIGEFHPDG 522
Cdd:cd05918 278 VVDPDN--------HDRLVPIgavGELLIEGPILARGYLNDPEKTAAAFiedpawlkqEGSGRGRRLYRTGDLVRYNPDG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992927 523 CLQIIDRKKDLVKLQaGEYVSLGKVEAALKNC-PLIDNICAFA-----KSDQSYVISFVVPN 578
Cdd:cd05918 350 SLEYVGRKDTQVKIR-GQRVELGEIEHHLRQSlPGAKEVVVEVvkpkdGSSSPQLVAFVVLD 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-627 |
3.64e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 89.64 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYSSP 304
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERL-GLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 305 LTlsDQSSKIKKGSKGDCTVLK--PTLMAAVpeimdriyknvmskvqemnyvqktlfkigydykLEQIKKG-YDAplcnl 381
Cdd:cd05917 78 SF--DPLAVLEAIEKEKCTALHgvPTMFIAE---------------------------------LEHPDFDkFDL----- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 382 ilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGR---VGAPLICCEIK 457
Cdd:cd05917 118 -----------SSLRTGIMAGAPCPPELmKRVIEVMNMKDVTIAYGMTETSPVSTQTRTDDSIEKRvntVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 458 LKDwQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQ 537
Cdd:cd05917 187 IVD-PEGGIVP--PVGVPGELCIRGYSVMKGYWNDPEKTAE--AID--GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 538 AGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYvisfvvpnqkkltllaqqkGVE-GSWVDICNNPAMEAEilkEIREAA 616
Cdd:cd05917 259 GGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-------------------GEEvCAWIRLKEGAELTEE---DIKAYC 316
|
410
....*....|.
gi 75992927 617 NAmKLERFEIP 627
Cdd:cd05917 317 KG-KIAHYKVP 326
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-557 |
3.68e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.10 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRA---EWMIAAQTCFKYNFPLvtlYATLGREAVVHGLNESEASYLI 161
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAaflELAFAASYLGAVFLPI---NYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 162 TSVELlesKLKAALVDINCVkhiiyvdnktinraeypegLEIHSMQSVEELGAKpeNLSVPPSRPT-PSDMAIVMYTSGS 240
Cdd:PRK06145 105 VDEEF---DAIVALETPKIV-------------------IDAAAQADSRRLAQG--GLEIPPQAAVaPTDLVRLMYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 241 TGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHV--LELTAeISCFTYGCRIGYSSPLTLSDQSSKIKKgS 318
Cdd:PRK06145 161 TDRPKGVMHSYGNLHWKSIDHVIAL-GLTASERLLVVGPLYHVgaFDLPG-IAVLWVGGTLRIHREFDPEAVLAAIER-H 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 319 KGDCTVLKPTLMAAVPEIMDRiyknvmskvqemnyvqktlfkigYDYKLeqikkgydaplcnlilfkkvkallgGNVRMM 398
Cdd:PRK06145 238 RLTCAWMAPVMLSRVLTVPDR-----------------------DRFDL-------------------------DSLAWC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 399 LSGGAPLSPQTHR-----FMNVCFCcpigQGYGLTESCGAGTVTEVTDY--TTGRVGAPLICCEIKLKDwQEGGYTvhdK 471
Cdd:PRK06145 270 IGGGEKTPESRIRdftrvFTRARYI----DAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIAD-GAGRWL---P 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 472 PNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAAL 551
Cdd:PRK06145 342 PNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVI 415
|
....*.
gi 75992927 552 KNCPLI 557
Cdd:PRK06145 416 YELPEV 421
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
210-579 |
4.00e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.44 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 210 EELGAKPENLSVPPSRPtpSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTG----QCERIPGLGPKDTYIGYLPLAHVLE 285
Cdd:PLN02574 181 ELIKEDFDFVPKPVIKQ--DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELfvrfEASQYEYPGSDNVYLAALPMFHIYG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 286 LtaeiSCFTYGcrigyssplTLSDQSSKIkkgskgdctvlkptlmaavpeIMDRIYKNVMSKVQEMNYVqkTLFKIgydy 365
Cdd:PLN02574 259 L----SLFVVG---------LLSLGSTIV---------------------VMRRFDASDMVKVIDRFKV--THFPV---- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 366 kleqikkgydAPLCNLILFKKVKALLGG---NVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGT----VT 437
Cdd:PLN02574 299 ----------VPPILMALTKKAKGVCGEvlkSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIQGYGMTESTAVGTrgfnTE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 438 EVTDYTTGRVGAPLIccEIKLKDWQEGGYTvhdKPNPRGEIVIGGQNISMGYFKNEEKTaeDYCVDENGqrWFCTGDIGE 517
Cdd:PLN02574 369 KLSKYSSVGLLAPNM--QAKVVDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNPKAT--QSTIDKDG--WLRTGDIAY 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 518 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQ 579
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYK-GFQIAPADLEAVLISHPEIIDAAVTAVPDKecgEIPVAFVVRRQ 503
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
101-534 |
5.19e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 90.71 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 101 LTALGLKPKNTIAIFCETRAEWMIaaqtcfkynfplvtLY-ATLGREAVVHGLN----ESEASYLITSVEllesklkAAL 175
Cdd:PRK07514 45 LVALGVKPGDRVAVQVEKSPEALA--------------LYlATLRAGAVFLPLNtaytLAELDYFIGDAE-------PAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 176 VdincvkhiiYVDNKtiNRAEYPEGLEIHSMQSVEELGAKPEN------LSVPPSRPT----PSDMAIVMYTSGSTGRPK 245
Cdd:PRK07514 104 V---------VCDPA--NFAWLSKIAAAAGAPHVETLDADGTGslleaaAAAPDDFETvprgADDLAAILYTSGTTGRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 246 GVMMHHSNLIA-GMTgqCERIPGLGPKDTYIGYLPLAHVLELTAEISCftygcrigyssplTLSDQSSKIkkgskgdctv 324
Cdd:PRK07514 173 GAMLSHGNLLSnALT--LVDYWRFTPDDVLIHALPIFHTHGLFVATNV-------------ALLAGASMI---------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LKPTL-MAAVPEIMDRiyKNVMSKVqemnyvqKTLfkigYDYKLEQikKGYDAPLCnlilfkkvkallgGNVRMMLSGGA 403
Cdd:PRK07514 228 FLPKFdPDAVLALMPR--ATVMMGV-------PTF----YTRLLQE--PRLTREAA-------------AHMRLFISGSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 404 PLSPQTHRfmnvCFCCPIGQG----YGLTESC--------G---AGTVtevtdyttgrvGAPLICCEIKLKDWQEGgytv 468
Cdd:PRK07514 280 PLLAETHR----EFQERTGHAilerYGMTETNmntsnpydGerrAGTV-----------GFPLPGVSLRVTDPETG---- 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75992927 469 hdKPNPRGE---IVIGGQNISMGYFKNEEKTAEDYCVDenGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK07514 341 --AELPPGEigmIEVKGPNVFKGYWRMPEKTAEEFRAD--G--FFITGDLGKIDERGYVHIVGRGKDLI 403
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
143-534 |
6.55e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 90.78 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 143 LGREAVVHGLNESEASYLITSVELLES----KLKAALVDINCVKHIIYVDnktINRAEYPEGLEIHSMQSV--------- 209
Cdd:PRK07529 116 LEPEQIAELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVD---LARYLPGPKRLAVPLIRRkaharildf 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 210 -EELGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTA 288
Cdd:PRK07529 193 dAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA-NAWLGALLLGLGPGDTVFCGLPLFHVNALLV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 289 EI-SCFTYGCRIGYSSPLtlsdqsskikkGSKGdctvlkPTLMAAVPEIMDRIYKNVMSKVqemnyvqKTLfkigYDYKL 367
Cdd:PRK07529 272 TGlAPLARGAHVVLATPQ-----------GYRG------PGVIANFWKIVERYRINFLSGV-------PTV----YAALL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 368 EQIKKGYDAplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHR-FMNVCfCCPIGQGYGLTESCGAGTVTEV-TDYTTG 445
Cdd:PRK07529 324 QVPVDGHDI----------------SSLRYALCGAAPLPVEVFRrFEAAT-GVRIVEGYGLTEATCVSSVNPPdGERRIG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 446 RVGAPLICCEIKLKDWQEGGYTVHD-KPNPRGEIVIGGQNISMGYFknEEKTAEDYCVDEngqRWFCTGDIGEFHPDGCL 524
Cdd:PRK07529 387 SVGLRLPYQRVRVVILDDAGRYLRDcAVDEVGVLCIAGPNVFSGYL--EAAHNKGLWLED---GWLNTGDLGRIDADGYF 461
|
410
....*....|
gi 75992927 525 QIIDRKKDLV 534
Cdd:PRK07529 462 WLTGRAKDLI 471
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
36-534 |
1.02e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 89.87 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 36 DTLDKLFDHAVAKFGKKDSLGTREilseenemqpngkvfkklilGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIF 115
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRD--------------------QGLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 116 CETRAEWmiaaqtcfkynfpLVTLYAT--LG----------REA-VVHGLNESEASYLITS--------VELLES----- 169
Cdd:PRK08315 75 APNVPEW-------------VLTQFATakIGailvtinpayRLSeLEYALNQSGCKALIAAdgfkdsdyVAMLYElapel 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 170 ------KLKAALVDinCVKHIIYV-DNKTINRAEYPEGLEIHSMQSVEELGAKPENLSvppsrptPSDmAIVM-YTSGST 241
Cdd:PRK08315 142 atcepgQLQSARLP--ELRRVIFLgDEKHPGMLNFDELLALGRAVDDAELAARQATLD-------PDD-PINIqYTSGTT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 242 GRPKGVMMHHSNLI--AGMTGQCERipgLGPKDTYIGYLPLAH----VLeltAEISCFTYGCRIGYssPLTLSDQSSKIK 315
Cdd:PRK08315 212 GFPKGATLTHRNILnnGYFIGEAMK---LTEEDRLCIPVPLYHcfgmVL---GNLACVTHGATMVY--PGEGFDPLATLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 316 KGSKGDCTVLK--PTL----------------------MAAVP---EIMdriyKNVMSKvqeMNYVQKTLfkigydykle 368
Cdd:PRK08315 284 AVEEERCTALYgvPTMfiaeldhpdfarfdlsslrtgiMAGSPcpiEVM----KRVIDK---MHMSEVTI---------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 369 qikkgydaplcnlilfkkvkallggnvrmmlsggaplspqthrfmnvcfccpigqGYGLTESCGAGTVTEVTD-----YT 443
Cdd:PRK08315 347 -------------------------------------------------------AYGMTETSPVSTQTRTDDplekrVT 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 444 TgrVGAPLICCEIKLKDwQEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGC 523
Cdd:PRK08315 372 T--VGRALPHLEVKIVD-PETGETV--PRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDADG--WMHTGDLAVMDEEGY 442
|
570
....*....|.
gi 75992927 524 LQIIDRKKDLV 534
Cdd:PRK08315 443 VNIVGRIKDMI 453
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
227-587 |
1.20e-18 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 89.29 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIgylpLAH-------VLELtaeISCFTYGCRI 299
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDDVWT----LFHsyafdfsVWEI---WGALLHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 300 gysspltlsdqsskikkgskgdctVLKPTLMAAVPEIMDRIYKNvmSKVQEMNYVqKTLFkigydYKLEQIKKGYDAPLC 379
Cdd:cd17643 163 ------------------------VVVPYEVARSPEDFARLLRD--EGVTVLNQT-PSAF-----YQLVEAADRDGRDPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 380 NLilfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQ---GYGLTESCGAGTVTEVTDYTTGRVGAPLICCEI 456
Cdd:cd17643 211 AL--------------RYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETTVHVTFRPLDAADLPAAAASPIGRPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 457 klkdwqeGGYTVH-----DKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVDEN---GQRWFCTGDIGEFHPDGCLQ 525
Cdd:cd17643 277 -------PGLRVYvldadGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpGSRMYRTGDLARRLPDGELE 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 526 IIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQKKLTLLAQ 587
Cdd:cd17643 350 YLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDepgDTRLVAYVVADDGAAADIAE 413
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-567 |
1.61e-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: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 93 RVNNFGSGLTALGLKPKNTIAI-------FCETRAEWMIAAQTCFKYnfpLVTLYATLgREAVVHGLNESEASYLITSVE 165
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLilpnrftYIELSFAVAYAGGRLGLV---FVPLNPTL-KESVLRYLVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 166 LLESKLKAALVDincvkhiiYVDNKTINRAEypegleihsmqsveelGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRPK 245
Cdd:cd05922 78 GAADRLRDALPA--------SPDPGTVLDAD----------------GIRAARASAPAHEVSHEDLALLLYTSGSTGSPK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 246 GVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI----GYSSPLTLSDqsskikkgskgD 321
Cdd:cd05922 134 LVRLSHQNLLANARSIAEYL-GITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDDAFWE-----------D 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 322 CTVLKPTLMAAVP---EIMDRiyknvmskvqemnyvqktlfkIGYDykleqikkgyDAPLCNLilfkkvkallggnvRMM 398
Cdd:cd05922 202 LREHGATGLAGVPstyAMLTR---------------------LGFD----------PAKLPSL--------------RYL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 399 LSGGAPLSPQT-HRFmnvcfcCPIGQG------YGLTEsCGAGTVT---EVTDYTTGRVGAPLICCEIKLKDwQEGGYTv 468
Cdd:cd05922 237 TQAGGRLPQETiARL------RELLPGaqvyvmYGQTE-ATRRMTYlppERILEKPGSIGLAIPGGEFEILD-DDGTPT- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 469 hdKPNPRGEIVIGGQNISMGYFKNEEKTAEDycVDENGQRWfcTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVE 548
Cdd:cd05922 308 --PPGEPGEIVHRGPNVMKGYWNDPPYRRKE--GRGGGVLH--TGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIE 380
|
490
....*....|....*....
gi 75992927 549 AALKNCPLIDNICAFAKSD 567
Cdd:cd05922 381 AAARSIGLIIEAAAVGLPD 399
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
230-555 |
1.98e-18 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 86.79 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCRIGYSSPLTlsd 309
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFH-----------TFGYKAGIVACLL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 310 qsskikKGSkgdcTVLkPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGY--DYKLEQIKKGYD-APLCNLILFKK 386
Cdd:cd17638 66 ------TGA----TVV-PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGrkKFDLSSLRAAVTgAATVPVELVRR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 387 VKALLGgnvrmmlsggaplspqthrFMNVCfccpigQGYGLTEsCGAGTVTEVTDYTT---GRVGAPLICCEIKLKDwqe 463
Cdd:cd17638 135 MRSELG-------------------FETVL------TAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 464 ggytvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVS 543
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAE--AIDADG--WLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVY 249
|
330
....*....|..
gi 75992927 544 LGKVEAALKNCP 555
Cdd:cd17638 250 PAEVEGALAEHP 261
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
60-564 |
2.89e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 88.66 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 60 ILSEENEMQPNgkvfKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAE---------WMIAAQTcf 130
Cdd:PRK06155 26 MLARQAERYPD----RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEfldvflgcaWLGAIAV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 131 kynfPLVTLYATLGREavvHGLNESEASYLITSVELLESkLKAALVDINCVKHIIYVDNKTINRAeyPEGLEIHSMqsve 210
Cdd:PRK06155 100 ----PINTALRGPQLE---HILRNSGARLLVVEAALLAA-LEAADPGDLPLPAVWLLDAPASVSV--PAGWSTAPL---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 211 elgaKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAG-MTGqceRIPGLGPKDTYIGYLPLAHVLELTA 288
Cdd:PRK06155 166 ----PPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyWWGrNSA---EDLEIGADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 289 EISCFTYGCRIgysspltlsdqsskikkgskgdctVLKPTLMAAvpEIMDRIYKNvmskvqemnyvQKTLFkigydYKLe 368
Cdd:PRK06155 239 FFQALLAGATY------------------------VLEPRFSAS--GFWPAVRRH-----------GATVT-----YLL- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 369 qikkGYDAPlcnlILFKKVK--ALLGGNVRMMLSGGAPlsPQTHRFMNVCFCCPIGQGYGLTES---CGaGTVTEVTDYT 443
Cdd:PRK06155 276 ----GAMVS----ILLSQPAreSDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETnfvIA-VTHGSQRPGS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 444 TGRVgAPLIccEIKLKDwqeggytVHDKPNPR---GEIVIGGQN---ISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGE 517
Cdd:PRK06155 345 MGRL-APGF--EARVVD-------EHDQELPDgepGELLLRADEpfaFATGYFGMPEKTVEAW-----RNLWFHTGDRVV 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 75992927 518 FHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 564
Cdd:PRK06155 410 RDADGWFRFVDRIKDAIRRR-GENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
192-579 |
5.43e-18 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 87.72 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 192 INRAEYPEGLEIHSMQSVEELGAKPENLSVPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPK 271
Cdd:cd05906 132 FAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTPQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 272 DTYIGYLPLAHVLELT-AEISCFTYGCR-IGYSSPLTLSDqsskikkgskgdctvlkPTLMAavpEIMDRiyknvmskvq 349
Cdd:cd05906 209 DVFLNWVPLDHVGGLVeLHLRAVYLGCQqVHVPTEEILAD-----------------PLRWL---DLIDR---------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 350 emnyvqktlFKIGYDYkleqikkgydAP--LCNLIL-----FKKVKALLgGNVRMMLSGGAPLSPQTHRFM--------- 413
Cdd:cd05906 259 ---------YRVTITW----------APnfAFALLNdlleeIEDGTWDL-SSLRYLVNAGEAVVAKTIRRLlrllepygl 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 414 --NVcfccpIGQGYGLTESCgAGTVTEVTDYTTGR--------VGAPLICCEIKLKDwqeggytVHDKPNPRGEI---VI 480
Cdd:cd05906 319 ppDA-----IRPAFGMTETC-SGVIYSRSFPTYDHsqalefvsLGRPIPGVSMRIVD-------DEGQLLPEGEVgrlQV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 481 GGQNISMGYFKNEEKTAEDYCVDEngqrWFCTGDIGEFHpDGCLQIIDRKKDLVKLQAGEYvSLGKVEAALKNCPLIDN- 559
Cdd:cd05906 386 RGPVVTKGYYNNPEANAEAFTEDG----WFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNY-YSHEIEAAVEEVPGVEPs 459
|
410 420
....*....|....*....|....*.
