|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
101-682 |
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: 843.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSMTLVHEfGLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEI 180
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSL-GGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVDsfkkaesliknrenmptlkniividsadelkdgtaiiDTIRVESLTNALNLGSRYPFTNNLPKPDDNYIICYTS 260
Cdd:cd05927 81 SIVFCD-------------------------------------AGVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 261 GTTGTPKGVMLTHSNIVANISGFLKILFAFQpsMIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRGSIQGLTDDI 340
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILN--KINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 341 KTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKVGRDTIWDRLVFNKIQQQIGGKVDLMVT 420
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 421 GSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLNYFAKD--GKGEIRIK 498
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKDpnPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 499 GPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGD 578
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 579 SLERWLIAVVVPEPDVLKEWNDKQGSGSRKIEEICNDEKAKEFVLSELHAIGKANKLNSIEQVKKVILTSDTFTVENGLL 658
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 17556552 659 TPTLKAKRPQLRLKYKDGMAKVYK 682
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
65-685 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 624.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 65 LTRF--YPEVATLHDVFVKGKTESNGGPCVGTRSSGD---ADYEFLTYDDVHEQAKNLSMTLVHeFGLTPAntTNIGIYA 139
Cdd:PLN02736 34 VSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvGEYKWMTYGEAGTARTAIGSGLVQ-HGIPKG--ACVGLYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 140 RNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVdSFKKAESLIKNRENMPTLKNIIVIDSADELKDG 219
Cdd:PLN02736 111 INRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSEIPSVRLIVVVGGADEPLPS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 220 TAIIDTIRVESLTNALNLGSRYPFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfAFQPSmidatQ 299
Cdd:PLN02736 190 LPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLST-KFYPS-----D 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 300 VHISYLPLSHMMEQLTHWTLLGFGSKIGYFRGSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNF 379
Cdd:PLN02736 264 VHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 380 AFARKLSLVKAGKvGRDTIWDRLVFNKIQQQIGGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWM 459
Cdd:PLN02736 344 AYNAKKQALENGK-NPSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 460 GDPSTGHCGAPAPCALVKLGDVPDLNYFAKDG---KGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGT 536
Cdd:PLN02736 423 GDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGR 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 537 IRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERWLIAVVVPEPDVLKEWNDKQGSGSRKIEEICNDE 616
Cdd:PLN02736 503 LKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKYEDLKQLCNDP 582
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17556552 617 KAKEFVLSELHAIGKANKLNSIEQVKKVILTSDTFTVENGLLTPTLKAKRPQLRLKYKDGMAKVYKQFP 685
Cdd:PLN02736 583 RVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAELA 651
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
69-675 |
8.08e-154 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 458.03 E-value: 8.08e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 69 YPEVATLHDVFVKGKTESNGGPCVGTRSSGDadYEFLTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVS 148
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGI--WQSLTWAEFAERVRALAAGL-LALGVKPGDR--VAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 149 AVACveQSM--VVVPLYDTLGAEAATFIISQAEISVVIVDSFKKAESLIKNRENMPTLKNIIVIDSADELKDgtaiidtI 226
Cdd:COG1022 82 DLAI--LAAgaVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDD-------P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 227 RVESLTNALNLGSRYPFTNNL------PKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfafqpsMIDATQV 300
Cdd:COG1022 153 RLLSLDELLALGREVADPAELearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL------PLGPGDR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 301 HISYLPLSHMMEQLTHWTLLGFGSKIGYFRgSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFA 380
Cdd:COG1022 227 TLSFLPLAHVFERTVSYYALAAGATVAFAE-SPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 381 FARKLSLVKAGKVGRD---------TIWDRLVFNKIQQQIGGKVDLMVTGSAPISSTVLETCRvTLGTTIVEGYGQTECT 451
Cdd:COG1022 306 LAVGRRYARARLAGKSpslllrlkhALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 452 ALATFTWMGDPSTGHCGAPAPCALVKLGDvpdlnyfakdgKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEM 531
Cdd:COG1022 385 PVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGEL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 532 LPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSlERWLIAVVVPEPDVLKEWNDKQGSGSRKIEE 611
Cdd:COG1022 454 DEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPYTSYAE 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17556552 612 ICNDEKAKEFVLSElhaIGKANK-LNSIEQVKKVILTSDTFTVENGLLTPTLKAKRPQLRLKYKD 675
Cdd:COG1022 533 LAQDPEVRALIQEE---VDRANAgLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYAD 594
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
101-666 |
1.04e-147 |
|
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: 438.96 E-value: 1.04e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSMTLvHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEI 180
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGL-VELGLKPGD--KVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETEC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVDsfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlPKPDDNYIICYTS 260
Cdd:cd17639 79 SAIFTD-------------------------------------------------------------GKPDDLACIMYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 261 GTTGTPKGVMLTHSNIVANISGFLKILfafqPSMIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYfrGSIQGLTDDI 340
Cdd:cd17639 98 GSTGNPKGVMLTHGNLVAGIAGLGDRV----PELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDKS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 341 K--------TLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKvgrDT-IWDRLVFNKIQQQI 411
Cdd:cd17639 172 KrgckgdltEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAAL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 412 GGKVDLMVTGSAPISSTVLETCRVTLGTtIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLNY--FAK 489
Cdd:cd17639 249 GGRLRYMLSGGAPLSADTQEFLNIVLCP-VIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYstDKP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 490 DGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPV 569
Cdd:cd17639 328 PPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 570 VQQVYVDGDSLERWLIAVVVPEPDVLKEWNDKQGSGSRKIEEICNDEKAKEFVLSELHAIGKANKLNSIEQVKKVILTSD 649
Cdd:cd17639 408 VNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDE 487
|
570
....*....|....*..
gi 17556552 650 TFTVENGLLTPTLKAKR 666
Cdd:cd17639 488 EWTPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
42-683 |
2.65e-143 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 433.09 E-value: 2.65e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 42 AVEVK-GQPG---------VWKSALmeneSEDVLTRFYPEVATLHDVFVKGKTESNGGPCVGTRSSGDAD---YEFLTYD 108
Cdd:PLN02430 5 AAQVEeGVKGkdgkpsvgpVYRNLL----SKKGFPPIDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGKvgpYMWKTYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 109 DVHEQAKNLSMTLvHEFGLTPAntTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDSF 188
Cdd:PLN02430 81 EVYEEVLQIGSAL-RASGAEPG--SRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 189 KKAESLIKNRENMPTLKNIIVIDS-ADELKDGTAIIDtIRVESLTNALNLGSRYPFTNNLPKPDDNYIICYTSGTTGTPK 267
Cdd:PLN02430 158 KIKELLEPDCKSAKRLKAIVSFTSvTEEESDKASQIG-VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 268 GVMLTHSNIVANISGFLKILFAFQPSMIdATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRGSIQGLTDDIKTLKPTV 347
Cdd:PLN02430 237 GVVLTHEAVATFVRGVDLFMEQFEDKMT-HDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 348 FPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKVGRDT--IWDRLVFNKIQQQIGGKVDLMVTGSAPI 425
Cdd:PLN02430 316 LAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 426 SSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPS-TGHCGAPAPCALVKLGDVPDLNY--FAKDGKGEIRIKGPCV 502
Cdd:PLN02430 396 STEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCmLGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 503 TKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLER 582
Cdd:PLN02430 476 FSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKS 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 583 WLIAVVVPEPDVLKEWNDKQGSgSRKIEEICNDEKAKEFVLSELHAIGKANKLNSIEQVKKVILTSDTFTVENGLLTPTL 662
Cdd:PLN02430 555 MLVAVVVPNEENTNKWAKDNGF-TGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATL 633
|
650 660
....*....|....*....|.
gi 17556552 663 KAKRPQLRLKYKDGMAKVYKQ 683
Cdd:PLN02430 634 KKRRNNLLKYYQVEIDEMYRK 654
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
41-681 |
1.74e-142 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 432.23 E-value: 1.74e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 41 QAVEVKGQPGVWK-----SALMENESEDVltrfypevATLHDVFVKGKTESNGGPCVGTR--------SSGDA------- 100
Cdd:PLN02387 29 VPVDVGGEPGYAIrnarfPELVETPWEGA--------TTLAALFEQSCKKYSDKRLLGTRklisrefeTSSDGrkfeklh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 --DYEFLTYDDVHEQAKNLSMTLVHefgLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQA 178
Cdd:PLN02387 101 lgEYEWITYGQVFERVCNFASGLVA---LGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNET 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 179 EISVVIVDSfKKAESLIKNRENMPTLKNIIVI-DSADELKDGTAIIDTIRVESLTNALNLGSRYPFTNNLPKPDDNYIIC 257
Cdd:PLN02387 178 EVTTVICDS-KQLKKLIDISSQLETVKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISGFLKILfafqPSmIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYfrGSIQGLT 337
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVV----PK-LGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 D-----------DIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKVG----RDTIWDRL 402
Cdd:PLN02387 330 DtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGSWFGawglEKLLWDAL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 403 VFNKIQQQIGGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVP 482
Cdd:PLN02387 410 VFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 483 DLNYFAKDG---KGEIRIKGPCVTKGYYKDPERTAELF--DEEG--FLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYV 555
Cdd:PLN02387 490 EGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVYkvDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYV 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 556 APEKIEQVYIRTPVVQQVYVDGDSLERWLIAVVVPEPDVLKEWNDKQGSGSRKIEEICNDEKAKEFVLSELHAIGKANKL 635
Cdd:PLN02387 570 SLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCEKEEAVKEVQQSLSKAAKAARL 649
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 17556552 636 NSIEQVKKVILTSDTFTVENGLLTPTLKAKRPQLRLKYKDGMAKVY 681
Cdd:PLN02387 650 EKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
77-682 |
3.80e-134 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 409.80 E-value: 3.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 77 DVFVKGKTESNGGPCVGTRSSGDAD---YEFLTYDDVHEQAKNLSMTLvHEFGLTpaNTTNIGIYARNSPQWLVSAVACV 153
Cdd:PLN02614 49 DVFRMSVEKYPNNPMLGRREIVDGKpgkYVWQTYQEVYDIVIKLGNSL-RSVGVK--DEAKCGIYGANSPEWIISMEACN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 154 EQSMVVVPLYDTLGAEAATFIISQAEISVVIVDSfKKAESLIKNRENMPT-LKNIIVIDSADELKDGTAIIDTIRVESLT 232
Cdd:PLN02614 126 AHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNSTEyMKTVVSFGGVSREQKEEAETFGLVIYAWD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 233 NALNLGSRYPFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPSMiDATQVHISYLPLSHMME 312
Cdd:PLN02614 205 EFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAL-TVKDVYLSYLPLAHIFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 313 QLTHWTLLGFGSKIGYFRGSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAGK 392
Cdd:PLN02614 284 RVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 393 --VGRDTIWDRLVFNKIQQQIGGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTAlATFTWMGDP--STGHCG 468
Cdd:PLN02614 364 shVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCA-GTFVSLPDEldMLGTVG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 469 APAPCALVKLGDVPDLNY--FAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEeGFLQTGDIGEMLPNGTIRIIDRKKHI 546
Cdd:PLN02614 443 PPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKKNI 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 547 FKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERWLIAVVVPEPDVLKEWNDKQGSgSRKIEEICNDEKAKEFVLSEL 626
Cdd:PLN02614 522 FKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGV-SGDYNALCQNEKAKEFILGEL 600
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 17556552 627 HAIGKANKLNSIEQVKKVILTSDTFTVENGLLTPTLKAKRPQLRLKYKDGMAKVYK 682
Cdd:PLN02614 601 VKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
101-683 |
1.51e-131 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 402.68 E-value: 1.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSmTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEI 180
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIG-SAIRSRGVNPGD--RCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVDSFKKAESLIKNRENMPTLKNIIVIDSADELKDGTAIIDTIRVESLTNALNLGSrypFTNNLPK--PDDNYIICY 258
Cdd:PLN02861 151 SIAFVQESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGS---LDCELPPkqKTDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 259 TSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPSmIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRGSIQGLTD 338
Cdd:PLN02861 228 TSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRV-ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLME 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 339 DIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAG--KVGRDTIWDRLVFNKIQQQIGGKVD 416
Cdd:PLN02861 307 DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGlkQEEASPRLDRLVFDKIKEGLGGRVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 417 LMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTAlATFTWMGD--PSTGHCGAPAPCALVKLGDVPDLNY--FAKDGK 492
Cdd:PLN02861 387 LLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANvfSMVGTVGVPMTTIEARLESVPEMGYdaLSDVPR 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAS 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 573 VYVDGDSLERWLIAVVVPEPDVLKEWNdKQGSGSRKIEEICNDEKAKEFVLSELHAIGKANKLNSIEQVKKVILTSDTFT 652
Cdd:PLN02861 545 IWVYGNSFESFLVAVVVPDRQALEDWA-ANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFD 623
|
570 580 590
....*....|....*....|....*....|.
gi 17556552 653 VENGLLTPTLKAKRPQLRLKYKDGMAKVYKQ 683
Cdd:PLN02861 624 IERDLITPTFKLKRPQLLKYYKDCIDQLYSE 654
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
105-669 |
4.43e-123 |
|
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: 373.85 E-value: 4.43e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEfGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIAL-GVEPGD--RVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDsfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpKPDDNYIICYTSGTTG 264
Cdd:cd05907 83 VE--------------------------------------------------------------DPDDLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVANISGFLKILFAfqpsmiDATQVHISYLPLSHMMEQLT-HWTLLGFGSKIGYFRgSIQGLTDDIKTL 343
Cdd:cd05907 101 RPKGVMLSHRNILSNALALAERLPA------TEGDRHLSFLPLAHVFERRAgLYVPLLAGARIYFAS-SAETLLDDLSEV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 344 KPTVFPVVPRLLNRLYDAItSKVQQQGFMAKLvynFAFArklslvkagkvgrdtiwdrlvfnkiqqqIGGKVDLMVTGSA 423
Cdd:cd05907 174 RPTVFLAVPRVWEKVYAAI-KVKAVPGLKRKL---FDLA----------------------------VGGRLRFAASGGA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 424 PISSTVLETCRvTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDvpdlnyfakdgKGEIRIKGPCVT 503
Cdd:cd05907 222 PLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVM 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 504 KGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLeRW 583
Cdd:cd05907 290 LGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGR-PF 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 584 LIAVVVPEPDVLKEWNDKQGSGSRKIEEICNDEKAKEFVLSelhAIGKANK-LNSIEQVKKVILTSDTFTVENGLLTPTL 662
Cdd:cd05907 369 LVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEA---AVEAANArLSRYEQIKKFLLLPEPFTIENGELTPTL 445
|
....*..