gi 75992927 560 -ICAFAKSDQS-----YVIsFVVPNQ 579
Cdd:cd05906 460 fTAAFAVRDPGaeteeLAI-FFVPEY 484
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
220-577 |
6.15e-18 |
|
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: 87.33 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 220 SVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLA---HVLELTAEISCftyG 296
Cdd:cd17646 129 TPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYP-LGPGDRVLQKTPLSfdvSVWELFWPLVA---G 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 297 CRIGYSSPLTLSDqsskikkgskgdctvlkptlMAAVPEIMDRiyknvmSKVQEMNYVQKTLfkigyDYKLEQIKKGYDA 376
Cdd:cd17646 205 ARLVVARPGGHRD--------------------PAYLAALIRE------HGVTTCHFVPSML-----RVFLAEPAAGSCA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 377 PLcnlilfkkvkallggnvRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTEscgagTVTEVTDYT-TGRVGAPLIcc 454
Cdd:cd17646 254 SL-----------------RRVFCSGEALPPELaARFLAL-PGAELHNLYGPTE-----AAIDVTHWPvRGPAETPSV-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 455 EIKLKDWQEGGYTVHDKPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQII 527
Cdd:cd17646 309 PIGRPVPNTRLYVLDDALRPVpvgvpGELYLGGVQLARGYLGRPALTAERFVPDpfGPGSRMYRTGDLARWRPDGALEFL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 75992927 528 DRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd17646 389 GRSDDQVKIR-GFRVEPGEIEAALAAHPAVTHAVVVARAAPAgaaRLVGYVVP 440
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
85-579 |
6.48e-18 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 87.20 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLESkLKAALVDINCVKHIIYVdnktiNRAEYPEgleihsMQSVEELGAKPENLSVPPSRPtpSDMAIVMYTSGSTGRP 244
Cdd:TIGR02262 111 ALLPV-IKAALGKSPHLEHRVVV-----GRPEAGE------VQLAELLATESEQFKPAATQA--DDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLsdqsskikkgskGDCTV 324
Cdd:TIGR02262 177 KGVVHTHSNPYWTAELYARNTLGIREDDVC-----------FSAAKLFFAYGLGNALTFPMSV------------GATTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 lkptLMAAVPeIMDRIYKnvmskvqEMNYVQKTLFKigydykleQIKKGYDAPLCNlilfKKVKALLGGNVRMMLSGGAP 404
Cdd:TIGR02262 234 ----LMGERP-TPDAVFD-------RLRRHQPTIFY--------GVPTLYAAMLAD----PNLPSEDQVRLRLCTSAGEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 405 LSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYTVHDkpNPRGEIVIGGQN 484
Cdd:TIGR02262 290 LPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG--DGGQDVAD--GEPGELLISGPS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 485 ISMGYFKNEEKTAEDYcvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFA 564
Cdd:TIGR02262 366 SATMYWNNRAKSRDTF----QGE-WTRSGDKYVRNDDGSYTYAGRTDDMLKV-SGIYVSPFEIESALIQHPAVLEAAVVG 439
|
490
....*....|....*...
gi 75992927 565 KSDQSYVI---SFVVPNQ 579
Cdd:TIGR02262 440 VADEDGLIkpkAFVVLRP 457
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
85-552 |
7.15e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 87.25 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL-YATLGREaVVHGLNESEASYLITS 163
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALVYE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 164 VELLEsKLKAALVDINCVKHIIYVDNKTINrAEYPEGLEIHSMQSveelGAKPENLSVPPSrptPSDMaIVMYTSGSTGR 243
Cdd:PRK07798 108 REFAP-RVAEVLPRLPKLRTLVVVEDGSGN-DLLPGAVDYEDALA----AGSPERDFGERS---PDDL-YLLYTGGTTGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 244 PKGVMMHHSNLiagmtgqceRIPGLGPKDTYIGylPLAHVLELTAEISCFTYGCRIGYSSPL--------TLSDQSSkik 315
Cdd:PRK07798 178 PKGVMWRQEDI---------FRVLLGGRDFATG--EPIEDEEELAKRAAAGPGMRRFPAPPLmhgagqwaAFAALFS--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 316 kgskGDCTVLKPTLMAAVPEIMDRIYKNvmsKVQEMnyvqktlFKIGydykleqikkgyDA---PLcnlilfkkVKALLG 392
Cdd:PRK07798 244 ----GQTVVLLPDVRFDADEVWRTIERE---KVNVI-------TIVG------------DAmarPL--------LDALEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 393 GN------VRMMLSGGAPLSPQTHR-----FMNVCfccpIGQGYGLTES--CGAGTVTEVTDYTTG-RVGAPLICCEIkl 458
Cdd:PRK07798 290 RGpydlssLFAIASGGALFSPSVKEallelLPNVV----LTDSIGSSETgfGGSGTVAKGAVHTGGpRFTIGPRTVVL-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 459 kdwQEGGYTVHDKPNPRGEIVIGGqNISMGYFKNEEKTAEDYCVdENGQRWFCTGDIGEFHPDGCLQIIDRkKDLVKLQA 538
Cdd:PRK07798 364 ---DEDGNPVEPGSGEIGWIARRG-HIPLGYYKDPEKTAETFPT-IDGVRYAIPGDRARVEADGTITLLGR-GSVCINTG 437
|
490
....*....|....
gi 75992927 539 GEYVSLGKVEAALK 552
Cdd:PRK07798 438 GEKVFPEEVEEALK 451
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
222-579 |
1.43e-17 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 86.24 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPL---AHVLELtaeiscFTYGCr 298
Cdd:cd17651 129 PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS-LGPGARTLQFAGLgfdVSVQEI------FSTLC- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 igysspltlsdqsskikkgsKGDCTVLKP--------TLMAAVPEimdriyknvmskvqemnyvqktlfkigydYKLEQI 370
Cdd:cd17651 201 --------------------AGATLVLPPeevrtdppALAAWLDE-----------------------------QRISRV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 371 kkgyDAP---LCNLILFKKVKALLGGNVRMMLSGGAPLS--------PQTHRFMNVCFccpigqGYGLTESCGAgTVTEV 439
Cdd:cd17651 232 ----FLPtvaLRALAEHGRPLGVRLAALRYLLTGGEQLVltedlrefCAGLPGLRLHN------HYGPTETHVV-TALSL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 440 TDYTTGR-----VGAPLICCEIKLKDwqeggytVHDKPNPR---GEIVIGGQNISMGYFKNEEKTAEDYCVDE--NGQRW 509
Cdd:cd17651 301 PGDPAAWpapppIGRPIDNTRVYVLD-------AALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPfvPGARM 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992927 510 FCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQ 579
Cdd:cd17651 374 YRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALARHPGVREAVVLAREDRPgekRLVAYVVGDP 445
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
226-577 |
1.54e-17 |
|
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: 85.44 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 226 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-------AGMTgqceripgLGPKDTyigylpLAHVLELTAEISCFTYGCR 298
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyvsqppARLD--------VGPGSR------VAQVLSIAFDACIGEIFST 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IGYSSPLTLSDQSSKIKKGSKG-DCTVLKPTLMAAVPeimdriyknvmskvqemnyvqktlfkigydykleqiKKGYDap 377
Cdd:cd17653 168 LCNGGTLVLADPSDPFAHVARTvDALMSTPSILSTLS------------------------------------PQDFP-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 378 lcnlilfkkvkallggNVRMMLSGGAPLSP-------QTHRFMNvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAP 450
Cdd:cd17653 210 ----------------NLKTIFLGGEAVPPslldrwsPGRRLYN---------AYGPTECTISSTMTELLPGQPVTIGKP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 451 LICCEIKLKDWQEggytvhdKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQ 525
Cdd:cd17653 265 IPNSTCYILDADL-------QPVPegvVGEICISGVQVARGYLGNPALTASKFVPDpfWPGSRMYRTGDYGRWTEDGGLE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 75992927 526 IIDRKKDLVKLQaGEYVSLGKVEA-ALKNCPLIDNICAFAKSDQsyVISFVVP 577
Cdd:cd17653 338 FLGREDNQVKVR-GFRINLEEIEEvVLQSQPEVTQAAAIVVNGR--LVAFVTP 387
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
229-568 |
1.92e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 86.19 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMtgqCERIPGLGP----KDTYIGYLPLAHVLELTAeISCFTYgcrigyssp 304
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRNLVANL---CSSLFSVGPemigQVVTLGLIPFFHIYGITG-ICCATL--------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 305 ltlsDQSSKIKKGSKGDCTVLKPTLMAA-------VPEIMDRIYKNVMskVQEmnyvqktlfkigydYKLEQIKkgydap 377
Cdd:PLN02330 251 ----RNKGKVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKNPI--VEE--------------FDLSKLK------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 378 lcnlilfkkvkallggnVRMMLSGGAPLSPQ-----THRFMNVcfccPIGQGYGLTE-SCGagTVTEvTDYTTGR----- 446
Cdd:PLN02330 305 -----------------LQAIMTAAAPLAPElltafEAKFPGV----QVQEAYGLTEhSCI--TLTH-GDPEKGHgiakk 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 447 --VGAPLICCEIKLKDWQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCL 524
Cdd:PLN02330 361 nsVGFILPNLEVKFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYNNKEETDR--TIDEDG--WLHTGDIGYIDDDGDI 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 75992927 525 QIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:PLN02330 434 FIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
81-580 |
2.14e-17 |
|
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: 85.60 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 81 NYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYL 160
Cdd:cd17656 11 NQKL-TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ITSVELlESKLKaalvdincvkhiiyvDNKTINRAEYPegleIHSMQSVEELGAKPENlsvppsrptpSDMAIVMYTSGS 240
Cdd:cd17656 90 LTQRHL-KSKLS---------------FNKSTILLEDP----SISQEDTSNIDYINNS----------DDLLYIIYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 241 TGRPKGVMMHHSNLIAGMtgQCERipglgpkdTYIGYLPLAHVLELTAeiscftygcrigYSSPLTLSDQSSKIKKGskG 320
Cdd:cd17656 140 TGKPKGVQLEHKNMVNLL--HFER--------EKTNINFSDKVLQFAT------------CSFDVCYQEIFSTLLSG--G 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 321 DCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKigydykleqiKKGYDAPLcnlilFKKVKALLGGNVRMMLS 400
Cdd:cd17656 196 TLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS----------EREFINRF-----PTCVKHIITAGEQLVIT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 401 ggaplspQTHRFMNVCFCCPIGQGYGLTEScgagtvTEVTDYTTGR---------VGAPLICCEIKLKDWQEggytvhdK 471
Cdd:cd17656 261 -------NEFKEMLHEHNVHLHNHYGPSET------HVVTTYTINPeaeipelppIGKPISNTWIYILDQEQ-------Q 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 472 PNPRG---EIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 546
Cdd:cd17656 321 LQPQGivgELYISGASVARGYLNRQELTAEKFFPDpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR-GYRIELGE 399
|
490 500 510
....*....|....*....|....*....|....*..
gi 75992927 547 VEAALKNCPLIDNICAFAKSD---QSYVISFVVPNQK 580
Cdd:cd17656 400 IEAQLLNHPGVSEAVVLDKADdkgEKYLCAYFVMEQE 436
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
87-555 |
2.44e-17 |
|
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: 85.33 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 87 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkynfpLVTLYAtlgreavvhGlneseASYLITSVEL 166
Cdd:cd12117 25 YAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVAL--------LAVLKA---------G-----AAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 167 LESKLKAALVDINCVkhIIYVDNKTINRAEYPEGLEIHsmqsVEELGAKPEnlSVPPSRPTPSDMAIVMYTSGSTGRPKG 246
Cdd:cd12117 82 PAERLAFMLADAGAK--VLLTDRSLAGRAGGLEVAVVI----DEALDAGPA--GNPAVPVSPDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 247 VMMHHSNLIAGMTGQCERipGLGPKDTYIGYLPL---AHVLELtaeiscftYGCRIgysspltlsdqsskikkgSKGDCT 323
Cdd:cd12117 154 VAVTHRGVVRLVKNTNYV--TLGPDDRVLQTSPLafdASTFEI--------WGALL------------------NGARLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 324 VLKPTLMAAVPEIMDRIYKNVMSkvqemnyvqkTLFKIgydykleqikkgydAPLCNLILFKKVKALLGgnVRMMLSGGA 403
Cdd:cd12117 206 LAPKGTLLDPDALGALIAEEGVT----------VLWLT--------------AALFNQLADEDPECFAG--LRELLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 404 PLSPQ-THRFMNVCFCCPIGQGYGLTESCGAGTVTEVT--DYTTGRV--GAPLicceiklkdwqeGGYTV-----HDKPN 473
Cdd:cd12117 260 VVSPPhVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTelDEVAGSIpiGRPI------------ANTRVyvldeDGRPV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 474 PR---GEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 548
Cdd:cd12117 328 PPgvpGELYVGGDGLALGYLNRPALTAERFVADpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR-GFRIELGEIE 406
|
....*..
gi 75992927 549 AALKNCP 555
Cdd:cd12117 407 AALRAHP 413
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
208-670 |
3.59e-17 |
|
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: 85.18 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 208 SVEELGAKPENLSVPPSRP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKD-TYIGYLPLAHvl 284
Cdd:cd05921 142 SFAELAATPPTAAVDAAFAavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNH-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 285 eltaeiscfTYGCRIGYSspLTLSDQSS-KIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyvqkt 357
Cdd:cd05921 220 ---------TFGGNHNFN--LVLYNGGTlYIDDG--------KPmpggfeETLRNLREISPTVYFNV------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 358 lfKIGYDYKLEQIKKgyDAPLCNLiLFKkvkallggNVRMMLSGGAPLSPQT-------------HRFmnvcfccPIGQG 424
Cdd:cd05921 268 --PAGWEMLVAALEK--DEALRRR-FFK--------RLKLMFYAGAGLSQDVwdrlqalavatvgERI-------PMMAG 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 425 YGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLkdwqeggYTVHDKPnprgEIVIGGQNISMGYFKNEEKTAEDYcvDE 504
Cdd:cd05921 328 LGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKY----EVRVKGPNVTPGYWRQPELTAQAF--DE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 505 NGqrWFCTGDIGEF----HPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNC--PLIDNIcAFAKSDQSYVISFVVPN 578
Cdd:cd05921 395 EG--FYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRARAVAAcaPLVHDA-VVAGEDRAEVGALVFPD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 579 QKKLTLLAQqkgvegswvdicNNPAMEAEILK--EIREAANAMkLERFE--------IPIKVRLSPEPWTPETGLVTDAF 648
Cdd:cd05921 472 LLACRRLVG------------LQEASDAEVLRhaKVRAAFRDR-LAALNgeatgsssRIARALLLDEPPSIDKGEITDKG 538
|
490 500
....*....|....*....|..
gi 75992927 649 KLKRKELKNHYLKDIERMYGGK 670
Cdd:cd05921 539 YINQRAVLERRAALVERLYADT 560
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
230-577 |
4.02e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 84.94 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI-----GYSS 303
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYHGHGLIAALlATLASGGAVllparGRFS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 304 PLTLSDqsskikkgskgDCTVLKPTLMAAVPeimdriyknvmskvqemnyvqkTLFKIGYDYKLEQIKKGYDAPLcnlil 383
Cdd:PRK05852 256 AHTFWD-----------DIKAVGATWYTAVP----------------------TIHQILLERAATEPSGRKPAAL----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 384 fkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDY--------TTGRVG---APLI 452
Cdd:PRK05852 298 ------------RFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIgqtenpvvSTGLVGrstGAQI 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 453 ccEIKLKDWQEGGytvhdkPNPRGEIVIGGQNISMGYFKNEEKTAEDYCvdeNGqrWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PRK05852 366 --RIVGSDGLPLP------AGAVGEVWLRGTTVVRGYLGDPTITAANFT---DG--WLRTGDLGSLSAAGDLSIRGRIKE 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 75992927 533 LVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVP 577
Cdd:PRK05852 433 LIN-RGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
214-583 |
8.78e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 83.92 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 214 AKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCE-------RIPGLGPKDTYIGYLPLAHVLEL 286
Cdd:PRK07059 189 AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-QMEawlqpafEKKPRPDQLNFVCALPLYHIFAL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 287 TAeisCFTYGCRIGYSSPLTLS--DQSSKIKKGSKgdctvLKPTLMAAVpeimdriyknvmskvqemnyvqKTLfkigyd 364
Cdd:PRK07059 268 TV---CGLLGMRTGGRNILIPNprDIPGFIKELKK-----YQVHIFPAV----------------------NTL------ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 365 ykleqikkgYDAPLCN----LILFKKVKALLGGnvrmmlsGGAPLSPQTHRFMNVCfCCPIGQGYGLTESCGAGTV--TE 438
Cdd:PRK07059 312 ---------YNALLNNpdfdKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCnpVD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 439 VTDYTtGRVGAPLICCEIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEF 518
Cdd:PRK07059 375 ATEFS-GTIGLPLPSTEVSIRD--DDGNDL--PLGEPGEICIRGPQVMAGYWNRPDETAK--VMTADG--FFRTGDVGVM 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 519 HPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQ---SYVISFVVPNQKKLT 583
Cdd:PRK07059 446 DERGYTKIVDRKKDMI-LVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEhsgEAVKLFVVKKDPALT 512
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
229-656 |
1.30e-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: 82.77 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLTLS 308
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPT-AAYWLGLRPDDIH-----------WNIADPGWAKGAWSSFFGPWLLG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 309 dqsskikkgskgdCTVLKPTLMAAVPEimdRIYKnVMSKvqemnyvqktlfkigydyklEQIKKGYDAPlcnlILFKKVK 388
Cdd:cd05972 149 -------------ATVFVYEGPRFDAE---RILE-LLER--------------------YGVTSFCGPP----TAYRMLI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 389 ALLG-----GNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQE 463
Cdd:cd05972 188 KQDLssykfSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 464 GGYTvhdKPNPRGEIVIGGQNISM--GYFKNEEKTAEDYCVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEY 541
Cdd:cd05972 267 GREL---PPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD-----YYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 542 VSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVpnqkkltllaQQKGVEGSwvdicnnPAMEAEILKEIREaana 618
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRgevVKAFVV----------LTSGYEPS-------EELAEELQGHVKK---- 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 75992927 619 mKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELK 656
Cdd:cd05972 397 -VLAPYKYPREIEFVEElPKTI-SG------KIRRVELR 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-577 |
1.89e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.24 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 164
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-- 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ellESKLKAALVDincvkhiiYVDNKTINRAeyPEGLEIHSmqsveelgakpenlsvPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 3161 ---QSHLRLPLAQ--------GVQVLDLDRG--DENYAEAN----------------PAIRTMPENLAYVIYTSGSTGKP 3211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLI--AGMTGQCEripGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQsskikkgskgdc 322
Cdd:PRK12316 3212 KGVGIRHSALSnhLCWMQQAY---GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP------------ 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 323 tvlkptlmAAVPEIMDRIYKNVMSKVQEMNYVqktlfkigydykleqikkgydaplcnliLFKKVKALLGGNVRMMLSGG 402
Cdd:PRK12316 3277 --------ALLVELINSEGVDVLHAYPSMLQA----------------------------FLEEEDAHRCTSLKRIVCGG 3320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 403 APLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEVTDYTTGR--VGAPLICCEIKLKDwqeggytVHDKPNPRG---E 477
Cdd:PRK12316 3321 EALPADLQQQVFAGL--PLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-------GSLEPVPVGalgE 3391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 478 IVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCP 555
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLTAERFVPDpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHP 3470
|
490 500
....*....|....*....|..
gi 75992927 556 LIDNICAFAKSDQSyVISFVVP 577
Cdd:PRK12316 3471 WVREAVVLAVDGRQ-LVAYVVP 3491
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
85-577 |
2.26e-16 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 82.10 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITsv 164
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ellesklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgaKPENLsvppsrptpsdmAIVMYTSGSTGRP 244
Cdd:cd17644 104 --------------------------------------------------QPENL------------AYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDtyigylplaHVLELtaeiSCFTYGCRIGYSSPLTLSdqsskikkgskGDCTV 324
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEY-GITSSD---------RVLQF----ASIAFDVAAEEIYVTLLS-----------GATLV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LKPTLMAAVPEIMdriyknvMSKVQEMnyvQKTLFKIGYDYKLEQIKKGydaplcnlilfKKVKALLGGNVRMMLSGGAP 404
Cdd:cd17644 177 LRPEEMRSSLEDF-------VQYIQQW---QLTVLSLPPAYWHLLVLEL-----------LLSTIDLPSSLRLVIVGGEA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 405 LSPQTH-----------RFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGR-----VGAPLICCEIKLKDwqeggytV 468
Cdd:cd17644 236 VQPELVrqwqknvgnfiQLINV---------YGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-------E 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 469 HDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD----ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEY 541
Cdd:cd17644 300 NLQPVPvgvPGELHIGGVGLARGYLNRPELTAEKFISHpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIR-GFR 378
|
490 500 510
....*....|....*....|....*....|....*....
gi 75992927 542 VSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVIVREDQPgnkRLVAYIVP 417
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
207-557 |
3.16e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 81.78 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 207 QSVEELGAKPENlSVPPSRPTpsdmaIVMYTSGSTGRPKGVMMHHSNLIA-----GMTGQceripgLGPKDTYIGYLPLA 281
Cdd:PRK09088 119 ASADALEPADTP-SIPPERVS-----LILFTSGTSGQPKGVMLSERNLQQtahnfGVLGR------VDAHSSFLCDAPMF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 282 HVLELTAEI-SCFTYGCRI----GYSSPLTLsdqsskikkGSKGDCTvLKPTLMAAVPEIMDRIyknvmskvqemnyvqk 356
Cdd:PRK09088 187 HIIGLITSVrPVLAVGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAF---------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 357 tlfkigydykleQIKKGYDAplcnlilfkkvKALlgGNVRMMLSGGAPlSPQTHRFMNVCFCCPIGQGYGLTEscgAGTV 436
Cdd:PRK09088 241 ------------RAQPGFDA-----------AAL--RHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSE---AGTV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 437 ------TEVTDYTTGRVGAPLICCEIKLKDWQEggytvHD-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvDENGqrW 509
Cdd:PRK09088 292 fgmsvdCDVIRAKAGAAGIPTPTVQTRVVDDQG-----NDcPAGVPGELLLRGPNLSPGYWRRPQATARAF--TGDG--W 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 75992927 510 FCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLI 557
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
230-551 |
3.48e-16 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 81.35 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYigylplahvleLTAEISCFTYGCRIGYSSPLtlsd 309
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRV-----------FSSAKMFFGYGLGNSLWFPL---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 310 qsskikkgSKGDCTVLKPTlmAAVPEimdriykNVMSKVQEMnyvQKTLFkigydykleqikkgYDAP--LCNLILFKKV 387
Cdd:cd05919 157 --------AVGASAVLNPG--WPTAE-------RVLATLARF---RPTVL--------------YGVPtfYANLLDSCAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 388 KALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYT 467
Cdd:cd05919 203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD--EEGHT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 468 VhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdeNGQrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKV 547
Cdd:cd05919 281 I--PPGEEGDLLVRGPSAAVGYWNNPEKSRATF----NGG-WYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEV 352
|
....
gi 75992927 548 EAAL 551
Cdd:cd05919 353 ESLI 356
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
227-656 |
4.72e-16 |
|
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: 81.26 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCE---RIPGLGPKDTYIGYLPL---AHVLELTAEISCftygcrig 300
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQataERYGLTPGDRELQFASFnfdGAHEQLLPPLIC-------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 301 ysspltlsdqsskikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmskvQEMNYVQktlFKIGYDYKLeqikkgydaplcn 380
Cdd:cd17649 160 -------------------GACVVLRPDELWASADELAEMVRE-----LGVTVLD---LPPAYLQQL------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 381 LILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGR-----VGAPLicce 455
Cdd:cd17649 200 AEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLF-NAYGPTEATVTPLVWKCEAGAARAgasmpIGRPL---- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 456 iklkdwqeGGYTVH--DK------PNPRGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCL 524
Cdd:cd17649 275 --------GGRSAYilDAdlnpvpVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgAPGSRLYRTGDLARWRDDGVI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 525 QIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS--YVISFVVPNQkkltllaqqkgvegswvdicnnP 602
Cdd:cd17649 347 EYLGRVDHQVKIR-GFRIELGEIEAALLEHPGVREAAVVALDGAGgkQLVAYVVLRA----------------------A 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 603 AMEAEILKEIReAANAMKLERFEIPIK-VRLSPEPWTPETglvtdafKLKRKELK 656
Cdd:cd17649 404 AAQPELRAQLR-TALRASLPDYMVPAHlVFLARLPLTPNG-------KLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
227-577 |
5.60e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 80.82 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPglgpKDTyigylpLAHVLELTA---EISCF------TYGC 297
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFS----AEE------LAGVLASTSicfDLSVFelfgplATGG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 298 RIGY-SSPLTLSDQSSKikkgskgdCTVlkpTLMAAVPEIMDRIyknvmskvqemnyvqktlfkigydykLEQikkgyDA 376
Cdd:cd12115 173 KVVLaDNVLALPDLPAA--------AEV---TLINTVPSAAAEL--------------------------LRH-----DA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 377 plcnlilfkkvkalLGGNVRMMLSGGAPLS----------PQTHRFMNVcfccpigqgYGLTESCGAGTVTEVTDYTTGR 446
Cdd:cd12115 211 --------------LPASVRVVNLAGEPLPrdlvqrlyarLQVERVVNL---------YGPSEDTTYSTVAPVPPGASGE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 447 V--GAPLicceiklkdwqeGGYTV-----HDKPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGD 514
Cdd:cd12115 268 VsiGRPL------------ANTQAyvldrALQPVPlgvPGELYIGGAGVARGYLGRPGLTAERFLPDpfGPGARLYRTGD 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992927 515 IGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd12115 336 LVRWRPDGLLEFLGRADNQVKVR-GFRIELGEIEAALRSIPGVREAVVVAIGDAAgerRLVAYIVA 400
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
228-656 |
6.51e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 81.38 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVleltaeiscftyGcriGYSSPLTL 307
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIA-IVGYGEDDVYLHTAPLCHI------------G---GLSSALAM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 308 SdqsskikkgSKGDCTVLKPTLMA-AVPEIMDRIYKNVMSKVQEMnyvqktlfkigydykleqikkgydapLCNLILFKK 386
Cdd:PLN02860 235 L---------MVGACHVLLPKFDAkAALQAIKQHNVTSMITVPAM--------------------------MADLISLTR 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 387 VKALLGGN--VRMMLSGGAPLSPQTHRFMNVCF-CCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPL-ICCEIKLKDWQ 462
Cdd:PLN02860 280 KSMTWKVFpsVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLqTVNQTKSSSVH 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 463 EGGYTVHDKPNPRGEIVIG-------------GQNISMGYFKNEEKTAEDyCVDENgqrWFCTGDIGEFHPDGCLQIIDR 529
Cdd:PLN02860 360 QPQGVCVGKPAPHVELKIGldessrvgriltrGPHVMLGYWGQNSETASV-LSNDG---WLDTGDIGWIDKAGNLWLIGR 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 530 KKDLVKlQAGEYVSLGKVEAALKNCP--------------LIDNICAFAKSDQSYVISFV-VPNQKKLTLLAQQkgvegs 594
Cdd:PLN02860 436 SNDRIK-TGGENVYPEEVEAVLSQHPgvasvvvvgvpdsrLTEMVVACVRLRDGWIWSDNeKENAKKNLTLSSE------ 508
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75992927 595 wvdicnnpameaeilkEIREAANAMKLERFEIP--IKVRLSPEPWTpETGlvtdafKLKRKELK 656
Cdd:PLN02860 509 ----------------TLRHHCREKNLSRFKIPklFVQWRKPFPLT-TTG------KIRRDEVR 549
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
225-583 |
7.01e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 81.25 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 225 RP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERI--PGLGP-KDTYIGYLPLAHVLELTaeISCFTYgcri 299
Cdd:PRK08974 200 KPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QAKAAygPLLHPgKELVVTALPLYHIFALT--VNCLLF---- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 300 gysspltlsdqsskIKKGSKGdctvLKPTLMAAVPEIMDRIYKNVMSKVQEMNyvqkTLFKigydykleqikkgydaPLC 379
Cdd:PRK08974 273 --------------IELGGQN----LLITNPRDIPGFVKELKKYPFTAITGVN----TLFN----------------ALL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 380 NLILFKKVKAllgGNVRMMLSGGAPL-SPQTHRFMNVCfCCPIGQGYGLTEsCG---AGTVTEVTDYTtGRVGAPLICCE 455
Cdd:PRK08974 315 NNEEFQELDF---SSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTE-CSplvSVNPYDLDYYS-GSIGLPVPSTE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 456 IKLKDwQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVk 535
Cdd:PRK08974 389 IKLVD-DDGNEVPPGEP---GELWVKGPQVMLGYWQRPEATDE---VIKDG--WLATGDIAVMDEEGFLRIVDRKKDMI- 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 75992927 536 LQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFVVPNQKKLT 583
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLT 509
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
77-659 |
1.29e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 79.98 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 77 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESE 156
Cdd:PRK08316 30 LVFGDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 157 ASYLITSVELLEsKLKAALVDINCVKHIiyVDNKTINRaEYPEGleihsMQSVEELgAKPENLSVPPSRPTPSDMAIVMY 236
Cdd:PRK08316 109 ARAFLVDPALAP-TAEAALALLPVDTLI--LSLVLGGR-EAPGG-----WLDFADW-AEAGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 237 TSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvlelTAEISCFTygcrigysSPLTLSDQSSKIkk 316
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVS-CIVAGDMSADDIPLHALPLYH----CAQLDVFL--------GPYLYVGATNVI-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 317 gskgdctVLKPTLmaavPEIMDRIYKnvmskvqemnYVQKTLFK-----IG------YD-YKLEQIKKGYdaplcnlilf 384
Cdd:PRK08316 244 -------LDAPDP----ELILRTIEA----------ERITSFFApptvwISllrhpdFDtRDLSSLRKGY---------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 385 kkvkallggnvrmmlsGGAPLSPQT------HRFMNVCF--CcpigqgYGLTESCGAGTV--TEVTDYTTGRVGAPLICC 454
Cdd:PRK08316 293 ----------------YGASIMPVEvlkelrERLPGLRFynC------YGQTEIAPLATVlgPEEHLRRPGSAGRPVLNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 455 EIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK08316 351 ETRVVD--DDGNDV--APGEVGEIVHRSPQLMLGYWDDPEKTAEAF---RGG--WFHSGDLGVMDEEGYITVVDRKKDMI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 535 KlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPnqkkltllaqqkgVEGSWVDicnnpamEAEILKE 611
Cdd:PRK08316 422 K-TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWieaVTAVVVP-------------KAGATVT-------EDELIAH 480
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 75992927 612 IREaanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKNHY 659
Cdd:PRK08316 481 CRA-----RLAGFKVPKRVIFVDElPRNP-SG------KILKRELRERY 517
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-578 |
1.38e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.36 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLEIHSM-QSVEELGAKPEnlSVPPSRPTPSDMAIVMYTSGSTGR 243
Cdd:PRK12467 1680 HLQA-------------------------RLPLPDGLRSLVLdQEDDWLEGYSD--SNPAVNLAPQNLAYVIYTSGSTGR 1732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 244 PKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaEISCFtygcriGYSSPLTlsdqsskikkgsKGDCT 323
Cdd:PRK12467 1733 PKGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAF------DVSVW------ELFWPLI------------NGARL 1787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 324 VLKPTLMAAVPE-IMDRIYKNvmsKVQEMNYVQKTLfkigydYKLEQIKKGYDAPLcnlilfkkvkallggNVRMMLSGG 402
Cdd:PRK12467 1788 VIAPPGAHRDPEqLIQLIERQ---QVTTLHFVPSML------QQLLQMDEQVEHPL---------------SLRRVVCGG 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 403 APLSPQTHR-FMNVCFCCPIGQGYGLTEscgagTVTEVTDYT------TGRVGAPLiccEIKLKDWqeGGYTVHDKPNPR 475
Cdd:PRK12467 1844 EALEVEALRpWLERLPDTGLFNLYGPTE-----TAVDVTHWTcrrkdlEGRDSVPI---GQPIANL--STYILDASLNPV 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 476 -----GEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 547
Cdd:PRK12467 1914 pigvaGELYLGGVGLARGYLNRPALTAERFVADpfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEI 1992
|
490 500 510
....*....|....*....|....*....|...
gi 75992927 548 EAALKNCPLIDNICAFAK--SDQSYVISFVVPN 578
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQdgANGKQLVAYVVPT 2025
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-577 |
1.56e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.16 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsklkaaLVDINCVKHIIYVDNKTINRAEYPEGleihsmqsveelgakpenlsVPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 617 HLGR------KLPLAAGVQVLDLDRPAAWLEGYSEE--------------------NPGTELNPENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkgskgdctv 324
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRD--------------- 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 lkptlMAAVPEIMDRIYKNVMSKVQEMnyvqktlfkigydykleqikkgydapLCNLILFKKVKALLggNVRMMLSGGAP 404
Cdd:PRK12316 735 -----PAKLVELINREGVDTLHFVPSM--------------------------LQAFLQDEDVASCT--SLRRIVCSGEA 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 405 LS-----------PQTHRFmNVcfccpigqgYGLTESCGAGT----VTEVTDytTGRVGAPLICCEIKLKDWQEGgytvh 469
Cdd:PRK12316 782 LPadaqeqvfaklPQAGLY-NL---------YGPTEAAIDVThwtcVEEGGD--SVPIGRPIANLACYILDANLE----- 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 470 dkPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVDE--NGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSL 544
Cdd:PRK12316 845 --PVPvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRIEL 921
|
490 500 510
....*....|....*....|....*....|...
gi 75992927 545 GKVEAALKNCPLIDNICAFAKSDQSYViSFVVP 577
Cdd:PRK12316 922 GEIEARLLEHPWVREAAVLAVDGKQLV-GYVVL 953
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
208-669 |
2.38e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 79.54 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 208 SVEELGAKPENLSVPPS--RPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPGLGPKdTYIGYLPLAHV 283
Cdd:PRK08180 186 PFAALLATPPTAAVDAAhaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqMLAQTFPFLAEEPP-VLVDWLPWNHT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 284 LeltaeiscftygcriGYSSPLTLsdqsskikkgskgdctVL-----------KPTlmaavPEIMDRIYKNvmskvqeMN 352
Cdd:PRK08180 265 F---------------GGNHNLGI----------------VLynggtlyiddgKPT-----PGGFDETLRN-------LR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 353 YVQKTLF---KIGYDYKLEQIKKgyDAPLCNLiLFKKVkallggnvRMMLSGGAPLSPQT----HRF-MNVC-----FCC 419
Cdd:PRK08180 302 EISPTVYfnvPKGWEMLVPALER--DAALRRR-FFSRL--------KLLFYAGAALSQDVwdrlDRVaEATCgerirMMT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 420 pigqGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqeggytVHDKPnprgEIVIGGQNISMGYFKNEEKTAED 499
Cdd:PRK08180 371 ----GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVP-------VGGKL----EVRVKGPNVTPGYWRAPELTAEA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 500 YcvDENGqrWFCTGDIGEFH-PDgclqiiDRKKDLV---------KLQAGEYVSLG----KVEAALKncPLIDNICaFAK 565
Cdd:PRK08180 436 F--DEEG--YYRSGDAVRFVdPA------DPERGLMfdgriaedfKLSSGTWVSVGplraRAVSAGA--PLVQDVV-ITG 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 566 SDQSYVISFVVPNQKKLTLLAQQkGVEGSWVDICNNPAMEA---EILKEIREAA--NAMKLERfeipikVRLSPEPWTPE 640
Cdd:PRK08180 503 HDRDEIGLLVFPNLDACRRLAGL-LADASLAEVLAHPAVRAafrERLARLNAQAtgSSTRVAR------ALLLDEPPSLD 575
|
490 500 510
....*....|....*....|....*....|....*.
gi 75992927 641 TGLVTD-------AFKLKRKELknhylkdIERMYGG 669
Cdd:PRK08180 576 AGEITDkgyinqrAVLARRAAL-------VEALYAD 604
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
236-655 |
2.41e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 79.50 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 236 YTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHvleltAEISCFTYGCRIGYSSPLTLSDQSSKIK 315
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYL-MALSNALIWGMNEGAVYLWTLPMFH-----CNGWCFTWTLAALCGTNICLRQVTAKAI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 316 KGSKGDCTVlkpTLMAAVPEIMDRIYknvmskvqemnyvqktlfkigydykleqikkgyDAPLCNLILfkkvkaLLGGNV 395
Cdd:PLN02479 276 YSAIANYGV---THFCAAPVVLNTIV---------------------------------NAPKSETIL------PLPRVV 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 396 RMMLSGGAP-------LSPQTHRfmnvcfccpIGQGYGLTESCGAGTVT-------EVTDYTTGRVGAPLICCEIKLKdw 461
Cdd:PLN02479 314 HVMTAGAAPppsvlfaMSEKGFR---------VTHTYGLSETYGPSTVCawkpewdSLPPEEQARLNARQGVRYIGLE-- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 462 qegGYTVHD----KPNPR-----GEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKD 532
Cdd:PLN02479 383 ---GLDVVDtktmKPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF---ANG--WFHSGDLGVKHPDGYIEIKDRSKD 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 533 LVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVIS---FVVPNQKkltllaqqkgvegswVDICNNPAMEAEIL 609
Cdd:PLN02479 455 II-ISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESpcaFVTLKPG---------------VDKSDEAALAEDIM 518
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 75992927 610 KEIREaanamKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKEL 655
Cdd:PLN02479 519 KFCRE-----RLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEM 559
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
228-534 |
2.89e-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: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcriGYSSPLTl 307
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE-WKTKDRILSWMPLTHDMGLIA-----------FHLAPLI- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 308 sdqsskikkgsKGDCTVLKPTLMAAVPEImdriykNVMSKVQEMNYVQKTLFKIGYDYKLEQIK--KGYDAPLcnlilfk 385
Cdd:cd05908 172 -----------AGMNQYLMPTRLFIRRPI------LWLKKASEHKATIVSSPNFGYKYFLKTLKpeKANDWDL------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 386 kvkallgGNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQG-----YGLTE-SCGA---------------------GTVT 437
Cdd:cd05908 228 -------SSIRMILNGAEPIDYElCHEFLDHMSKYGLKRNailpvYGLAEaSVGAslpkaqspfktitlgrrhvthGEPE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 438 EVTD------YTTGRVGAPLICCEIKLKDWQ----EGGYTvhdkpnprGEIVIGGQNISMGYFKNEEKTAEdyCVDENGq 507
Cdd:cd05908 301 PEVDkkdsecLTFVEVGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEATAK--VFTDDG- 369
|
330 340
....*....|....*....|....*..