gi 17556552 663 KAKRPQL 669
Cdd:cd05907 446 KLKRPVI 452
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
98-550 |
8.87e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 345.84 E-value: 8.87e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 98 GDADYEFLTYDDVHEQAKNLSMTLVHeFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQ 177
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRA-LGVGKGDR--VAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 178 AEISVVIVDSFKKAESLIKNRENMPTLKNIIVIDSADELKDGTAIIDTIRVESLtnalnlgsryPFTNNLPKPDDNYIIC 257
Cdd:pfam00501 92 SGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP----------PPPPPPPDPDDLAYII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPsmIDATQVHISYLPLSHMMEQLTH-WTLLGFGSKIGYFRGSIQ-- 334
Cdd:pfam00501 162 YTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFG--LGPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGFPAld 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 335 --GLTDDIKTLKPTVFPVVPRLLNRLYDAitskvqqqgfmaklvynfafarklslvkagkvgrdtiwdrlvfNKIQQQIG 412
Cdd:pfam00501 240 paALLELIERYKVTVLYGVPTLLNMLLEA-------------------------------------------GAPKRALL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 413 GKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDP---STGHCGAPAPCALVKLGDVPDLNYFAK 489
Cdd:pfam00501 277 SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPP 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17556552 490 DGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLA 550
Cdd:pfam00501 357 GEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
104-682 |
4.94e-87 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 287.26 E-value: 4.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 104 FLTYDDVHEQAKNLSMTLvHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVV 183
Cdd:PTZ00216 121 YITYAELWERIVNFGRGL-AELGLTKGS--NVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 184 IVDSfKKAESLIKNRENMpTLKNIIVIdSADELKDGtaiIDT--IRVESLTNALNLGSRYPFTNNLPKPDDN---YIICY 258
Cdd:PTZ00216 198 VCNG-KNVPNLLRLMKSG-GMPNTTII-YLDSLPAS---VDTegCRLVAWTDVVAKGHSAGSHHPLNIPENNddlALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 259 TSGTTGTPKGVMLTHSNIVANISG----FLKILFAFQPsmidaTQVHISYLPLSHMMEQLTHWTLLGFGSKIGYfrGSIQ 334
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILAledrLNDLIGPPEE-----DETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 335 GLTD-------DIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKvgrDT-IWDRLVFNK 406
Cdd:PTZ00216 345 TLTDtfarphgDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGK---DTpYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 IQQQIGGKVDLMVTGSAPISSTVLETCRVTLGTtIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLNY 486
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 487 FAK-DGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYI 565
Cdd:PTZ00216 501 TDTpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYG 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 566 RTPVVQQ----VYVDGDsleRWLIA--VVVPEPDVLK--EWNDKQGSgsrkIEEICNDEKAKEFVLSELHAIGKANKLNS 637
Cdd:PTZ00216 581 QNELVVPngvcVLVHPA---RSYICalVLTDEAKAMAfaKEHGIEGE----YPAILKDPEFQKKATESLQETARAAGRKS 653
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 17556552 638 IEQVKKVILTSDTFTVENGLLTPTLKAKRPQLRLKYKDGMAKVYK 682
Cdd:PTZ00216 654 FEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
102-673 |
1.04e-74 |
|
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: 249.31 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 102 YEFLTYDDVHEQAKNLSMTLVHeFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEIS 181
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRA-LGLEPGS--KIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 182 VVIVDSfkkaesliknrenmptlkniivIDSADELKDGTAIIDTIRVESLTNALN-------LGSRYPFTNNLPKPDDNY 254
Cdd:cd05932 81 ALFVGK----------------------LDDWKAMAPGVPEGLISISLPPPSAANcqyqwddLIAQHPPLEERPTRFPEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 255 I--ICYTSGTTGTPKGVMLTHSNIVANISGFLKILfafqpsMIDATQVHISYLPLSHMMEQlthwTLLGFGSKIG----Y 328
Cdd:cd05932 139 LatLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI------GTEENDRMLSYLPLAHVTER----VFVEGGSLYGgvlvA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 329 FRGSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQgfmaklvynfafarKLS-LVKAGKVGRdtiwdrLVFNKI 407
Cdd:cd05932 209 FAESLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQ--------------KLNlLLKIPVVNS------LVKRKV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 408 QQQIG-GKVDLMVTGSAPISSTVLETCRvTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDvpdlny 486
Cdd:cd05932 269 LKGLGlDQCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 487 fakdgKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIR 566
Cdd:cd05932 342 -----DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 567 TPVVQQVYVDGDSLERWLIAVVVPEPDVLKEwndkqgsgsrkieeicnDEKAKEFVLSELHA-IGKANK-LNSIEQVKKV 644
Cdd:cd05932 417 HDRVEMVCVIGSGLPAPLALVVLSEEARLRA-----------------DAFARAELEASLRAhLARVNStLDSHEQLAGI 479
|
570 580
....*....|....*....|....*....
gi 17556552 645 ILTSDTFTVENGLLTPTLKAKRPQLRLKY 673
Cdd:cd05932 480 VVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
101-667 |
4.36e-72 |
|
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: 241.11 E-value: 4.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSMTLVHeFGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEI 180
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRS-LGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVDSfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpKPDDNYIICYTS 260
Cdd:cd17640 79 VALVVEN-------------------------------------------------------------DSDDLATIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 261 GTTGTPKGVMLTHSNIVANISGFLKIlfaFQPsmiDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYfrGSIQGLTDDI 340
Cdd:cd17640 98 GTTGNPKGVMLTHANLLHQIRSLSDI---VPP---QPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 341 KTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAfarklslvkagkvgrdtiwdrLVFNKIQQQIGGkvdlmvT 420
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF---------------------LSGGIFKFGISG------G 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 421 GSAPISstvLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLNYFAKDGKGEIRIKGP 500
Cdd:cd17640 223 GALPPH---VDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 501 CVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSl 580
Cdd:cd17640 300 QVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD- 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 581 ERWLIAVVVPEPDVLKEWNDKQGSGSRKIEE--ICNDEKAKEFVLSELHAIGKANKLNSIEQVKKVILTSDTFTvENGLL 658
Cdd:cd17640 379 QKRLGALIVPNFEELEKWAKESGVKLANDRSqlLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPFI-ENGEM 457
|
....*....
gi 17556552 659 TPTLKAKRP 667
Cdd:cd17640 458 TQTMKIKRN 466
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
90-659 |
1.41e-70 |
|
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: 240.44 E-value: 1.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 90 PCVGTRSSGDAD--------------YEFLTYDDVHEQAKNLSMTLVHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQ 155
Cdd:cd17632 39 PALGQRATELVTdpatgrttlrllprFETITYAELWERVGAVAAAHDPEQPVRPGDF--VAVLGFTSPDYATVDLALTRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 156 SMVVVPLydTLGAEAATF--IISQAEISVVIVDsfkkAESLIKNRE---NMPTLKNIIVIDSADELKDGTAIIDTIR--- 227
Cdd:cd17632 117 GAVSVPL--QAGASAAQLapILAETEPRLLAVS----AEHLDLAVEavlEGGTPPRLVVFDHRPEVDAHRAALESARerl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 228 ------VESLTNALNLGSRYPFTNNLPKPDDN---YIICYTSGTTGTPKGVMLTHSNIVAnisgFLKILFAFQ-PSMIDA 297
Cdd:cd17632 191 aavgipVTTLTLIAVRGRDLPPAPLFRPEPDDdplALLIYTSGSTGTPKGAMYTERLVAT----FWLKVSSIQdIRPPAS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 298 TQVHisYLPLSHMMEQLTHWTLLGFGSkIGYFRGS--IQGLTDDIKTLKPTVFPVVPRLLNRLYdaitskvqqQGFMAKL 375
Cdd:cd17632 267 ITLN--FMPMSHIAGRISLYGTLARGG-TAYFAAAsdMSTLFDDLALVRPTELFLVPRVCDMLF---------QRYQAEL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 376 VynfafarklSLVKAGkVGRDTIWDRLVFNKIQQQIGGKVDLMVTGSAPISS---TVLETCrvtLGTTIVEGYGQTECTA 452
Cdd:cd17632 335 D---------RRSVAG-ADAETLAERVKAELRERVLGGRLLAAVCGSAPLSAemkAFMESL---LDLDLHDGYGSTEAGA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 453 LATFTWMGDPstghcgapaPCALVKLGDVPDLNYFAKDG---KGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIG 529
Cdd:cd17632 402 VILDGVIVRP---------PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 530 EMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERWLIAVVVPEPDVLKEWNDKQgsgsrki 609
Cdd:cd17632 473 AELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTAR------- 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 17556552 610 eeicndekAKEFVLSELHAIGKANKLNSIEQVKKVILTSDTFTVENGLLT 659
Cdd:cd17632 546 --------LRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
97-681 |
1.94e-68 |
|
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: 234.94 E-value: 1.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 97 SGDADYEFLTYDDVHEQAKNLSMTLVHeFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIIS 176
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLK-LGLERFHG--VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 177 QAEISVVIVDSFKKAESLIKNRENMPTLKNIIVI-DSADELKDG----TAIIDTIRVESLTNALNLGSRYpftnnlpKPD 251
Cdd:cd05933 78 TSEANILVVENQKQLQKILQIQDKLPHLKAIIQYkEPLKEKEPNlyswDEFMELGRSIPDEQLDAIISSQ-------KPN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 252 DNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfafqpSMIDATQVH---ISYLPLSHMMEQ-LTHWTLLGFGSKIg 327
Cdd:cd05933 151 QCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHM-----DLRPATVGQesvVSYLPLSHIAAQiLDIWLPIKVGGQV- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 328 YF------RGSiqgLTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFA------RKLSLVKAGKVGR 395
Cdd:cd05933 225 YFaqpdalKGT---LVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGvgletnLKLMGGESPSPLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 396 DTIWDRLVFNKIQQQIG-GKVDLMVTGSAPISSTVLETCrVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCA 474
Cdd:cd05933 302 YRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLgDVPDlnyfaKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEY 554
Cdd:cd05933 381 KTKI-HNPD-----ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 555 VAPEKIEQ-VYIRTPVVQQVYVDGDslERWLIAVVVP----------EP-DVLK----EWNDKQGSGSRKIEEICN--DE 616
Cdd:cd05933 455 VPPVPIEDaVKKELPIISNAMLIGD--KRKFLSMLLTlkcevnpetgEPlDELTeeaiEFCRKLGSQATRVSEIAGgkDP 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17556552 617 KAKEFVLSelhAIGKANK--LNSIEQVKK-VILTSDtFTVENGLLTPTLKAKRPQLRLKYKDGMAKVY 681
Cdd:cd05933 533 KVYEAIEE---GIKRVNKkaISNAQKIQKwVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
101-593 |
4.53e-62 |
|
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: 213.90 E-value: 4.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEI 180
Cdd:COG0318 21 GGRRLTYAELDARARRLAAAL-RALGVGPGDR--VALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVdsfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnALnlgsrypftnnlpkpddnyiICYTS 260
Cdd:COG0318 98 RALVT------------------------------------------------AL--------------------ILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 261 GTTGTPKGVMLTHSNIVANISGFLKILfafqpsMIDATQVHISYLPLSHMMeQLTHWTLLGF--GSKIGYFRG-SIQGLT 337
Cdd:COG0318 110 GTTGRPKGVMLTHRNLLANAAAIAAAL------GLTPGDVVLVALPLFHVF-GLTVGLLAPLlaGATLVLLPRfDPERVL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 DDIKTLKPTVFPVVPRLLNRLYDAitskvqqqgfmaklvYNFAfARKLSLVKagkvgrdtiwdrlvfnkiqqqiggkvdL 417
Cdd:COG0318 183 ELIERERVTVLFGVPTMLARLLRH---------------PEFA-RYDLSSLR---------------------------L 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 418 MVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTW--MGDPSTGHCGAPAPCALVKLGDvPDLNYFAKDGKGEI 495
Cdd:COG0318 220 VVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEI 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 496 RIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQVYV 575
Cdd:COG0318 299 VVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAV 376
|
490 500
....*....|....*....|.