gi 75992927 508 rWFCTGDIGeFHPDGCLQIIDRKKDLV 534
Cdd:cd05908 370 -WLKTGDLG-FIRNGRLVITGREKDII 394
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
227-583 |
4.56e-15 |
|
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: 78.21 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPlAHVLELTAEiscftygcrigyssPLT 306
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFS-NYVFDFFVE--------------QMT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LSDQSskikkgskGDCTVLKPTLMAAVPeimDRIYKnVMSKvQEMNYVQKTlfkigyDYKLEQikkgYDAPLCNlilfkk 386
Cdd:cd17648 157 LALLN--------GQKLVVPPDEMRFDP---DRFYA-YINR-EKVTYLSGT------PSVLQQ----YDLARLP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 387 vkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgagTVTE-VTDYTTGRVGAPLICCEIKLKDWqegg 465
Cdd:cd17648 208 -------HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET----TVTNhKRFFPGDQRFDKSLGRPVRNTKC---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 466 YTVHD--KPNP---RGEIVIGGQNISMGYFKNEEKTAEDYC----------VDENGQRWFCTGDIGEFHPDGCLQIIDRK 530
Cdd:cd17648 273 YVLNDamKRVPvgaVGELYLGGDGVARGYLNRPELTAERFLpnpfqteqerARGRNARLYKTGDLVRWLPSGELEYLGRN 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75992927 531 KDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSD--------QSYVISFVVPNQKKLT 583
Cdd:cd17648 353 DFQVKIR-GQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriQKYLVGYYLPEPGHVP 412
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
83-534 |
4.97e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 78.54 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 83 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYL-- 160
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlc 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ----------ITSVELLESKLKAALVD-INCVKHIIY--VDNKTINR-AEYPEGLEIHSMQSVEelgaKPENLSVPPSRP 226
Cdd:PRK06710 128 ldlvfprvtnVQSATKIEHVIVTRIADfLPFPKNLLYpfVQKKQSNLvVKVSESETIHLWNSVE----KEVNTGVEVPCD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG-MTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCftygcrigysspl 305
Cdd:PRK06710 204 PENDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNL------------- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 306 tlsdqssKIKKGSKgdctvlkptlMAAVPEI-MDRIYKNVMSKvqemnyvQKTLFKigydykleqikkgyDAPLCNLILF 384
Cdd:PRK06710 271 -------SIMQGYK----------MVLIPKFdMKMVFEAIKKH-------KVTLFP--------------GAPTIYIALL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 385 KK--VKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT----DYTTGRVGAPLICCEIKL 458
Cdd:PRK06710 313 NSplLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES---SPVTHSNflweKRVPGSIGVPWPDTEAMI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992927 459 KDWQEGGYTvhdKPNPRGEIVIGGQNISMGYFKNEEKTAedyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK06710 390 MSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETA---AVLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMI 457
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
222-551 |
9.17e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 77.34 E-value: 9.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltaeiscftYGCRIGY 301
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW-QWTADDVLVHGLPLFHV-----------HGLVLGV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 302 SSPLTLSDQSSKIKKGSK---GDCTVLKPTLMAAVPEIMDRIYKNVmskvqemnyvqktlfkigydykleqikkgyDAPl 378
Cdd:PRK07787 189 LGPLRIGNRFVHTGRPTPeayAQALSEGGTLYFGVPTVWSRIAADP------------------------------EAA- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 379 cnlilfkkvKALlgGNVRMMLSGGAPLS-PQTHRFMNVCFCCPIgQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIK 457
Cdd:PRK07787 238 ---------RAL--RGARLLVSGSAALPvPVFDRLAALTGHRPV-ERYGMTETLITLSTRADGERRPGWVGLPLAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 458 LKDwQEGGYTVHDkPNPRGEIVIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKK-DLVKl 536
Cdd:PRK07787 306 LVD-EDGGPVPHD-GETVGELQVRGPTLFDGYLNRPDATAA--AFTADG--WFRTGDVAVVDPDGMHRIVGREStDLIK- 378
|
330
....*....|....*.
gi 75992927 537 qAGEY-VSLGKVEAAL 551
Cdd:PRK07787 379 -SGGYrIGAGEIETAL 393
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
228-569 |
1.74e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.06 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTaeISCFT---YGCRIG-YSS 303
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFGLT--VGLFTpllTGAEVFlYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 304 PL-------TLSDQsskikkgskgDCTVL--KPTLMAavpeimdriyknvmskvqemNYVQktlFKIGYDYkleqikkgy 374
Cdd:PRK08043 441 PLhyrivpeLVYDR----------NCTVLfgTSTFLG--------------------NYAR---FANPYDF--------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 375 daplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-----------SCGAGTVTEVTDYT 443
Cdd:PRK08043 479 ------------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEcapvvsinvpmAAKPGTVGRILPGM 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 444 TGRVgaplicceIKLKDWQEGgytvhdkpnprGEIVIGGQNISMGYFKNEE------KTAEdycvDENGQR---WFCTGD 514
Cdd:PRK08043 541 DARL--------LSVPGIEQG-----------GRLQLKGPNIMNGYLRVEKpgvlevPTAE----NARGEMergWYDTGD 597
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 75992927 515 IGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEA-ALKNCPLIDNiCAFAKSDQS 569
Cdd:PRK08043 598 IVRFDEQGFVQIQGRAKRFAKI-AGEMVSLEMVEQlALGVSPDKQH-ATAIKSDAS 651
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-579 |
2.16e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.51 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLeihSMQSVEELGAKPENLSV--PPSRPTPSDMAIVMYTSGSTG 242
Cdd:PRK12467 618 HLLA-------------------------QLPVPAGL---RSLCLDEPADLLCGYSGhnPEVALDPDNLAYVIYTSGSTG 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 243 RPKGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDC 322
Cdd:PRK12467 670 QPKGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGV 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 323 TVLKptlmaAVPeimdriyknvmSKVQEMnyvqktlfkigydykLEQIKKGYDAPLCNLIlfkkvkalLGGNVrMMLSGG 402
Cdd:PRK12467 749 TVLK-----IVP-----------SHLQAL---------------LQASRVALPRPQRALV--------CGGEA-LQVDLL 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 403 AP---LSPQThRFMNVcfccpigqgYGLTEscgagTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNP----- 474
Cdd:PRK12467 789 ARvraLGPGA-RLINH---------YGPTE-----TTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPvpvgv 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 475 RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAAL 551
Cdd:PRK12467 854 VGELYIGGAGLARGYHRRPALTAERFVPDpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR-GFRIELGEIEARL 932
|
490 500 510
....*....|....*....|....*....|
gi 75992927 552 KNCPLIDN--ICAFAKSDQSYVISFVVPNQ 579
Cdd:PRK12467 933 LAQPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-577 |
2.22e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsklkaalvdincvkhiiyvdnktinRAEYPEGLEIHSMQSVEELGAKPEnlSVPPSRPTPSDMAIVMYTSGSTGRP 244
Cdd:PRK12316 2109 HLLE-------------------------RLPLPAGVARLPLDRDAEWADYPD--TAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAhvLELTAEiSCFTygcrigyssPLTlsdqsskikkgsKGDCTV 324
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS--FDGAHE-QWFH---------PLL------------NGARVL 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LKPTLMAAVPEIMDRIYKNVMSKVqemnyvqktlfkigydykleqikkgyDAPLCNLILFKKVKALLGG--NVRMMLSGG 402
Cdd:PRK12316 2217 IRDDELWDPEQLYDEMERHGVTIL--------------------------DFPPVYLQQLAEHAERDGRppAVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 403 ----APLSPQTHRFMNVCFccpIGQGYGLTEscgagTVTEVTDYTTGRV---GAPLICCEIKLKDwqEGGYTVHDKPNP- 474
Cdd:PRK12316 2271 eavpAASLRLAWEALRPVY---LFNGYGPTE-----AVVTPLLWKCRPQdpcGAAYVPIGRALGN--RRAYILDADLNLl 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 475 ----RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKV 547
Cdd:PRK12316 2341 apgmAGELYLGGEGLARGYLNRPGLTAERFVPDpfsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR-GFRIELGEI 2419
|
490 500 510
....*....|....*....|....*....|..
gi 75992927 548 EAALKNCPLIDNICAFAKSDQS--YVISFVVP 577
Cdd:PRK12316 2420 EARLQAHPAVREAVVVAQDGASgkQLVAYVVP 2451
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
227-577 |
3.31e-14 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 75.37 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAeisCFTYGCR--IGY 301
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF-DVGPGSRVLQFASPsfdASVWELLM---ALLAGATlvLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 302 SSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEimdriyknvmskvqemnyvqktlfkigydykleqikkgydaplcnl 381
Cdd:cd17652 167 AEELLPGEPLADLLREHRITHVTLPPAALAALPP---------------------------------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 382 ilfkkvKALLGGnvRMMLSGGAPLSPQ-------THRFMNvcfccpigqGYGLTESCGAGTVTEV-TDYTTGRVGAPLIC 453
Cdd:cd17652 201 ------DDLPDL--RTLVVAGEACPAElvdrwapGRRMIN---------AYGPTETTVCATMAGPlPGGGVPPIGRPVPG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 454 CEIK-LKDWQEggytvhdkPNP---RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQI 526
Cdd:cd17652 264 TRVYvLDARLR--------PVPpgvPGELYIAGAGLARGYLNRPGLTAERFVADpfgAPGSRMYRTGDLARWRADGQLEF 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 75992927 527 IDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYV---ISFVVP 577
Cdd:cd17652 336 LGRADDQVKIR-GFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDkrlVAYVVP 388
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
228-577 |
3.81e-14 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 75.28 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIagmtGQCEripglgpkdtyigylplahvleltAEISCFTygcrigysspLTL 307
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCE------------------------WHRPYFG----------VTP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 308 SDQSSKIKkGSKGDCTVLK--PTLMA-AVPEIMDRIYKNVMSKVQEmnYVQKTLFKIGYdykleqikkgYDAPLCnlilf 384
Cdd:cd17645 145 ADKSLVYA-SFSFDASAWEifPHLTAgAALHVVPSERRLDLDALND--YFNQEGITISF----------LPTGAA----- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 385 KKVKALLGGNVRMMLSGGAPLSpqthRFMNVCFccPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIKL--KDW 461
Cdd:cd17645 207 EQFMQLDNQSLRVLLTGGDKLK----KIERKGY--KLVNNYGPTENTVVATSFEIdKPYANIPIGKPIDNTRVYIldEAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 462 QEGGYTVhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaG 539
Cdd:cd17645 281 QLQPIGV------AGELCIAGEGLARGYLNRPELTAEKFIVHpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR-G 353
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 75992927 540 EYVSLGKVEAALKNCPLIDNICAFAKSD---QSYVISFVVP 577
Cdd:cd17645 354 YRIEPGEIEPFLMNHPLIELAAVLAKEDadgRKYLVAYVTA 394
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
103-567 |
9.41e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 74.23 E-value: 9.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 103 ALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGREAVV-------------HGLNESEASYLITSVELLEs 169
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAY-------------YAILRANAVVvpvnpmnreeelaHYVTDSGARVAIVGSELAP- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 170 KLKAALVDINcVKHIIYVDNKTINRAEY----PEGLEI-HSMQSVEELGAKP------ENLSVPPSRPTPSDMAIVMYTS 238
Cdd:PRK08314 121 KVAPAVGNLR-LRHVIVAQYSDYLPAEPeiavPAWLRAePPLQALAPGGVVAwkealaAGLAPPPHTAGPDDLAVLPYTS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 239 GSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLeltaeiscftyGCRIGYSSPLTLsdqsskikkgs 318
Cdd:PRK08314 200 GTTGVPKGCMHTHRTVMANAVGSV-LWSNSTPESVVLAVLPLFHVT-----------GMVHSMNAPIYA----------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 319 kGDCTVLKPTL-MAAVPEIMDRIYKNVMSKVQEMnyVQKTLFKIGYDykleqikkGYDapLCNLilfkkvkALLGGnvrm 397
Cdd:PRK08314 257 -GATVVLMPRWdREAAARLIERYRVTHWTNIPTM--VVDFLASPGLA--------ERD--LSSL-------RYIGG---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 398 mlsGGAPLsPQT-----HRFMNVCFCcpigQGYGLTESCGA-------------------GTVTEVTDYTTGRVGAplic 453
Cdd:PRK08314 313 ---GGAAM-PEAvaerlKELTGLDYV----EGYGLTETMAQthsnppdrpklqclgiptfGVDARVIDPETLEELP---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 454 ceiklkdwqeggytvhdkPNPRGEIVIGGQNISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDL 533
Cdd:PRK08314 381 ------------------PGEVGEIVVHGPQVFKGYWNRPEATAEAF-IEIDGKRFFRTGDLGRMDEEGYFFITDRLKRM 441
|
490 500 510
....*....|....*....|....*....|....
gi 75992927 534 VKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:PRK08314 442 IN-ASGFKVWPAEVENLLYKHPAIQEACVIATPD 474
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
31-578 |
1.03e-13 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 73.95 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 31 DIPGADTLDKLFDHAVAKFGKKDSLgtreilseenemqpngkVFKKLIlGNYKWINYLEVNCRVNNFGSGLTALGLKPKN 110
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVYGHKTAL-----------------IFESSG-GVVRRYSYLELNEEINRTANLFYSLGIRKGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 111 TIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLESKLKAALVDINCVKHIIyvdnk 190
Cdd:PRK08008 64 KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHIC----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 191 tINRAEYPEGLEIHSMQsvEELGAKPENLS-VPPSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLI-AGMTG--QCerip 266
Cdd:PRK08008 139 -LTRVALPADDGVSSFT--QLKAQQPATLCyAPPL--STDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSawQC---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 267 GLGPKDTYIGYLPLAHV-LELTAEISCFTYGCRI----GYSSPlTLSDQSSKIKkgskgdctvlkptlmAAVPEIMDRIY 341
Cdd:PRK08008 210 ALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFvlleKYSAR-AFWGQVCKYR---------------ATITECIPMMI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 342 KNVMSKVQEMNYVQKTLFKIGYDYKL-EQIKKGYDAPLcnlilfkkvkallggNVRMMLSggaplspqthrfmnvcfccp 420
Cdd:PRK08008 274 RTLMVQPPSANDRQHCLREVMFYLNLsDQEKDAFEERF---------------GVRLLTS-------------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 421 igqgYGLTEScgagTVTEVTDYTTGR-----VGAPLICCEIKLKDwqEGGYTVhdKPNPRGEIVIG---GQNISMGYFKN 492
Cdd:PRK08008 319 ----YGMTET----IVGIIGDRPGDKrrwpsIGRPGFCYEAEIRD--DHNRPL--PAGEIGEICIKgvpGKTIFKEYYLD 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 493 EEKTAEdyCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSD---QS 569
Cdd:PRK08008 387 PKATAK--VLEADG--WLHTGDTGYVDEEGFFYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVGIKDsirDE 461
|
....*....
gi 75992927 570 YVISFVVPN 578
Cdd:PRK08008 462 AIKAFVVLN 470
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
226-630 |
1.09e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 74.29 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 226 PTPSDMAIVM------------YTSGSTGRPKGVMMHH--------SNLIAGMTGQCEripglgpkdTYIGYLPLAHVLE 285
Cdd:PLN03102 171 PTPSLVARMFriqdehdpislnYTSGTTADPKGVVISHrgaylstlSAIIGWEMGTCP---------VYLWTLPMFHCNG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 286 LTaeiscFTYGCrigysspltlsdqsskikkGSKGDCTVLKPTLMAavPEImdriYKNV-MSKVQEMNYVqKTLFKIgyd 364
Cdd:PLN03102 242 WT-----FTWGT-------------------AARGGTSVCMRHVTA--PEI----YKNIeMHNVTHMCCV-PTVFNI--- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 365 ykleqIKKGYDAPLCNLilfkkvkallGGNVRMMLSGGAPLSPQTHRFMNVCFccPIGQGYGLTESCGAGTVTEVTD--- 441
Cdd:PLN03102 288 -----LLKGNSLDLSPR----------SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEWQDewn 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 442 --------YTTGRVGAPLIC---CEIKLKDWQEggyTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWF 510
Cdd:PLN03102 351 rlpenqqmELKARQGVSILGladVDVKNKETQE---SVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF---KHG--WL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 511 CTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPlidnicafaKSDQSYVISFVVP--NQKKLTLLAQQ 588
Cdd:PLN03102 423 NTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYP---------KVLETAVVAMPHPtwGETPCAFVVLE 492
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 75992927 589 KGVEGSWVDICNNPAMEAEILKEIREaanamKLERFEIPIKV 630
Cdd:PLN03102 493 KGETTKEDRVDKLVTRERDLIEYCRE-----NLPHFMCPRKV 529
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
95-567 |
1.81e-13 |
|
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: 72.92 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 95 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVELLEsklkaa 174
Cdd:cd05969 11 ARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 175 lvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL 254
Cdd:cd05969 85 --------------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 255 IA-GMTGQceRIPGLGPKDTYIgylplahvleLTAEISCFTyGCRIGYSSPLTlsDQSSKIKKGSKGDctvlkptlmaav 333
Cdd:cd05969 115 IFyYFTGK--YVLDLHPDDIYW----------CTADPGWVT-GTVYGIWAPWL--NGVTNVVYEGRFD------------ 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 334 PEimdRIYKNVMS-KVQEMnYVQKTLFKIGYDYKLEQIKKgYDAplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHRF 412
Cdd:cd05969 168 AE---SWYGIIERvKVTVW-YTAPTAIRMLMKEGDELARK-YDL----------------SSLRFIHSVGEPLNPEAIRW 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 413 MNVCFCCPIGQGYGLTESCGAGTVTEV-TDYTTGRVGAPLICCEIKLKDwQEGGYTvhdKPNPRGEIVIGGQNISM--GY 489
Cdd:cd05969 227 GMEVFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVD-ENGNEL---PPGTKGILALKPGWPSMfrGI 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 490 FKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:cd05969 303 WNDEERYKNSF---IDG--WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAVAEAGVIGKPD 374
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-656 |
1.86e-13 |
|
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: 72.85 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 89 EVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSVelle 168
Cdd:cd05971 11 ELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 169 sklkaalvdincvkhiiyvdnktinraeypegleihsmqsveelgakpenlsvppsrptPSDMAIVMYTSGSTGRPKGVM 248
Cdd:cd05971 87 -----------------------------------------------------------SDDPALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 249 MHHSNLIaGMTGQCERIPGLGPKDTYIGYLPlahvleltAEISCftygcrIGysspltlsdqsskikkgskGDCTVLKPT 328
Cdd:cd05971 108 HAHRVLL-GHLPGVQFPFNLFPRDGDLYWTP--------ADWAW------IG-------------------GLLDVLLPS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 329 LMAAVPEIMDRIYKnvmskvqemnYVQKTLFKIGYDYKLEQIKkgydAPLCNLILFKKVKALL---GGNVRMMLSGGAPL 405
Cdd:cd05971 154 LYFGVPVLAHRMTK----------FDPKAALDLMSRYGVTTAF----LPPTALKMMRQQGEQLkhaQVKLRAIATGGESL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 406 SPQTHRFMNVCFCCPIGQGYGLTEsCGA--GTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytVHDKPNPRGEIVIGGQ 483
Cdd:cd05971 220 GEELLGWAREQFGVEVNEFYGQTE-CNLviGNCSALFPIKPGSMGKPIPGHRVAIVD-DNG---TPLPPGEVGEIAVELP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 484 NISM--GYFKNEEKTAEDYCVDengqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNIC 561
Cdd:cd05971 295 DPVAflGYWNNPSATEKKMAGD-----WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMAA 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 562 AFAKSDQ---SYVISFVVPNQkkltllaqqkGVEGSwvdicnnpameAEILKEIREAANAmKLERFEIPIKVRLSPEPWT 638
Cdd:cd05971 369 VVGIPDPirgEIVKAFVVLNP----------GETPS-----------DALAREIQELVKT-RLAAHEYPREIEFVNELPR 426
|
570
....*....|....*...
gi 75992927 639 PETGlvtdafKLKRKELK 656
Cdd:cd05971 427 TATG------KIRRRELR 438
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
211-618 |
1.89e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.54 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 211 ELGAKPENLSVPPSRP--TPSDMAIVMYTSGSTGRPKGVMMHHSNL---IAGMTGQCERIPGLGPKDtYIGYLPLAHvle 285
Cdd:PRK12582 200 DLAATPPTAAVAAAIAaiTPDTVAKYLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPV-SLDWMPWNH--- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 286 ltaeiscfTYGCRIGYSsPLTLSDQSSKIKKGskgdctvlKP------TLMAAVPEIMDRIYKNVmskvqemnyvqktlf 359
Cdd:PRK12582 276 --------TMGGNANFN-GLLWGGGTLYIDDG--------KPlpgmfeETIRNLREISPTVYGNV--------------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 360 KIGYDYKLEQIKKgyDAPLCNLiLFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQ------GYGLTEScgA 433
Cdd:PRK12582 324 PAGYAMLAEAMEK--DDALRRS-FFK--------NLRLMAYGGATLSDDLYERMQALAVRTTGHripfytGYGATET--A 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 434 GTVTEVTDYT--TGRVGAPLICCEIKLKdwqeggytvhdkpnPRG---EIVIGGQNISMGYFKNEEKTAEDYcvDENGqr 508
Cdd:PRK12582 391 PTTTGTHWDTerVGLIGLPLPGVELKLA--------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAF--DEEG-- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 509 WFCTGDIGEF-HPDGCLQ--IID-RKKDLVKLQAGEYVSLGKVEA-ALKNC-PLIDNIcAFAKSDQSYVISFVVPNQKKL 582
Cdd:PRK12582 453 FYRLGDAARFvDPDDPEKglIFDgRVAEDFKLSTGTWVSVGTLRPdAVAACsPVIHDA-VVAGQDRAFIGLLAWPNPAAC 531
|
410 420 430
....*....|....*....|....*....|....*.
gi 75992927 583 TLLAQQKGVEGSwvDICNNPAMeAEILKEIREAANA 618
Cdd:PRK12582 532 RQLAGDPDAAPE--DVVKHPAV-LAILREGLSAHNA 564
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
209-570 |
3.00e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 72.89 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 209 VEELGAKPENLSVPPSRPtpsdmAIVMYTSGSTGRPKGVMMHHSNLiAGMTGQCERIPGLGPKDTyIGYL--PLAHVLEL 286
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSP-----ALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADINSD-VGFVgvPLFHIAGI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 287 TAEISCFTYGCRigysspltlsdqsskikkgskgdcTVLKPTLMAAVPEIMDriyknvmskVQEMNYVQkTLFKIGYDYK 366
Cdd:PRK07786 232 GSMLPGLLLGAP------------------------TVIYPLGAFDPGQLLD---------VLEAEKVT-GIFLVPAQWQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 367 L---EQIKKGYDAPLcnlilfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFccPIGQ---GYGLTEscgAGTVTEVT 440
Cdd:PRK07786 278 AvcaEQQARPRDLAL-----------------RVLSWGAAPASDTLLRQMAATF--PEAQilaAFGQTE---MSPVTCML 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 441 D-----YTTGRVGAPLICCEIKLKDwqeggYTVHD-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGD 514
Cdd:PRK07786 336 LgedaiRKLGSVGKVIPTVAARVVD-----ENMNDvPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---AGG--WFHSGD 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 75992927 515 IGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY 570
Cdd:PRK07786 406 LVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-590 |
1.11e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 71.73 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsKLKAALVDincvkHIIYVDNKTINrAEYPEGLEIHSMqsveelgakPENLsvppsrptpsdmAIVMYTSGSTGRP 244
Cdd:PRK12467 3201 HLLE-QLPAPAGD-----TALTLDRLDLN-GYSENNPSTRVM---------GENL------------AYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLAhvLELTAEISCFTYGCrigysspltlsdqsskikkgskGDCTV 324
Cdd:PRK12467 3253 KGVGVRHGAL-ANHLCWIAEAYELDANDRVLLFMSFS--FDGAQERFLWTLIC----------------------GGCLV 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LKPTLMAAvPEimdriyknvmSKVQEMNYVQKTL--FKIGYDYKLEQIKKGYDAPlcnlilfkkvkallggNVRMMLSGG 402
Cdd:PRK12467 3308 VRDNDLWD-PE----------ELWQAIHAHRISIacFPPAYLQQFAEDAGGADCA----------------SLDIYVFGG 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 403 APLSPQT-----HRFMNVCfccpIGQGYGLTEscgagTVTEVTDYTTGRVGAP-LICCEIKLKDWQEGGYTVHDKPNP-- 474
Cdd:PRK12467 3361 EAVPPAAfeqvkRKLKPRG----LTNGYGPTE-----AVVTVTLWKCGGDAVCeAPYAPIGRPVAGRSIYVLDGQLNPvp 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 475 ---RGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVE 548
Cdd:PRK12467 3432 vgvAGELYIGGVGLARGYHQRPSLTAERFVADpfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIE 3510
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75992927 549 AALKNCPLIDNICAFAKSDQS--YVISFVVPNQKKLTLLAQQKG 590
Cdd:PRK12467 3511 ARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQGDWRETLRD 3554
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
425-581 |
2.23e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 69.92 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 425 YGLTESCGAGTVTEVTD-----YTTGRVGAPLICCEIKLKDwqEGGYTVhdkPNP-RGEIVIGGQNISMGYFKNEEKTAE 498
Cdd:PRK04813 293 YGPTEATVAVTSIEITDemldqYKRLPIGYAKPDSPLLIID--EEGTKL---PDGeQGEIVISGPSVSKGYLNNPEKTAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 499 DYcVDENGQRWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDNICAFAKSDQS---YVISFV 575
Cdd:PRK04813 368 AF-FTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVESAVVVPYNKDHkvqYLIAYV 444
|
....*.
gi 75992927 576 VPNQKK 581
Cdd:PRK04813 445 VPKEED 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-567 |
2.44e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 69.05 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVL-ELTAEISCFTYGCRIGYSSPLT 306
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVY-NAWMLALNSLFDPDDVLLCGLPLFHVNgSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LSDqsskikKGSKGDCTVL----KPTLMAAVPEIMDriyknvmskvqemnyvqktlfkigydyKLEQIKKGYDAplcnli 382
Cdd:cd05944 80 YRN------PGLFDNFWKLveryRITSLSTVPTVYA---------------------------ALLQVPVNADI------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 383 lfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTE-SCGAGTVTEVTDYTTGRVGAPLICCEIKLKDW 461
Cdd:cd05944 121 ----------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 462 QEGGYTVHD-KPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 540
Cdd:cd05944 191 DGVGRLLRDcAPDEVGEICVAGPGVFGGYLYTEGNKNAFV-----ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGH 264
|
330 340
....*....|....*....|....*..
gi 75992927 541 YVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:cd05944 265 NIDPALIEEALLRHPAVAFAGAVGQPD 291
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
230-577 |
4.11e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 68.66 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAhvleltaeiscFTYGCRIGYSSPLtlsd 309
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLA-----------FTFGLGGVLLFPF---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 310 qsskikkgSKGDCTVLKPtlmAAVPEimdriykNVMSKVQEmnYVQKTLFKIGYDYKLEQIKKGYDAPLcnlilfkkvka 389
Cdd:cd05958 163 --------GVGASGVLLE---EATPD-------LLLSAIAR--YKPTVLFTAPTAYRAMLAHPDAAGPD----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 390 llGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwQEGgytvh 469
Cdd:cd05958 212 --LSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEG----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 470 dKPNPRGEI---VIGGQNismGYFKNEEKTAEDYCVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGK 546
Cdd:cd05958 284 -NPVPDGTIgrlAVRGPT---GCRYLADKRQRTYVQGG----WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPE 354
|
330 340 350
....*....|....*....|....*....|....
gi 75992927 547 VEAALKNCPLIDNICAFAKSDQS---YVISFVVP 577
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESrgvVVKAFVVL 388
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
221-592 |
4.99e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.61 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 221 VPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcriG 300
Cdd:PRK06814 785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLTG-----------G 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 301 YSSPLtlsdqSSKIKkgskgdcTVLKPTLM--AAVPEImdrIYKnvmskvqemnyVQKTLFkIGYDYKLeqikKGYdAPL 378
Cdd:PRK06814 853 LVLPL-----LSGVK-------VFLYPSPLhyRIIPEL---IYD-----------TNATIL-FGTDTFL----NGY-ARY 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 379 CNLILFKkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTES-----------CGAGTVtevtdyttGRV 447
Cdd:PRK06814 901 AHPYDFR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapvialntpmhNKAGTV--------GRL 964
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 448 gAPLIccEIKLKD---WQEGgytvhdkpnprGEIVIGGQNISMGYFKNE-----EKTAEDycvdengqrWFCTGDIGEFH 519
Cdd:PRK06814 965 -LPGI--EYRLEPvpgIDEG-----------GRLFVRGPNVMLGYLRAEnpgvlEPPADG---------WYDTGDIVTID 1021
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992927 520 PDGCLQIIDRKKDLVKLqAGEYVSLGKVEAAlkncplidnICAFAKSDQSYVISfvVPNQKK---LTLLAQQKGVE 592
Cdd:PRK06814 1022 EEGFITIKGRAKRFAKI-AGEMISLAAVEEL---------AAELWPDALHAAVS--IPDARKgerIILLTTASDAT 1085
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
85-256 |
5.90e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 68.77 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKyNFPLVT-LYATLGREAVVHGLNESEASYLITS 163
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALK-NGAIVGpLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 164 VELLESKLKAalvDINCVKHIIYVDnktinrAEYPEGLEIHSMQsvEELGAKPENLSVPPSrpTPSDMAIVMYTSGSTGR 243
Cdd:PRK04319 153 PALLERKPAD---DLPSLKHVLLVG------EDVEEGPGTLDFN--ALMEQASDEFDIEWT--DREDGAILHYTSGSTGK 219
|
170
....*....|...
gi 75992927 244 PKGVMMHHSNLIA 256
Cdd:PRK04319 220 PKGVLHVHNAMLQ 232
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
229-576 |
7.27e-12 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 67.29 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLE-------LTAEISCFTYGCRIGY 301
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiltcLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 302 SSPLtlsdqssKIKKGSKGDCTVLKPTLMAAVPEImdriYKNVMSKVQEMNYVQktlfkIGYDYKLEQikkgydaplcnl 381
Cdd:cd17635 81 KSLF-------KILTTNAVTTTCLVPTLLSKLVSE----LKSANATVPSLRLIG-----YGGSRAIAA------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 382 ilfKKVKALLGGNVRmmlsggaplspqthrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYT-TGRVGAPLICCEIKLKD 460
Cdd:cd17635 133 ---DVRFIEATGLTN------------------------TAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 461 wQEGGYTVHDKpnpRGEIVIGGQNISMGYFKNEEKTAEDYcVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGE 540
Cdd:cd17635 186 -TDGIAGPSAS---FGTIWIKSPANMLGYWNNPERTAEVL-IDG----WVNTGDLGERREDGFLFITGRSSESI-NCGGV 255
|
330 340 350
....*....|....*....|....*....|....*....
gi 75992927 541 YVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVV 576
Cdd:cd17635 256 KIAPDEVERIAEGVSGVQECACYEISDEEFgelVGLAVV 294
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
85-534 |
1.03e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 67.62 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplVTLYATlgreAVVHGLNESEASY----- 159
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARR-----SGLYYT----PINWHLTAAEIAYivdds 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 ----LITSVELLESKLKAAlvdincvkhiiyvdnktinrAEYPEGLEIHSM--------QSVEELGA-KPEnlsVPPSRP 226
Cdd:PRK08276 83 gakvLIVSAALADTAAELA--------------------AELPAGVPLLLVvagpvpgfRSYEEALAaQPD---TPIADE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TP-SDMAivmYTSGSTGRPKGVM-----MHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrig 300
Cdd:PRK08276 140 TAgADML---YSSGTTGRPKGIKrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 301 ySSPLTLSDQSSKIkkgskGDCTVLkptlmaavpeiMDRiyknvMSKVQEMNYVQKtlFKIGYDY----------KL-EQ 369
Cdd:PRK08276 199 -TAPLRFGMSALAL-----GGTVVV-----------MEK-----FDAEEALALIER--YRVTHSQlvptmfvrmlKLpEE 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 370 IKKGYDaplcnlilfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDYTT--GRV 447
Cdd:PRK08276 255 VRARYD-----------VSSL-----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGV-TVITSEDWLAhpGSV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 448 GAPLIcCEIKLKDwqEGGytvhdKPNPRGEI-----VIGGQNISmgYFKNEEKTAEDYcvdeNGQRWFCTGDIGEFHPDG 522
Cdd:PRK08276 318 GKAVL-GEVRILD--EDG-----NELPPGEIgtvyfEMDGYPFE--YHNDPEKTAAAR----NPHGWVTVGDVGYLDEDG 383
|
490
....*....|..
gi 75992927 523 CLQIIDRKKDLV 534
Cdd:PRK08276 384 YLYLTDRKSDMI 395
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
230-586 |
1.77e-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: 66.97 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 230 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTAE--ISCFTYGCRIGYSSPltl 307
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVR-ASAEVCGLDQDTVYLAVLPAAHNFPLACPgvLGTLLAGGRVVLAPD--- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 308 sdqsskikkGSKGDCTVL----KPTLMAAVPEImdriyknVMSKVQEmnyvqktlfkigydykleqiKKGYDAPLCNLil 383
Cdd:cd05920 216 ---------PSPDAAFPLiereGVTVTALVPAL-------VSLWLDA--------------------AASRRADLSSL-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 384 fkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTVT--------EVTDYTTGRVGAPLIccE 455
Cdd:cd05920 258 ------------RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE----GLLNytrlddpdEVIIHTQGRPMSPDD--E 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 456 IKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVK 535
Cdd:cd05920 320 IRVVD--EEGNPV--PPGEEGELLTRGPYTIRGYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRIKDQIN 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 75992927 536 lQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLTLLA 586
Cdd:cd05920 392 -RGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLgerSCAFVVLRDPPPSAAQ 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
206-541 |
4.32e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 65.69 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 206 MQSVEELGAKPENLSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIpglgpKDTYigylplahvle 285
Cdd:PRK09274 151 GTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA----QIEAL-----REDY----------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 286 ltaeiscftygcrigysspltlsdqssKIKKGSKGDCT-----VLKPTL-MAAV-PEiMDriyknvMSKVQEMNYvqktl 358
Cdd:PRK09274 211 ---------------------------GIEPGEIDLPTfplfaLFGPALgMTSViPD-MD------PTRPATVDP----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 359 fkigyDYKLEQI-KKGYDAPLCNLILFKKV------KALLGGNVRMMLSGGAPLSPQTH-RFMNVcfccpIGQG------ 424
Cdd:PRK09274 252 -----AKLFAAIeRYGVTNLFGSPALLERLgrygeaNGIKLPSLRRVISAGAPVPIAVIeRFRAM-----LPPDaeiltp 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 425 YGLTESCGAGTVT--EVTDYTTGR--------VGAPLICCEIKL--------KDWQEggytvhDKPNPR---GEIVIGGQ 483
Cdd:PRK09274 322 YGATEALPISSIEsrEILFATRAAtdngagicVGRPVDGVEVRIiaisdapiPEWDD------ALRLATgeiGEIVVAGP 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 484 NISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEY 541
Cdd:PRK09274 396 MVTRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
85-551 |
1.29e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLITSV 164
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ELLEsklkaalvDINCVKHIIYVDNKTINRAEYPE---GLEIHSmqsveelgakpENLsvppsrptpsdmAIVMYTSGST 241
Cdd:PRK05691 1237 HLLE--------RLPQAEGVSAIALDSLHLDSWPSqapGLHLHG-----------DNL------------AYVIYTSGST 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 242 GRPKGVMMHHSNLIagmtgqcERIPGLgpKDTYIgyLPLAHVLELTAEIS-------CF---TYGCRIgysspltlsdqs 311
Cdd:PRK05691 1286 GQPKGVGNTHAALA-------ERLQWM--QATYA--LDDSDVLMQKAPISfdvsvweCFwplITGCRL------------ 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 312 skikkgskgdctvlkptLMAAVPEIMD--RIYKNVMSK-VQEMNYVqktlfkigydykleqikkgydAPLcnLILFKKVK 388
Cdd:PRK05691 1343 -----------------VLAGPGEHRDpqRIAELVQQYgVTTLHFV---------------------PPL--LQLFIDEP 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 389 ALLG-GNVRMMLSGGAPLSPQ-THRFMNVCFCCPIGQGYGLTEScgAGTVT----EVTDYTTGRVGAPL--ICCEIKLKD 460
Cdd:PRK05691 1383 LAAAcTSLRRLFSGGEALPAElRNRVLQRLPQVQLHNRYGPTET--AINVThwqcQAEDGERSPIGRPLgnVLCRVLDAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 461 WQeggytvhdkPNPRG---EIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK05691 1461 LN---------LLPPGvagELCIGGAGLARGYLGRPALTAERFVPDplgEDGARLYRTGDRARWNADGALEYLGRLDQQV 1531
|
490
....*....|....*..