gi 17556552 576 DGDSLERW---LIAVVVPEPD 593
Cdd:COG0318 377 VGVPDEKWgerVVAFVVLRPG 397
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
105-666 |
3.08e-58 |
|
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: 203.83 E-value: 3.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEfGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd05914 8 LTYKDLADNIAKFALLLKIN-GVGTGD--RVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDsfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpKPDDNYIICYTSGTTG 264
Cdd:cd05914 85 VS--------------------------------------------------------------DEDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVANISGFLKILfafqpsMIDATQVHISYLPLSHMMEqLTHWTLLGF--GSKIGYFRGSIQGLTDDIKT 342
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVV------LLGKGDKILSILPLHHIYP-LTFTLLLPLlnGAHVVFLDKIPSAKIIALAF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 343 LKPTVFPVVPRLLNRLYDAITSKVQQ---QGFMAKLvynfafarklslvkAGKVGRDTIWdRLVFNKIQQQIGGKVDLMV 419
Cdd:cd05914 176 AQVTPTLGVPVPLVIEKIFKMDIIPKltlKKFKFKL--------------AKKINNRKIR-KLAFKKVHEAFGGNIKEFV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 TGSAPISSTVLETCRvTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDvPDlnyfAKDGKGEIRIKG 499
Cdd:cd05914 241 IGGAKINPDVEEFLR-TIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDS-PD----PATGEGEIIVRG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 500 PCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTP------VVQQv 573
Cdd:cd05914 315 PNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPfvleslVVVQ- 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 574 yvdgdslERWLIAVVVPEPDVLKEwndkqgsgsrKIEEICNDEKA-KEFVLSELHaigkaNKLNSIEQVKKVILTSDTFT 652
Cdd:cd05914 394 -------EKKLVALAYIDPDFLDV----------KALKQRNIIDAiKWEVRDKVN-----QKVPNYKKISKVKIVKEEFE 451
|
570
....*....|....
gi 17556552 653 VengllTPTLKAKR 666
Cdd:cd05914 452 K-----TPKGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
256-598 |
2.62e-56 |
|
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: 194.81 E-value: 2.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 256 ICYTSGTTGTPKGVMLTHSNIVANISGFLKILFafqpsmIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRGSIQG 335
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG------LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 336 LT-DDIKTLKPTVFPVVPRLLNRLYDAITSKvqqqgfmaklvynfafARKLSLVKAGkvgrdtiwdrlvfnkiqqqiggk 414
Cdd:cd04433 79 AAlELIEREKVTILLGVPTLLARLLKAPESA----------------GYDLSSLRAL----------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 415 vdlmVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPST--GHCGAPAPCALVKLGDvPDLNYFAKDGK 492
Cdd:cd04433 120 ----VSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARkpGSVGRPVPGVEVRIVD-PDGGELPPGEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAElFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPEATAA-VDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAE 272
|
330 340 350
....*....|....*....|....*....|....*
gi 17556552 573 VYV---DGDSLERWLIAVVVPEP------DVLKEW 598
Cdd:cd04433 273 AAVvgvPDPEWGERVVAVVVLRPgadldaEELRAH 307
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
106-594 |
1.19e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 195.41 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLVhEFGLTPANTtnIGIYARNSPQWLVSAVACveQSM--VVVPLYDTLGAEAATFIISQAEISVV 183
Cdd:PRK06187 33 TYAELDERVNRLANALR-ALGVKKGDR--VAVFDWNSHEYLEAYFAV--PKIgaVLHPINIRLKPEEIAYILNDAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 184 IVDSfKKAESLIKNRENMPTLKNIIVIDSADElkdGTAIIDTIRVESLTNALNlgSRYPFTNnlPKPDDNYIICYTSGTT 263
Cdd:PRK06187 108 LVDS-EFVPLLAAILPQLPTVRTVIVEGDGPA---APLAPEVGEYEELLAAAS--DTFDFPD--IDENDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNIVANIsgflkiLFAFQPSMIDATQVHISYLPLSHMMEqlTHWTLLGF--GSKIGYFRgSIQ--GLTDD 339
Cdd:PRK06187 180 GHPKGVVLSHRNLFLHS------LAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPYLALmaGAKQVIPR-RFDpeNLLDL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 IKTLKPTVFPVVPRLLNRLydaitskvqqqgfmakLVYNFAFARKLSLVKagkvgrdtiwdrlvfnkiqqqiggkvdLMV 419
Cdd:PRK06187 251 IETERVTFFFAVPTIWQML----------------LKAPRAYFVDFSSLR---------------------------LVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 TGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTW----MGDPSTGHCGAPAPCALVKLGDV-PDLNYFAKDGK-- 492
Cdd:PRK06187 288 YGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPpedqLPGQWTKRRSAGRPLPGVEARIVdDDGDELPPDGGev 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELFDeEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAE 445
|
490 500
....*....|....*....|....*
gi 17556552 573 VYVDGDSLERW---LIAVVVPEPDV 594
Cdd:PRK06187 446 VAVIGVPDEKWgerPVAVVVLKPGA 470
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
105-593 |
7.38e-51 |
|
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: 184.34 E-value: 7.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd05911 11 LTYAQLRTLSRRLAAGL-RKLGLKKGDV--VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfKKAESLIKNRENMPTLKNIIVIDSADElkdgtaiiDTIRVESLTNALNLGS-RYPFTNNLPKPDDNYIICYTSGTT 263
Cdd:cd05911 88 TDP-DGLEKVKEAAKELGPKDKIIVLDDKPD--------GVLSIEDLLSPTLGEEdEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNIVANISgflkILFAFQPSMIDATQVHISYLPLSHMMEQL-THWTLLGFGSKIGYFRGSIQGLTDDIKT 342
Cdd:cd05911 159 GLPKGVCLSHRNLIANLS----QVQTFLYGNDGSNDVILGFLPLYHIYGLFtTLASLLNGATVIIMPKFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 343 LKPTVFPVVPRLLNRLydAITSKVQQQgfmaklvynfafarKLSLVKAgkvgrdtiwdrlvfnkiqqqiggkvdlMVTGS 422
Cdd:cd05911 235 YKITFLYLVPPIAAAL--AKSPLLDKY--------------DLSSLRV---------------------------ILSGG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 423 APISSTVLETC-RVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLNYFAKDGKGEIRIKGPC 501
Cdd:cd05911 272 APLSKELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 502 VTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVYV----DG 577
Cdd:cd05911 352 VMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVigipDE 430
|
490
....*....|....*.