gi 75992927 535 KLQaGEYVSLGKVEAAL 551
Cdd:PRK05691 1532 KLR-GFRVEPEEIQARL 1547
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
89-567 |
1.62e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.95 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 89 EVNCRVNNFGSGLTALGLKP--------KNTIAIFCETRAEWMIAAqtcfkYNFPlVTLYATlgREAVVHGLNESEASYL 160
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPgdcvallmRNDFAFFEAAYAAMRLGA-----YAVP-VNWHFK--PEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ITSVELLESkLKAALvdincvkhiiyvdnktinraeyPEGLEIHSMQSVEELGAK----PENLSVP-------------- 222
Cdd:PRK12406 88 IAHADLLHG-LASAL----------------------PAGVTVLSVPTPPEIAAAyrisPALLTPPagaidwegwlaqqe 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 223 ----PSRPTPSDMaivMYTSGSTGRPKGVmmhhsnliagmtgqcERIPGLgPKDTyigylplAHVLELTAEISCFTYGCR 298
Cdd:PRK12406 145 pydgPPVPQPQSM---IYTSGTTGHPKGV---------------RRAAPT-PEQA-------AAAEQMRALIYGLKPGIR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IGYSSPLTLSDQSS-KIKKGSKGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYVQKTLFKIgydYKL-EQIKKGYDa 376
Cdd:PRK12406 199 ALLTGPLYHSAPNAyGLRAGRLGGVLVLQPRFDPE--ELLQLIERH---RITHMHMVPTMFIRL---LKLpEEVRAKYD- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 377 plcnlilfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEScgaGTVTEVT--DYTT--GRVGAPLI 452
Cdd:PRK12406 270 ----------VSSL-----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTES---GAVTFATseDALShpGTVGKAAP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 453 CCEIKLKDwQEGgytvhdKPNPRGEI-----VIGGqNISMGYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQII 527
Cdd:PRK12406 332 GAELRFVD-EDG------RPLPQGEIgeiysRIAG-NPDFTYHNKPEKRAE---IDRGG--FITSGDVGYLDADGYLFLC 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 75992927 528 DRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSD 567
Cdd:PRK12406 399 DRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPD 437
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
37-543 |
2.17e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 63.62 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 37 TLDKLFDHAVAKFGKkdslgtREILSEENEmqpngkvfkklilGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAifc 116
Cdd:PRK06018 11 LCHRIIDHAARIHGN------REVVTRSVE-------------GPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 117 eTRAeWMIAAQtcfkynfpLVTLYATLGREAVVHGLN---------------ESEASYL-ITSVELLEsKLKAALVDINc 180
Cdd:PRK06018 69 -TIA-WNTWRH--------LEAWYGIMGIGAICHTVNprlfpeqiawiinhaEDRVVITdLTFVPILE-KIADKLPSVE- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 181 vKHIIYVDNKTI------NRAEYPEGLEIHSMQSVeeLGAKPENLSvppsrptpsdmAIVMYTSGSTGRPKGVMM-HHSN 253
Cdd:PRK06018 137 -RYVVLTDAAHMpqttlkNAVAYEEWIAEADGDFA--WKTFDENTA-----------AGMCYTSGTTGDPKGVLYsHRSN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 254 LIAGMTGQCERIPGLGPKDTYIGYLPLAHVleltaeiscFTYGcrIGYSSPltlSDQSSKIKKGSKGDCTVL-------K 326
Cdd:PRK06018 203 VLHALMANNGDALGTSAADTMLPVVPLFHA---------NSWG--IAFSAP---SMGTKLVMPGAKLDGASVyelldteK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 327 PTLMAAVPEIMDRIyknvmskvqeMNYVQKTlfkigyDYKLEQIKK----GYDAPLCNLILFKKvkalLGGNVRmmlsgg 402
Cdd:PRK06018 269 VTFTAGVPTVWLML----------LQYMEKE------GLKLPHLKMvvcgGSAMPRSMIKAFED----MGVEVR------ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 403 aplspqthrfmnvcfccpigQGYGLTESCGAGTVTEVT---DYTTG--------RVGAPLICCEIKLKDwQEGGYTVHDK 471
Cdd:PRK06018 323 --------------------HAWGMTEMSPLGTLAALKppfSKLPGdarldvlqKQGYPPFGVEMKITD-DAGKELPWDG 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75992927 472 PNPrGEIVIGGQNISMGYFKneektAEDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVS 543
Cdd:PRK06018 382 KTF-GRLKVRGPAVAAAYYR-----VDGEILDDDG--FFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWIS 444
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
85-282 |
3.89e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.97 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynFPLVTLYATLG-------REAVVHGLNESEA 157
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAW-------LGLAKLGAVVAllntqqrGAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 158 SYLITSVELLESkLKAALVDINcVKHIIYVDNKTINRAeyPEGL-EIHSMQSveelGAKPENlsvPPSRP--TPSDMAIV 234
Cdd:PRK08279 136 KHLIVGEELVEA-FEEARADLA-RPPRLWVAGGDTLDD--PEGYeDLAAAAA----GAPTTN---PASRSgvTAKDTAFY 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 75992927 235 MYTSGSTGRPKGVMMHHSNLI---AGMTGQCeripGLGPKDTYIGYLPLAH 282
Cdd:PRK08279 205 IYTSGTTGLPKAAVMSHMRWLkamGGFGGLL----RLTPDDVLYCCLPLYH 251
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
22-396 |
4.60e-10 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 63.34 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 22 THFDSLAvidipGADTLDKLFDHAVAKFGKKDSLGtreilsEENEmqpngkvfkkliLGNYKWINYLEVNCRVNNFGSGL 101
Cdd:PTZ00297 418 REYNPLA-----GVRSLGEMWERSVTRHSTFRCLG------QTSE------------SGESEWLTYGTVDARARELGSGL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 102 TALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLyatLGREAVVHGLneseasylitsveLLESKLKAALVDINCV 181
Cdd:PTZ00297 475 LALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPL---VGKGSTMRTL-------------IDEHKIKVVFADRNSV 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 182 KHIIYVDNKTINRAEYPE--------------GLEIHSMQSVEELGakpeNLSVPPSRPTPSDMAIVMY-----TSGSTG 242
Cdd:PTZ00297 539 AAILTCRSRKLETVVYTHsfydeddhavardlNITLIPYEFVEQKG----RLCPVPLKEHVTTDTVFTYvvdntTSASGD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 243 RPKGVMMHHSNLIAG-----MTGQcerIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIkkg 317
Cdd:PTZ00297 615 GLAVVRVTHADVLRDistlvMTGV---LPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVKF--- 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 318 skgdctvlKPTLMAAVPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYKLEQIK-KGYDAPLCNLILFKKVKALLGGNVR 396
Cdd:PTZ00297 689 --------QPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRSRLINiHRRDSSLLRFIFFRATQELLGGCVE 760
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
77-534 |
5.15e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 62.31 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 77 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAE-W--MIAAQTC-FKYnfplVTLYATLGREAVVHGL 152
Cdd:PRK06188 31 LVLGDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLmaIGAAQLAgLRR----TALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 153 NESEASYLITSVELLESKLKAALVDINCVKHIIyvdnkTINRAEYPEGLeihsMQSVEELGAKPenlSVPPSRPTpsDMA 232
Cdd:PRK06188 106 EDAGISTLIVDPAPFVERALALLARVPSLKHVL-----TLGPVPDGVDL----LAAAAKFGPAP---LVAAALPP--DIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 233 IVMYTSGSTGRPKGVMMHHSNlIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTaeiscFTygcrigyssPLTLsdqss 312
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRS-IATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF-----FL---------PTLL----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 313 kikkgsKGDCTVLKPTLMAAvpEIMDRIyknvmsKVQEMNYvqkTLFKIGYDYKLEQIKKGYDAPLCNLilfkkvkallg 392
Cdd:PRK06188 232 ------RGGTVIVLAKFDPA--EVLRAI------EEQRITA---TFLVPTMIYALLDHPDLRTRDLSSL----------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 393 gnvRMMLSGGAPLSPQ-----THRFMNVcfccpIGQGYGLTESCGAGTVTEVTDYTTGRV------GAPLICCEIKLKDw 461
Cdd:PRK06188 284 ---ETVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD- 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992927 462 qEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK06188 355 -EDGREV--AQGEVGEICVRGPLVMDGYWNRPEETAEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKDMI 419
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
83-557 |
5.77e-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: 62.21 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 83 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASYLIT 162
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 163 ---------SVELLESKLKAALVDINCVKHIIYVDnKTINRAEYPEGLEIHSMQSVEElgAKPENlsvPPSRPTPSDMAI 233
Cdd:cd17634 163 adggvragrSVPLKKNVDDALNPNVTSVEHVIVLK-RTGSDIDWQEGRDLWWRDLIAK--ASPEH---QPEAMNAEDPLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 234 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIgylplahvleLTAEISCFTYGCRIGYsSPLTLsdqssk 313
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYW----------CTADVGWVTGHSYLLY-GPLAC------ 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 314 ikkgskGDCTVL---KPTLMAAvPEIMDRIYKNVMSKVQEMNYVQKTLFKIGYDYkleqiKKGYDAplcnlilfkkvkal 390
Cdd:cd17634 300 ------GATTLLyegVPNWPTP-ARMWQVVDKHGVNILYTAPTAIRALMAAGDDA-----IEGTDR-------------- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 391 lgGNVRMMLSGGAPLSPQTHR-FMNVCFC--CPIGQGYGLTEScGAGTVTEVTDYTTGRVGA---PLICCEIKLKDwqEG 464
Cdd:cd17634 354 --SSLRILGSVGEPINPEAYEwYWKKIGKekCPVVDTWWQTET-GGFMITPLPGAIELKAGSatrPVFGVQPAVVD--NE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 465 GYTVhdKPNPRGEIVIG----GQniSMGYFKNEEKTAEDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGE 540
Cdd:cd17634 429 GHPQ--PGGTEGNLVITdpwpGQ--TRTLFGDHERFEQTYFSTFKG--MYFSGDGARRDEDGYYWITGRSDDVINV-AGH 501
|
490
....*....|....*..
gi 75992927 541 YVSLGKVEAALKNCPLI 557
Cdd:cd17634 502 RLGTAEIESVLVAHPKV 518
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
205-534 |
1.07e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.11 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 205 SMQSVEELGAK--PENLSVPPSRPT-----------PSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPgLG 269
Cdd:PRK05691 129 SLLQMEELAAAnaPELLCVDTLDPAlaeawqepalqPDDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGID-LN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 270 PKDTYIGYLPLAHVLELtaeiscftygcrIGysspltlsdqsskikkgskgdcTVLKPtLMAAVPEIMdriyknvMSKVQ 349
Cdd:PRK05691 208 PDDVIVSWLPLYHDMGL------------IG----------------------GLLQP-IFSGVPCVL-------MSPAY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 350 EMNYVQKTLFKIG-----------YDYKL--EQIKkgyDAPLCNLILfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNV 415
Cdd:PRK05691 246 FLERPLRWLEAISeyggtisggpdFAYRLcsERVS---ESALERLDL---------SRWRVAYSGSEPIRQDSlERFAEK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 416 CFCCPIGQ-----GYGLTESC--------GAG-TVTEVTDYTTGR------VGAPLICC-------EIKLKDWQEGGyTV 468
Cdd:PRK05691 314 FAACGFDPdsffaSYGLAEATlfvsggrrGQGiPALELDAEALARnraepgTGSVLMSCgrsqpghAVLIVDPQSLE-VL 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75992927 469 HDkpNPRGEIVIGGQNISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGeFHPDGCLQIIDRKKDLV 534
Cdd:PRK05691 393 GD--NRVGEIWASGPSIAHGYWRNPEASAKTF-VEHDGRTWLRTGDLG-FLRDGELFVTGRLKDML 454
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
80-281 |
2.91e-09 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 59.95 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 159
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 LITSVELLE----SKLKA----ALVDINC-VKHIIYVDNKTINRAEYPEGLEIHSMQSVEelGAKPEnlsVPPSRPTPSD 230
Cdd:TIGR02188 164 VITADEGLRggkvIPLKAivdeALEKCPVsVEHVLVVRRTGNPVVPWVEGRDVWWHDLMA--KASAY---CEPEPMDSED 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75992927 231 MAIVMYTSGSTGRPKGVMmhHS----NLIAGMTgqCERIPGLGPKD--------------TYIGYLPLA 281
Cdd:TIGR02188 239 PLFILYTSGSTGKPKGVL--HTtggyLLYAAMT--MKYVFDIKDGDifwctadvgwitghSYIVYGPLA 303
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
80-252 |
4.35e-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: 59.50 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 159
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 LITSVEL--------LESKLKAALVDINCVKHIIYVDNkTINRAEYPEGLEI--HSMQSveelGAKPEnlsVPPSRPTPS 229
Cdd:cd05966 160 VITADGGyrggkvipLKEIVDEALEKCPSVEKVLVVKR-TGGEVPMTEGRDLwwHDLMA----KQSPE---CEPEWMDSE 231
|
170 180
....*....|....*....|...
gi 75992927 230 DMAIVMYTSGSTGRPKGVMmhHS 252
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVV--HT 252
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
77-591 |
7.12e-09 |
|
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: 58.62 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 77 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYN-FPLVTLYATLGREaVVHGLNES 155
Cdd:COG1021 44 VVDGERRL-SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGaIPVFALPAHRRAE-ISHFAEQS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 156 EASYLITS--------VELLESkLKAALvdiNCVKHIIYVDnktinraeypeglEIHSMQSVEELGAKPENLSVPpsRPT 227
Cdd:COG1021 122 EAVAYIIPdrhrgfdyRALARE-LQAEV---PSLRHVLVVG-------------DAGEFTSLDALLAAPADLSEP--RPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKgvmmhhsnLI-------AGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscftygcrig 300
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPK--------LIprthddyLYSVRASAEICGLDADTVYLAALPAAHNFPL-------------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 301 ySSPLTLsdqsskikkG--SKGDCTVLKP----------------TLMAAVPEIMDRIyknvmskvqeMNYVQKtlfkig 362
Cdd:COG1021 241 -SSPGVL---------GvlYAGGTVVLAPdpspdtafplierervTVTALVPPLALLW----------LDAAER------ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 363 YDYKLeqikkgydaplcnlilfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTVT----- 437
Cdd:COG1021 295 SRYDL-------------------------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE----GLVNytrld 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 438 ---EVTDYTTGRvgaPlICC--EIKLKDwqeggytVHDKPNPRGE----IVIGGQNISmGYFKNEEKTAEdyCVDENGqr 508
Cdd:COG1021 346 dpeEVILTTQGR---P-ISPddEVRIVD-------EDGNPVPPGEvgelLTRGPYTIR-GYYRAPEHNAR--AFTPDG-- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 509 WFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLTLL 585
Cdd:COG1021 410 FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgerSCAFVVPRGEPLTLA 488
|
570
....*....|.
gi 75992927 586 A-----QQKGV 591
Cdd:COG1021 489 ElrrflRERGL 499
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
222-534 |
7.84e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.47 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 222 PPSRP---TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeiscftygcr 298
Cdd:PRK07768 142 DPIDPvetGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGM------------ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IGY-SSPLTLSdqsskikkgskgdCTVLKPTLMAAV------PEIMDRiYKNVMSKVQEMNY--VQKTLFKigydykleQ 369
Cdd:PRK07768 210 VGFlTVPMYFG-------------AELVKVTPMDFLrdpllwAELISK-YRGTMTAAPNFAYalLARRLRR--------Q 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 370 IKKG-YDAplcnlilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNV---------CFCCpigqGYGLTES-------- 430
Cdd:PRK07768 268 AKPGaFDL----------------SSLRFALNGAEPIDPADvEDLLDAgarfglrpeAILP----AYGMAEAtlavsfsp 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 431 CGAGTVTEVTD------------YTTGRV------GAPLICCEIKLKDwqEGGyTVHDkpnPR--GEIVIGGQNISMGYF 490
Cdd:PRK07768 328 CGAGLVVDEVDadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD--EDG-QVLP---PRgvGVIELRGESVTPGYL 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 75992927 491 kneekTAEDY--CVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLV 534
Cdd:PRK07768 402 -----TMDGFipAQDADG--WLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
148-553 |
1.08e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 58.26 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 148 VVHGLNESEASYLITSVELLEsKLKAALVDINCVKHIIYV--DNKTINRAEYPEGLEIHSMQSveELGAKPENLSVPPSR 225
Cdd:PRK05620 103 IVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIgpSDADSAAAHMPEGIKVYSYEA--LLDGRSTVYDWPELD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 226 PTpsDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysSP 304
Cdd:PRK05620 180 ET--TAAAICYSTGTTGAPKGVVYSHRSLyLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSG------TP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 305 LTLSDQSskikkgskgdctVLKPTLMAAVPEIMDRIYKNVMSK-VQEMNYVQKTLFKigydykleqikkgydaplcnlil 383
Cdd:PRK05620 252 LVFPGPD------------LSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPPE----------------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 384 fkkvkallggnvRMML----SGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT--------EVTD---YTTGRVG 448
Cdd:PRK05620 297 ------------RMSLqeiyVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVArppsgvsgEARWayrVSQGRFP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 449 APLiccEIKLKDwqeGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTA-------EDYCVDENGQR-----WFCTGDIG 516
Cdd:PRK05620 365 ASL---EYRIVN---DGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaastfRGEDVEDANDRftadgWLRTGDVG 438
|
410 420 430
....*....|....*....|....*....|....*..
gi 75992927 517 EFHPDGCLQIIDRKKDLVKlQAGEYVslgkVEAALKN 553
Cdd:PRK05620 439 SVTRDGFLTIHDRARDVIR-SGGEWI----YSAQLEN 470
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
85-661 |
1.14e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 58.16 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRA---EWMIAAQTCFKYnFPLVTLYATLGREAVVhgLNESEASYLI 161
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAAYI--VDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 162 TSVELLESkLKAALVDINCVKHIIYVDNKtinrAEYP--EGLEihsmQSVEELGAKPEnlsvpPSRPTPSDMaivMYTSG 239
Cdd:PRK13391 102 TSAAKLDV-ARALLKQCPGVRHRLVLDGD----GELEgfVGYA----EAVAGLPATPI-----ADESLGTDM---LYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 240 STGRPKGVM--MHHSNLIA--GMTGQCERIPGLGPKDTYIGYLPLAHvleltaeiscftygcrigySSPLTLSdqSSKIK 315
Cdd:PRK13391 165 TTGRPKGIKrpLPEQPPDTplPLTAFLQRLWGFRSDMVYLSPAPLYH-------------------SAPQRAV--MLVIR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 316 KGSkgdcTVLkptlmaavpeIMDR---------IYKNVMSKVQemnyVQKTLFKigYDYKL-EQIKKGYDaplcnlilfk 385
Cdd:PRK13391 224 LGG----TVI----------VMEHfdaeqylalIEEYGVTHTQ----LVPTMFS--RMLKLpEEVRDKYD---------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 386 kVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAgTVTEVTDY-----TTGRV--GAPLICceikl 458
Cdd:PRK13391 274 -LSSL-----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGF-TACDSEEWlahpgTVGRAmfGDLHIL----- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 459 kdwQEGGytvhdKPNPRGEIvigGQ-----NISMGYFKNEEKTAEDYcvDENGQrWFCTGDIGEFHPDGCLQIIDRKKDL 533
Cdd:PRK13391 342 ---DDDG-----AELPPGEP---GTiwfegGRPFEYLNDPAKTAEAR--HPDGT-WSTVGDIGYVDEDGYLYLTDRAAFM 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 534 VkLQAGEYVSLGKVEAALKNCPLIDNICAFAksdqsyvisfvVPNQKkltlLAQQ-KGVEGSWVDICNNPAMEAEILKEI 612
Cdd:PRK13391 408 I-ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNED----LGEEvKAVVQPVDGVDPGPALAAELIAFC 471
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 75992927 613 REaanamKLERFEIPIKVRLSPE-PWTPeTGlvtdafKLKRKELKNHYLK 661
Cdd:PRK13391 472 RQ-----RLSRQKCPRSIDFEDElPRLP-TG------KLYKRLLRDRYWG 509
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
220-583 |
1.57e-08 |
|
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: 57.52 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 220 SVPPSRPTPSDMAIVMYTSGSTGRPKGVMM---HHSNLIAGMTGQCeripGL--GPKDTYIGYLPLAHVleltaeiscft 294
Cdd:cd05923 141 LIEDPPREPEQPAFVFYTSGTTGLPKGAVIpqrAAESRVLFMSTQA----GLrhGRHNVVLGLMPLYHV----------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 295 ygcrIGYSSPLTLSdqsskikkgSKGDCTVLkptlmaaVPEIMDRiyknvmskVQEMNYVQKtlfkigydyklEQIKKGY 374
Cdd:cd05923 206 ----IGFFAVLVAA---------LALDGTYV-------VVEEFDP--------ADALKLIEQ-----------ERVTSLF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 375 DAP-----LCNLILFKKVKAllgGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgAGTVTEVTDYTTGRVGA 449
Cdd:cd05923 247 ATPthldaLAAAAEFAGLKL---SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE---AMNSLYMRDARTGTEMR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 450 PLICCEIKLKdwQEGGYTVHDKPN-PRGEIVI--GGQNISMGYFKNEEKTAEDYcvdenGQRWFCTGDIGEFHPDGCLQI 526
Cdd:cd05923 321 PGFFSEVRIV--RIGGSPDEALANgEEGELIVaaAADAAFTGYLNQPEATAKKL-----QDGWYRTGDVGYVDPSGDVRI 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 527 IDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQKKLT 583
Cdd:cd05923 394 LGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWgqsVTACVVPREGTLS 452
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
393-579 |
1.86e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.31 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 393 GNVRMMLSGGAPLSP---QTHRFMNVcfccPIGQGYGLTEScgAGTVTEVT--DYTTGR--VGAPLICCEIKLKdwqegg 465
Cdd:PRK07445 230 AQFRTILLGGAPAWPsllEQARQLQL----RLAPTYGMTET--ASQIATLKpdDFLAGNnsSGQVLPHAQITIP------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 466 ytvhdkPNPRGEIVIGGQNISMGYFKNEEktaedycvdeNGQRWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLG 545
Cdd:PRK07445 298 ------ANQTGNITIQAQSLALGYYPQIL----------DSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPA 360
|
170 180 190
....*....|....*....|....*....|....*..