gi 17556552 578 DSLERWLiAVVVPEPD 593
Cdd:cd05911 431 VSGELPR-AYVVRKPG 445
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
98-577 |
1.81e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 183.57 E-value: 1.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 98 GDAD-YEF----LTYDDVHEQAKNLSMTLVhEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAAT 172
Cdd:PRK07656 19 GDKEaYVFgdqrLTYAELNARVRRAAAALA-ALGIGKGD--RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 173 FIISQAEISVVIV-DSFKKAESLIKNRenMPTLKNIIVIDsadelkDGTAIIDTIRVESLTNALNLGSRYPFTNNLpKPD 251
Cdd:PRK07656 96 YILARGDAKALFVlGLFLGVDYSATTR--LPALEHVVICE------TEEDDPHTEKMKTFTDFLAAGDPAERAPEV-DPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 252 DNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfafqpsMIDATQVHISYLPLSHMmeqlthwtllgFGSKIGYFRG 331
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYL------GLTEGDRYLAANPFFHV-----------FGYKAGVNAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 332 SIQGLT-------------DDIKTLKPTVFPVVPRLLNRLYDAITSKvqqqgfmaklvynfafARKLSLVKAGkvgrdti 398
Cdd:PRK07656 230 LMRGATilplpvfdpdevfRLIETERITVLPGPPTMYNSLLQHPDRS----------------AEDLSSLRLA------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 399 wdrlvfnkiqqqiggkvdlmVTGSAPISSTVLETCRVTLG-TTIVEGYGQTECTALATFTWMGDPST---GHCGAPapCA 474
Cdd:PRK07656 287 --------------------VTGAASMPVALLERFESELGvDIVLTGYGLSEASGVTTFNRLDDDRKtvaGTIGTA--IA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLGDVPDLNYFAKDGK-GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGE 553
Cdd:PRK07656 345 GVENKIVNELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGF 423
|
490 500
....*....|....*....|....
gi 17556552 554 YVAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:PRK07656 424 NVYPAEVEEVLYEHPAVAEAAVIG 447
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
103-593 |
2.96e-49 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 179.30 E-value: 2.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 103 EFLTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISV 182
Cdd:cd05936 23 RKLTYRELDALAEAFAAGL-QNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 VIVDsfkkaesliknrenmptlkniividsadelkdgtaiidtirvESLTNALNLGSRYPFTNNLPkPDDNYIICYTSGT 262
Cdd:cd05936 100 LIVA------------------------------------------VSFTDLLAAGAPLGERVALT-PEDVAVLQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 263 TGTPKGVMLTHSNIVANISGFLKILfafqPSMIDATQVHISYLPLSH---MMEQLTHWTLLGfGSKIGYFRGSIQGLTDD 339
Cdd:cd05936 137 TGVPKGAMLTHRNLVANALQIKAWL----EDLLEGDDVVLAALPLFHvfgLTVALLLPLALG-ATIVLIPRFRPIGVLKE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 IKTLKPTVFPVVPRLLNRLYdaitskvqqqGFMAKLVYNFAfarklslvkagkvgrdtiwdrlvfnkiqqqiggKVDLMV 419
Cdd:cd05936 212 IRKHRVTIFPGVPTMYIALL----------NAPEFKKRDFS---------------------------------SLRLCI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 TGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPS-TGHCGAPAPCALVKLGDvpDLNYFAKDGK-GEIRI 497
Cdd:cd05936 249 SGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD--DDGEELPPGEvGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 498 KGPCVTKGYYKDPERTAELFDeEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYV-- 575
Cdd:cd05936 327 RGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvg 404
|
490 500
....*....|....*....|
gi 17556552 576 --DGDSLERwLIAVVVPEPD 593
Cdd:cd05936 405 vpDPYSGEA-VKAFVVLKEG 423
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
106-673 |
2.51e-47 |
|
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: 176.07 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:cd17641 13 TWADYADRVRAFALGL-LALGVGRGDV--VAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 DSFKKAESLIKNRENMPTLKNIIVIDSAdelkdGTAIIDTIRVESLTNALNLG----SRYP--FTNNLP--KPDDNYIIC 257
Cdd:cd17641 90 EDEEQVDKLLEIADRIPSVRYVIYCDPR-----GMRKYDDPRLISFEDVVALGraldRRDPglYEREVAagKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISGFLkilfAFQPSMIDATQVhiSYLPLSHMMEQ-LTHWTLLGFGSKIGyFRGSIQGL 336
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFLGHCAAYL----AADPLGPGDEYV--SVLPLPWIGEQmYSVGQALVCGFIVN-FPEEPETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 337 TDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKVGRDT---------IWDRLVFNKI 407
Cdd:cd17641 238 MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPVslwlrlaswLADALLFRPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 408 QQQIG-GKVDLMVTGSAPISSTVLETCRvTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVpdlny 486
Cdd:cd17641 318 RDRLGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 487 fakdgkGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIR 566
Cdd:cd17641 392 ------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 567 TPVVQQVYVDGDSLErWLIAVVVPEPDVLKEWNDKQGSGSRKIEEICNDEKAKEFVLSElhaIGKANK-LNSIEQVKKVI 645
Cdd:cd17641 466 SPYIAEAVVLGAGRP-YLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIRKE---VEKVNAsLPEAQRIRRFL 541
|
570 580
....*....|....*....|....*...