gi 75992927 546 KVEAALKNCPLIDNICAFAKSDQSY---VISFVVPNQ 579
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLGLPDPHWgevVTAIYVPKD 397
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
101-662 |
2.87e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.94 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 101 LTALGLKPKNTIAIFCETRAEWMIAAQTCfKYN----FPLVTLYATLGREAVVHGLN----ESEASYLITSVELLESKLK 172
Cdd:PRK09192 66 LLALGLKPGDRVALIAETDGDFVEAFFAC-QYAglvpVPLPLPMGFGGRESYIAQLRgmlaSAQPAAIITPDELLPWVNE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 173 AAlvdincvkhiiyvdnktiNRAEYPEGLeihsmqSVEELGAKPENlSVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 252
Cdd:PRK09192 145 AT------------------HGNPLLHVL------SHAWFKALPEA-DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 253 NLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELtaeISCFTygcrigysSPLTlsDQSSkikkgskgdcTVLKPTLMAA 332
Cdd:PRK09192 200 ALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGL---VGFLL--------TPVA--TQLS----------VDYLPTRDFA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 333 VPEI--MDRIYKNVMSkvqeMNYVQktlfKIGYDykleqikkgydapLCNLILFKKVKALL-------GGNvrmmlsGGA 403
Cdd:PRK09192 257 RRPLqwLDLISRNRGT----ISYSP----PFGYE-------------LCARRVNSKDLAELdlscwrvAGI------GAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 404 PLSPQT-HRFMNvCFcCPIG-------QGYGLTESC--------GAGTVTEVTDYT--------------TGRV------ 447
Cdd:PRK09192 310 MIRPDVlHQFAE-AF-APAGfddkafmPSYGLAEATlavsfsplGSGIVVEEVDRDrleyqgkavapgaeTRRVrtfvnc 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 448 GAPLICCEIKLKDwqEGGytvHDKPNPR-GEIVIGGQNISMGYFKNEEkTAEDYCVDEngqrWFCTGDIGeFHPDGCLQI 526
Cdd:PRK09192 388 GKALPGHEIEIRN--EAG---MPLPERVvGHICVRGPSLMSGYFRDEE-SQDVLAADG----WLDTGDLG-YLLDGYLYI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 527 IDRKKDLVKLQaGEYVSLGKVEAALKNCPLID--NICAFAKSDqsyvisfvvPNQKKLTLLAQqkgvegswvdiCNnpAM 604
Cdd:PRK09192 457 TGRAKDLIIIN-GRNIWPQDIEWIAEQEPELRsgDAAAFSIAQ---------ENGEKIVLLVQ-----------CR--IS 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 605 EAEILKEIREAANAMKLERFEIPIKVRLSPepwtPETGLVTDAFKLKRKELKNHYLKD 662
Cdd:PRK09192 514 DEERRGQLIHALAALVRSEFGVEAAVELVP----PHSLPRTSSGKLSRAKAKKRYLSG 567
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
85-577 |
4.30e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 56.29 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLGreAVVHGLN----ESEASYL 160
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ITS-----------------VELLESKLKAALVDincVKHIIYVDNKTinrAEYPEGLEIHSMQSVE-ELGAKPENLSVP 222
Cdd:PRK06164 103 LGRgrarwlvvwpgfkgidfAAILAAVPPDALPP---LRAIAVVDDAA---DATPAPAPGARVQLFAlPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 223 PSrpTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYG----CR 298
Cdd:PRK06164 177 AA--DPDAGALLFTTSGTTSGPKLVLHRQATLLR-HARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGaplvCE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IGYSSPLTLSD-QSSKIKKGSKGDctvlkptlmaavpEIMDRIYKnvmSKVQEMNYVQKTLFKIGyDY-----KLEQIKK 372
Cdd:PRK06164 254 PVFDAARTARAlRRHRVTHTFGND-------------EMLRRILD---TAGERADFPSARLFGFA-SFapalgELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 373 GYDAPLCNLILFKKVKALLGG-------NVRMmLSGGAPLSPQThrfmnvcfccpigqgygltescgagtvtevtdyttg 445
Cdd:PRK06164 317 ARGVPLTGLYGSSEVQALVALqpatdpvSVRI-EGGGRPASPEA------------------------------------ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 446 rvgapliccEIKLKDWQEGGYTVHDKPnprGEIVIGGQNISMGYFKNEEKTAEDYCVDEngqrWFCTGDIGEFHPDGCLQ 525
Cdd:PRK06164 360 ---------RVRARDPQDGALLPDGES---GEIEIRAPSLMRGYLDNPDATARALTDDG----YFRTGDLGYTRGDGQFV 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 75992927 526 IIDRKKDLVKLqAGEYVSLGKVEAALKNCPLIDN--ICAFAKSDQSYVISFVVP 577
Cdd:PRK06164 424 YQTRMGDSLRL-GGFLVNPAEIEHALEALPGVAAaqVVGATRDGKTVPVAFVIP 476
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
80-251 |
6.04e-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: 55.96 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 80 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEASY 159
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 160 LITS---------VELLESKLKAALVDINcVKHIIYVdnktiNRAEYPEGLEIHSMQSVEELGAKPEnlsVPPSRPTPSD 230
Cdd:cd05968 167 LITAdgftrrgreVNLKEEADKACAQCPT-VEKVVVV-----RHLGNDFTPAKGRDLSYDEEKETAG---DGAERTESED 237
|
170 180
....*....|....*....|.
gi 75992927 231 MAIVMYTSGSTGRPKGVMMHH 251
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
223-568 |
6.65e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 223 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGpkdTYIGYLPLAHVLELTAEISCFTYGcrigyS 302
Cdd:PRK07824 29 VGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG---QWLLALPAHHIAGLQVLVRSVIAG-----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 303 SPLTLsDQSSKIKkgskgdctvlKPTLMAAVPEI-MDRIYKNVMSKvqemnyvqktlfkigydykleQIKKGYDAPlcnl 381
Cdd:PRK07824 101 EPVEL-DVSAGFD----------PTALPRAVAELgGGRRYTSLVPM---------------------QLAKALDDP---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 382 ilfKKVKALLGGNVrmMLSGGAPLSPQTHRfMNVCFCCPIGQGYGLTESCGaGTVTEvtdyttgrvGAPLICCEIKLKDw 461
Cdd:PRK07824 145 ---AATAALAELDA--VLVGGGPAPAPVLD-AAAAAGINVVRTYGMSETSG-GCVYD---------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 462 qeggytvhdkpnprGEIVIGGQNISMGYFKNEEKTAedycVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVKlQAGEY 541
Cdd:PRK07824 208 --------------GRIALGGPTLAKGYRNPVDPDP----FAEPG--WFRTDDLGALD-DGVLTVLGRADDAIS-TGGLT 265
|
330 340
....*....|....*....|....*..
gi 75992927 542 VSLGKVEAALKNCPLIDNICAFAKSDQ 568
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGLPDD 292
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-555 |
7.04e-08 |
|
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: 55.08 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 226 PTPSDMAIvMYTSGSTGRPKGVMMHHsnliagmtGQCERIPGLGPKDTYIGYLPLAHVLELTAEIScftyGCRIGYSSPL 305
Cdd:cd05924 1 RSADDLYI-LYTGGTTGMPKGVMWRQ--------EDIFRMLMGGADFGTGEFTPSEDAHKAAAAAA----GTVMFPAPPL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 306 TLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmsKVQEMNYVQKTLFKIgydyKLEQIKKGYDAPLCNLilfk 385
Cdd:cd05924 68 MHGTGSWTAFGGLLGGQTVVLPDDRFDPEEVWRTIEKH---KVTSMTIVGDAMARP----LIDALRDAGPYDLSSL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 386 kvkallggnvRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGT-VTEVTDYTTG---RVGAPLICCEiklkd 460
Cdd:cd05924 137 ----------FAISSGGALLSPEVkQGLLELVPNITLVDAFGSSETGFTGSgHSAGSGPETGpftRANPDTVVLD----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 461 wqEGGYTVHDKPNPRGEIVIGGqNISMGYFKNEEKTAEDYcVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGE 540
Cdd:cd05924 202 --DDGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETF-PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-TGGE 276
|
330
....*....|....*
gi 75992927 541 YVSLGKVEAALKNCP 555
Cdd:cd05924 277 KVFPEEVEEALKSHP 291
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
210-545 |
7.69e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 55.43 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 210 EELGAKPENLSVppSRPTPsdmAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQ-CERIPGLGPKDTYIGYLPLAHvlelta 288
Cdd:PRK07470 149 RHLGARVANAAV--DHDDP---CWFFFTSGTTGRPKAAVLTHGQMAFVITNHlADLMPGTTEQDASLVVAPLSH------ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 289 eiscftyGCRIgysspltlsDQSSKIKKGSKgdcTVLKPTLMAAVPEIMDRIYKNvmsKVQEMNYVqKTLFKIgydykle 368
Cdd:PRK07470 218 -------GAGI---------HQLCQVARGAA---TVLLPSERFDPAEVWALVERH---RVTNLFTV-PTILKM------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 369 qikkgydaplcnLILFKKVKALLGGNVRMMLSGGAPL--SPQTH---RFMNVcfccpIGQGYGLTESCGAGTVT-----E 438
Cdd:PRK07470 268 ------------LVEHPAVDRYDHSSLRYVIYAGAPMyrADQKRalaKLGKV-----LVQYFGLGEVTGNITVLppalhD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 439 VTDYTTGRVGapliCC-------EIKLKDwqEGGYTVhdKPNPRGEIVIGGQNISMGYFKNEEKTAEDYcvdENGqrWFC 511
Cdd:PRK07470 331 AEDGPDARIG----TCgfertgmEVQIQD--DEGREL--PPGETGEICVIGPAVFAGYYNNPEANAKAF---RDG--WFR 397
|
330 340 350
....*....|....*....|....*....|....
gi 75992927 512 TGDIGEFHPDGCLQIIDRKKDLvklqageYVSLG 545
Cdd:PRK07470 398 TGDLGHLDARGFLYITGRASDM-------YISGG 424
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
416-577 |
9.94e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.88 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 416 CFCcpigqGYGLTEScgAGTVTEV-TDYTTGrVGAPLICCEIKLKDwqeggytvhdkpnprGEIVIGGQNISMGYFKNEE 494
Cdd:PRK09029 267 CWC-----GYGLTEM--ASTVCAKrADGLAG-VGSPLPGREVKLVD---------------GEIWLRGASLALGYWRQGQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 495 KTAedyCVDENGqrWFCTGDIGEFHpDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCPLIDNicafaksdqsyviSF 574
Cdd:PRK09029 324 LVP---LVNDEG--WFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQ-------------VF 383
|
...
gi 75992927 575 VVP 577
Cdd:PRK09029 384 VVP 386
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
221-534 |
2.41e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 221 VPPSrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLiagMTGQCERIPGLGPK--DTYIGYLPLAHVLELTAEISCFTYGCR 298
Cdd:PRK07769 173 VPPE-ANEDTIAYLQYTSGSTRIPAGVQITHLNL---PTNVLQVIDALEGQegDRGVSWLPFFHDMGLITVLLPALLGHY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IGYSSPLTLsdqsskikkgskgdctVLKP----TLMAAVPEIMDRIyknvmskvqemnyvqktlFKIGYDYKLEQ----- 369
Cdd:PRK07769 249 ITFMSPAAF----------------VRRPgrwiRELARKPGGTGGT------------------FSAAPNFAFEHaaarg 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 370 IKKGYDAPLcNLilfkkvkallgGNVRMMLSGGAPLSPQTHRFMNVCFCcPIG-------QGYGLTESC----------- 431
Cdd:PRK07769 295 LPKDGEPPL-DL-----------SNVKGLLNGSEPVSPASMRKFNEAFA-PYGlpptaikPSYGMAEATlfvsttpmdee 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 432 -----------GAGTVTEVTDYTTGRVgAPLICCEIKLKDWQE--GGYTVHDKPNPR-GEIVIGGQNISMGYFKNEEKTA 497
Cdd:PRK07769 362 ptviyvdrdelNAGRFVEVPADAPNAV-AQVSAGKVGVSEWAVivDPETASELPDGQiGEIWLHGNNIGTGYWGKPEETA 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 75992927 498 EDY--------------CVDENGqRWFCTGDIGEFHpDGCLQIIDRKKDLV 534
Cdd:PRK07769 441 ATFqnilksrlseshaeGAPDDA-LWVRTGDYGVYF-DGELYITGRVKDLV 489
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
220-534 |
2.42e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 53.79 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 220 SVPPSRPTPSdMAIVMYTSGSTGRPKGVMMHHSNLIA----GMTGQCERIPGLGPKD-TYIGYLPLAH----VLELTAEI 290
Cdd:PRK05850 152 SDARPRDLPS-TAYLQYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYFGDTGGVPPPDtTVVSWLPFYHdmglVLGVCAPI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 291 SCftyGCRIGYSSPLTLsdqsskikkgskgdctVLKPT----LMAAVPEImdriyknvmskvqemnyvqktlFKIGYDYK 366
Cdd:PRK05850 231 LG---GCPAVLTSPVAF----------------LQRPArwmqLLASNPHA----------------------FSAAPNFA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 367 LE-QIKKGYDAPLCNLILfkkvkallgGNVRMMLSGGAPLSPQT-HRFMN--VCFCCP---IGQGYGLTE------SCGA 433
Cdd:PRK05850 270 FElAVRKTSDDDMAGLDL---------GGVLGIISGSERVHPATlKRFADrfAPFNLRetaIRPSYGLAEatvyvaTREP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 434 GTVTEVTDY-----TTGRV-------GAPLIcceiklkdwqegGYTVHDKPNPR---------------GEIVIGGQNIS 486
Cdd:PRK05850 341 GQPPESVRFdyeklSAGHAkrcetggGTPLV------------SYGSPRSPTVRivdpdtciecpagtvGEIWVHGDNVA 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 487 MGYFKNEEKTAEDY---CVDEN----GQRWFCTGDIGEFHpDGCLQIIDRKKDLV 534
Cdd:PRK05850 409 AGYWQKPEETERTFgatLVDPSpgtpEGPWLRTGDLGFIS-EGELFIVGRIKDLL 462
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
425-557 |
4.98e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 52.74 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 425 YGLTESCGAGTVT---EVTDYT-TGR---VGAPLICCEIKLKDWQEGgytvhdKPNP---RGEIVIGGQNISMGYFKNEE 494
Cdd:PRK06178 360 WGMTETHTCDTFTagfQDDDFDlLSQpvfVGLPVPGTEFKICDFETG------ELLPlgaEGEIVVRTPSLLKGYWNKPE 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992927 495 KTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLI 557
Cdd:PRK06178 434 ATAE---ALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAV 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
222-564 |
4.99e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 53.12 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS---NLIAGMTGQCeripGLGPKDTyigylplahVLELTAeiscftygCR 298
Cdd:PRK10252 591 PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTaivNRLLWMQNHY----PLTADDV---------VLQKTP--------CS 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IGYSS-----PLTLsdqsskikkgskGDCTVLKPTLMAAVPEIMDRIYKNvmSKVQEMNYVQKTLfkigydykleqikKG 373
Cdd:PRK10252 650 FDVSVweffwPFIA------------GAKLVMAEPEAHRDPLAMQQFFAE--YGVTTTHFVPSML-------------AA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 374 YDAPLCNLILFKKVKALlggnVRMMLSGGA---PLSPQTHRFMNVcfccPIGQGYGLTEScgAGTVT------EVTDYTT 444
Cdd:PRK10252 703 FVASLTPEGARQSCASL----RQVFCSGEAlpaDLCREWQQLTGA----PLHNLYGPTEA--AVDVSwypafgEELAAVR 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 445 GR---VGAPLicceiklkdWQEGGYTVHDKPNP-----RGEIVIGGQNISMGYFKNEEKTAEDYCVD--ENGQRWFCTGD 514
Cdd:PRK10252 773 GSsvpIGYPV---------WNTGLRILDARMRPvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADpfAPGERMYRTGD 843
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 75992927 515 IGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLIDNICAFA 564
Cdd:PRK10252 844 VARWLDDGAVEYLGRSDDQLKIR-GQRIELGEIDRAMQALPDVEQAVTHA 892
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
209-539 |
5.32e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 209 VEELGAKPENLSVPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTA 288
Cdd:PRK05851 134 LATAAHTNRSASLTP--PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 289 EISCFTYGcrigysSPLTLSDQSSkikkgskgdctvlkptlMAAVPeimdriyknvMSKVQEMNYVQKTLFK---IGYDY 365
Cdd:PRK05851 212 LLTAALAG------APLWLAPTTA-----------------FSASP----------FRWLSWLSDSRATLTAapnFAYNL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 366 kleqIKKgYDaplcnlilfKKVKALLGGNVRMMLSGGAPLSPQ-THRFMNVcfCCPIG-------QGYGLTES------- 430
Cdd:PRK05851 259 ----IGK-YA---------RRVSDVDLGALRVALNGGEPVDCDgFERFATA--MAPFGfdagaaaPSYGLAEStcavtvp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 431 -CGAG-TVTEVTDYTTG------RVGAPLICCEIKLKDWQE----GGYTVhdkpnprGEIVIGGQNISMGYFKNEEKTAE 498
Cdd:PRK05851 323 vPGIGlRVDEVTTDDGSgarrhaVLGNPIPGMEVRISPGDGaagvAGREI-------GEIEIRGASMMSGYLGQAPIDPD 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 75992927 499 DycvdengqrWFCTGDIGEFhPDGCLQIIDRKKDLVKLqAG 539
Cdd:PRK05851 396 D---------WFPTGDLGYL-VDGGLVVCGRAKELITV-AG 425
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
228-584 |
9.40e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.13 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHvleltaeiscfTYGCrigysspltl 307
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRA-CLKFFSPKEDDVMMSFLPPFH-----------AYGF---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 308 sdqsskikkgskgDCTVLKPtLMAAVPEIMDriYKNVMSK--VQEMNYVQKTLF---KIGYDYKLEQIKKGyDAPLCNLI 382
Cdd:PRK06334 240 -------------NSCTLFP-LLSGVPVVFA--YNPLYPKkiVEMIDEAKVTFLgstPVFFDYILKTAKKQ-ESCLPSLR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 383 LfkkvkALLGGNV--RMMLSGGAPLSPQTHrfmnvcfccpIGQGYGLTESCGAGTVTEVTDYTTGR-VGAPLICCEIKLK 459
Cdd:PRK06334 303 F-----VVIGGDAfkDSLYQEALKTFPHIQ----------LRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 460 dwQEGGYTvhdkPNPRGE---IVIGGQNISMGYFKNEEKTAedyCVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKL 536
Cdd:PRK06334 368 --SEETKV----PVSSGEtglVLTRGTSLFSGYLGEDFGQG---FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 75992927 537 qAGEYVSLGKVEAALkncplidnICAFAKSDQSYVISFVV---PNQK-KLTL 584
Cdd:PRK06334 439 -GAEMVSLEALESIL--------MEGFGQNAADHAGPLVVcglPGEKvRLCL 481
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
85-259 |
1.79e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 51.29 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLGreA---VVHG---------- 151
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC-----------ARIG--AvhsVVFGgfsaealadr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 152 LNESEASYLITSVELLE----SKLKA----ALVDINCVKHIIYVdNKTINRAEYPEGLEI--HSMQSveelGAKPEnlsV 221
Cdd:PRK00174 166 IIDAGAKLVITADEGVRggkpIPLKAnvdeALANCPSVEKVIVV-RRTGGDVDWVEGRDLwwHELVA----GASDE---C 237
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 75992927 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMmhHS----NLIAGMT 259
Cdd:PRK00174 238 EPEPMDAEDPLFILYTSGSTGKPKGVL--HTtggyLVYAAMT 277
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
227-656 |
2.15e-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: 50.51 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHSNliagmtgqceripglgpkdTYIGYLPLAHVLELTAEIScfTYGCRIGYSSPLT 306
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRR-------------------TLVTSNLLSHDLNLKNGDR--TYTCMPLYHGTAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 LSDQSSKIKKGSkgdCTVLKPTLMAAvpEIMDRIYKNVMSKVQemnYVQKTLfkigyDYKLEQIKKGYDAplcnlilfkk 386
Cdd:cd05937 144 FLGACNCLMSGG---TLALSRKFSAS--QFWKDVRDSGATIIQ---YVGELC-----RYLLSTPPSPYDR---------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 387 vkallGGNVRMMLSGGapLSPQT-HRFMNVcFCCP-IGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQ-- 462
Cdd:cd05937 201 -----DHKVRVAWGNG--LRPDIwERFRER-FNVPeIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 463 --------------EGGYTVHDKPNPRGEIV--IGGQNISM--GYFKNEEKTAEDYCVD--ENGQRWFCTGDIGEFHPDG 522
Cdd:cd05937 273 vkmdpetddpirdpKTGFCVRAPVGEPGEMLgrVPFKNREAfqGYLHNEDATESKLVRDvfRKGDIYFRTGDLLRQDADG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 523 CLQIIDRKKDLVKLQaGEYVSLGKVEaalkncpliDNICAFAKSDQSYVISFVVPNqkkltllaqQKGVEGSW-VDICNN 601
Cdd:cd05937 353 RWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHPDIAEANVYGVKVPG---------HDGRAGCAaITLEES 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 602 PAMEAEILKEIREAANAMKLERFEIPIKVRLSPEpwtpetGLVTDAFKLKRKELK 656
Cdd:cd05937 414 SAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VATTDNHKQQKGVLR 462
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
476-548 |
3.04e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 50.48 E-value: 3.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75992927 476 GEIVIGGQNISMGYFKNEEKTAEDycvdengqRWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 548
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASPLVD--------GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
85-551 |
4.37e-06 |
|
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: 49.66 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 85 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGREAVVHGLNESEAsylitsv 164
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSA------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 165 ellesklkaalvdincvKHIIYvdnktinraeypegleihsmqsveelgakpenlsvppsrptpsDMAIVMYTSGSTGRP 244
Cdd:cd05940 77 -----------------KHLVV-------------------------------------------DAALYIYTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 245 KGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVlelTAEISCFTYGCRIGYSspltlsdqsskikkgskgdcTV 324
Cdd:cd05940 97 KAAIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYHS---TALIVGWSACLASGAT--------------------LV 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 325 LKPTLMAAvpEIMDRIYKNVMSKVQemnYVQKTLfkigyDYKLEQIKKGYDAplcnlilfkkvkallGGNVRMMLSGGap 404
Cdd:cd05940 153 IRKKFSAS--NFWDDIRKYQATIFQ---YIGELC-----RYLLNQPPKPTER---------------KHKVRMIFGNG-- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 405 LSPQTHRFMNVCFCCP-IGQGYGLTE-SCGAGTVTEVtDYTTGRVGAPLICC-EIKL-KDWQEGGYTVHD-----KPNPR 475
Cdd:cd05940 206 LRPDIWEEFKERFGVPrIAEFYAATEgNSGFINFFGK-PGAIGRNPSLLRKVaPLALvKYDLESGEPIRDaegrcIKVPR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 476 GEI------VIGGQNISmGYFKN---EEKTAEDycVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQaGEYVSLGK 546
Cdd:cd05940 285 GEPgllisrINPLEPFD-GYTDPaatEKKILRD--VFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK-GENVSTTE 360
|
....*
gi 75992927 547 VEAAL 551
Cdd:cd05940 361 VAAVL 365
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
233-578 |
4.95e-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: 49.22 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 233 IVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcrigysspltlsdqss 312
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLA-QALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAG---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 313 kikkgskGDCTVLKPTLMAAVPEIMDRiyknvmSKVQEMNYVQKTLfkigydyklEQIKKGYDAPLCNLILFKKVKALLG 392
Cdd:cd17636 67 -------GTNVFVRRVDAEEVLELIEA------ERCTHAFLLPPTI---------DQIVELNADGLYDLSSLRSSPAAPE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 393 GNvrMMLSggAPLSPQTHRFMnvcfccpigqGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDwqEGGYTVHDkp 472
Cdd:cd17636 125 WN--DMAT--VDTSPWGRKPG----------GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD--EDGREVPD-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 473 NPRGEIVIGGQNISMGYFKNEEktaedycvdENGQR----WFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVE 548
Cdd:cd17636 187 GEVGEIVARGPTVMAGYWNRPE---------VNARRtrggWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVE 256
|
330 340 350
....*....|....*....|....*....|....
gi 75992927 549 AALKNCPLIDNICAFAKSD----QSyVISFVVPN 578
Cdd:cd17636 257 RCLRQHPAVADAAVIGVPDprwaQS-VKAIVVLK 289
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
201-282 |
2.69e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 47.37 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 201 LEIHSMQSVEELGAKPENLsVPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTgQCERIpGLGPKDTYIGYLP 279
Cdd:PRK07867 125 INVDSPAWADELAAHRDAE-PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVM-LAQRF-GLGPDDVCYVSMP 201
|
...
gi 75992927 280 LAH 282
Cdd:PRK07867 202 LFH 204
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
236-560 |
7.96e-05 |
|
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: 45.09 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 236 YTSGSTGRPKGVMMHHSNLIAGMTGQcERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIK 315
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 316 KGSKgdctvlkpTLMAAVPEIMDRIYK--NVMSKVQEMNYVQKTLFKIgydyKLEQIKKGydAPLCNLILFkkvkallgg 393
Cdd:cd17633 86 QYNA--------TVIYLVPTMLQALARtlEPESKIKSIFSSGQKLFES----TKKKLKNI--FPKANLIEF--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 394 nvrmmlSGGAPLSPQTHRFMNvcfccpigqgygltescgagtvtevTDYTTGRVGAPLICCEIKLKDwQEGGYTvhdkpn 473
Cdd:cd17633 143 ------YGTSELSFITYNFNQ-------------------------ESRPPNSVGRPFPNVEIEIRN-ADGGEI------ 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 474 prGEIVIGGQNISMGYFKNEEktaedYCVDEngqrWFCTGDIGEFHPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKN 553
Cdd:cd17633 185 --GKIFVKSEMVFSGYVRGGF-----SNPDG----WMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKA 252
|
....*..
gi 75992927 554 CPLIDNI 560
Cdd:cd17633 253 IPGIEEA 259
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-283 |
1.22e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.97 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 87 YLEVNCRVNNFGSGL-TALGLKPKNTIAIFC--ETRAEWM---IAAQTCfkynfPLVTLYATLGREAVVHGLNESEASYL 160
Cdd:cd05938 8 YRDVDRRSNQAARALlAHAGLRPGDTVALLLgnEPAFLWIwlgLAKLGC-----PVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 161 ITSVELLES------KLKAALVdincvkHIIYVDNKTInraeyPEGleihsmqsVEELGAKPENLS---VPPS---RPTP 228
Cdd:cd05938 83 VVAPELQEAveevlpALRADGV------SVWYLSHTSN-----TEG--------VISLLDKVDAASdepVPASlraHVTI 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 75992927 229 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQceRIPGLGPKDTYIGYLPLAHV 283
Cdd:cd05938 144 KSPALYIYTSGTTGLPKAARISHLRVLQCSGFL--SLCGVTADDVIYITLPLYHS 196
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
209-555 |
2.15e-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: 44.29 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 209 VEELGAKPENLSVPPSRPTpsDMaivMYTSGSTGRPKGVMMHHS------NLIAGMTGQCeripGLGPKDTYIGYLPLAH 282
Cdd:cd05929 110 EAAEGGSPETPIEDEAAGW--KM---LYSGGTTGRPKGIKRGLPggppdnDTLMAAALGF----GPGADSVYLSPAPLYH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 283 vleltaeiscftygcrigySSPLTLSDQSSKIkkgskGDCTVLKPTLMAAvpEIMDRIYKNvmsKVQEMNYVqKTLF-KI 361
Cdd:cd05929 181 -------------------AAPFRWSMTALFM-----GGTLVLMEKFDPE--EFLRLIERY---RVTFAQFV-PTMFvRL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 362 gydYKL-EQIKKGYDaplcnlilfkkVKALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEsCGAGTVTEVT 440
Cdd:cd05929 231 ---LKLpEAVRNAYD-----------LSSL-----KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE-GQGLTIINGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 441 DYTT--GRVGAPLICcEIKLKDwqEGGYTVhdKPNPRGEIVIGGqNISMGYFKNEEKTAEDYcvDENGqrWFCTGDIGEF 518
Cdd:cd05929 291 EWLThpGSVGRAVLG-KVHILD--EDGNEV--PPGEIGEVYFAN-GPGFEYTNDPEKTAAAR--NEGG--WSTLGDVGYL 360
|
330 340 350
....*....|....*....|....*....|....*..
gi 75992927 519 HPDGCLQIIDRKKDLVkLQAGEYVSLGKVEAALKNCP 555
Cdd:cd05929 361 DEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHP 396
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
469-639 |
2.54e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 43.96 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 469 HDKPNPRgEIVIGGQNISMGYFKNEEKTaeDYCVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKLqAGEYVSLGKVE 548
Cdd:cd05915 355 KDGKALG-EVQLKGPWITGGYYGNEEAT--RSALTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 549 AALKNCPLIDNICAFAKSDQSYVISFVvpnqkkltllaqqkgvegSWVDICNNPAMEAEILKEIREAANAMKLerfeIPI 628
Cdd:cd05915 429 NALMGHPKVKEAAVVAIPHPKWQERPL------------------AVVVPRGEKPTPEELNEHLLKAGFAKWQ----LPD 486
|
170
....*....|..
gi 75992927 629 KVRLSPE-PWTP 639
Cdd:cd05915 487 AYVFAEEiPRTS 498
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
227-269 |
3.77e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 75992927 227 TPSDMAIVMYTSGSTGRPKGVMMHHsnliAGM-TGQCERIPGLG 269
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQ----RGMlNNQLSKVPYLA 3906
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
222-558 |
6.28e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 222 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL---AHVLELTAEISCftyGCR 298
Cdd:PRK05691 2326 LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF-GMRADDCELHFYSInfdAASERLLVPLLC---GAR 2401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 299 IgysspltlsdqsskikkgskgdctVLKPTLMAAVPEIMDRIyknvmsKVQEMNYVQktlFKIGYDYKLEQIKKGYDAPL 378
Cdd:PRK05691 2402 V------------------------VLRAQGQWGAEEICQLI------REQQVSILG---FTPSYGSQLAQWLAGQGEQL 2448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 379 cnlilfkkvkallggNVRMMLSGGAPLSPQTHRFMNVCFCcP--IGQGYGLTESC--------------GAGTVTeVTDY 442
Cdd:PRK05691 2449 ---------------PVRMCITGGEALTGEHLQRIRQAFA-PqlFFNAYGPTETVvmplaclapeqleeGAASVP-IGRV 2511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 443 TTGRVGAPLiccEIKLKDWQEGGytvhdkpnpRGEIVIGGQNISMGYFKNEEKTAEDYCVD---ENGQRWFCTGDIGEFH 519
Cdd:PRK05691 2512 VGARVAYIL---DADLALVPQGA---------TGELYVGGAGLAQGYHDRPGLTAERFVADpfaADGGRLYRTGDLVRLR 2579
|
330 340 350
....*....|....*....|....*....|....*....
gi 75992927 520 PDGCLQIIDRKKDLVKLQaGEYVSLGKVEAALKNCPLID 558
Cdd:PRK05691 2580 ADGLVEYVGRIDHQVKIR-GFRIELGEIESRLLEHPAVR 2617
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
402-555 |
7.30e-04 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 42.48 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 402 GAPLSPQT-HRFMNVCfCCPIGQGYGLTEScgagTVTEVT----DYTTGRVGAPLICCEIKLKDwQEGGYTvhdKPNPRG 476
Cdd:cd05970 310 GEALNPEVfNTFKEKT-GIKLMEGFGQTET----TLTIATfpwmEPKPGSMGKPAPGYEIDLID-REGRSC---EAGEEG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 477 EIVI---GGQNISM--GYFKNEEKTAEdycVDENGqrWFCTGDIGEFHPDGCLQIIDRKKDLVKlQAGEYVSLGKVEAAL 551
Cdd:cd05970 381 EIVIrtsKGKPVGLfgGYYKDAEKTAE---VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESAL 454
|
....
gi 75992927 552 KNCP 555
Cdd:cd05970 455 IQHP 458
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-558 |
8.99e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 42.45 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 226 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL----AHVLELTAEIScftygcRIGY 301
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY-GIRPGEVDLATFPLfalfGPALGLTSVIP------DMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 302 SSPLTLSDQS--SKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmSKVQEMNyvQKTLfkigydykleqikkgydaplc 379
Cdd:cd05910 155 TRPARADPQKlvGAIRQ--------YGVSIVFGSPALLERV-----ARYCAQH--GITL--------------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 380 nlilfkkvkallgGNVRMMLSGGAPLSPQTH-RFMN-VCFCCPIGQGYGLTESC------GAGTVTEVTDYTTGR----V 447
Cdd:cd05910 199 -------------PSLRRVLSAGAPVPIALAaRLRKmLSDEAEILTPYGATEALpvssigSRELLATTTAATSGGagtcV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 448 GAPLICCEIKL-----KDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYCVDENGQRWFCTGDIGEFHPDG 522
Cdd:cd05910 266 GRPIPGVRVRIieiddEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDLGYLDDEG 345
|
330 340 350
....*....|....*....|....*....|....*.
gi 75992927 523 CLQIIDRKKDLVKLQAGEYVSLgKVEAALKNCPLID 558
Cdd:cd05910 346 RLWFCGRKAHRVITTGGTLYTE-PVERVFNTHPGVR 380
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
198-254 |
1.95e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 41.59 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 75992927 198 PEGLEIHSMQSVEELGAKPENLSV-PPSRPTPSdmaivmYTSGSTGRPKGVMMHHSNL 254
Cdd:TIGR03443 389 LEGGETDVLAPYQALKDTPTGVVVgPDSNPTLS------FTSGSEGIPKGVLGRHFSL 440
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
476-534 |
3.82e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 40.49 E-value: 3.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75992927 476 GEIVIGGQNISMGYFKNEEKTAEDYC---------------VDENGqRWFCTGDIGeFHPDGCLQIIDRKKDLV 534
Cdd:PRK12476 430 GEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegshadgAADDG-TWLRTGDLG-VYLDGELYITGRIADLI 501
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
77-532 |
4.44e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 39.97 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 77 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIaaqtcfkynfplvTLYATLgrEAVVHGLNese 156
Cdd:PRK10946 42 VICGERQF-SYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYI-------------TFFALL--KLGVAPVN--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 157 ASYLITSVELLE--SKLKAALVdINCVKHIIYVDNKTIN--RAEYPEGLEIH-----SMQSVEELGAKPENLSVPpsRPT 227
Cdd:PRK10946 103 ALFSHQRSELNAyaSQIEPALL-IADRQHALFSDDDFLNtlVAEHSSLRVVLllnddGEHSLDDAINHPAEDFTA--TPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 228 PSD-MAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVLELtaeiscftygcrigySSPlt 306
Cdd:PRK10946 180 PADeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALPAAHNYPM---------------SSP-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 307 lsdqsskikkGS-----KGDCTVlkptlMAAVPE------IMDRIYKNVMSKVQEmnyvQKTLFkigydykLEQIKK-GY 374
Cdd:PRK10946 242 ----------GAlgvflAGGTVV-----LAPDPSatlcfpLIEKHQVNVTALVPP----AVSLW-------LQAIAEgGS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 375 DAPLCNLilfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTEscgaGTV--TEVTD-----YTTGrv 447
Cdd:PRK10946 296 RAQLASL--------------KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE----GLVnyTRLDDsderiFTTQ-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75992927 448 GAPlICC--EIKLKDwQEGgytvhdKPNPRGEI---VIGGQNISMGYFKNEEKTAEdyCVDENGqrWFCTGDIGEFHPDG 522
Cdd:PRK10946 356 GRP-MSPddEVWVAD-ADG------NPLPQGEVgrlMTRGPYTFRGYYKSPQHNAS--AFDANG--FYCSGDLVSIDPDG 423
|
490
....*....|
gi 75992927 523 CLQIIDRKKD 532
Cdd:PRK10946 424 YITVVGREKD 433
|
|
| |