gi 17556552 646 LTSDTFTVENGLLTPTLKAKRPQLRLKY 673
Cdd:cd17641 542 LLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
104-666 |
5.94e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 168.74 E-value: 5.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 104 FLTYDDVHEQAKNLSMTLVHEFGL-TPANTTN----------IGIYARNSPQWLVSAVACveqsMVvvplydtlgaEAAT 172
Cdd:PTZ00342 91 YITYGNFFKKVLSFSHSLNTYEGKgIPEKKYNeeqnngkfklLGLYGSNSINWLVADLAC----ML----------SGVT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 173 FIISQAEISV-VIVDSFKKA------------ESLIKNRENMPTLKNIIVIDS--------------------------- 212
Cdd:PTZ00342 157 TLVMHSKFSIdVIVDILNETklewlcldldlvEGLLERKNELPHLKKLIILDTlikskeininkeeknngsnvnnngnkn 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 213 -------------ADELKDGTAIIDTIRVESL----TNALNLGSRYPFTNNLPK----------PDDNYI--ICYTSGTT 263
Cdd:PTZ00342 237 nkeeqkgndlsneLEDISLGPLEYDKEKLEKIkdlkEKAKKLGISIILFDDMTKnkttnykiqnEDPDFItsIVYTSGTS 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNIVANISGFLK--ILFAFQPsmidatQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRGSIQGLTDDIK 341
Cdd:PTZ00342 317 GKPKGVMLSNKNLYNTVVPLCKhsIFKKYNP------KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 342 TLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKlvynFAFARKLSLVKAGKVGRDTIWDRLVFN---KIQQQIGGKVDLM 418
Cdd:PTZ00342 391 NSKGNILAGVPKVFNRIYTNIMTEINNLPPLKR----FLVKKILSLRKSNNNGGFSKFLEGITHissKIKDKVNPNLEVI 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 419 VTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAP-APCALVKLgdVPDLNYFAKDG--KGEI 495
Cdd:PTZ00342 467 LNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPiSPNTKYKV--RTWETYKATDTlpKGEL 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 496 RIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAQGEYVAPEKIEQVYIRTPVVQQVYV 575
Cdd:PTZ00342 545 LIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVV 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 576 DGD----------SLERWLIAVVVPEPDVLKEWNDKQGSGSRKI-EEICNDEKAKEFVLSELHAIGKANKLNSIEQVKKV 644
Cdd:PTZ00342 625 YGDdsmdgplaiiSVDKYLLFKCLKDDNMLESTGINEKNYLEKLtDETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDI 704
|
650 660
....*....|....*....|..
gi 17556552 645 ILTSDTFTVENgLLTPTLKAKR 666
Cdd:PTZ00342 705 YLTSKVWDTNN-YLTPTFKVKR 725
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
249-593 |
6.84e-39 |
|
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: 150.85 E-value: 6.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 249 KPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLkilfAFQPSMIDATQVHISYLPLSHMMeQLTHWT--LLGFGSKI 326
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV----AGEGSNSDSEDVFLCVLPMFHIY-GLSSFAlgLLRLGATV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 327 ---GYFrgSIQGLTDDIKTLKPTVFPVVPRLLnrlydaitskvqqqgfmaklvynfafarkLSLVKAGKVgrdtiwDRLV 403
Cdd:cd05904 231 vvmPRF--DLEELLAAIERYKVTHLPVVPPIV-----------------------------LALVKSPIV------DKYD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 404 FNKIQQqiggkvdlMVTGSAPISSTVLETCRVTLGTT-IVEGYGQTECTALATftwMGDPSTGH------CGAPAPCALV 476
Cdd:cd05904 274 LSSLRQ--------IMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTESTGVVA---MCFAPEKDrakygsVGRLVPNVEA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 477 KLGDVPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVA 556
Cdd:cd05904 343 KIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVA 421
|
330 340 350
....*....|....*....|....*....|....*..
gi 17556552 557 PEKIEQVYIRTPVVqqvyVDgdslerwliAVVVPEPD 593
Cdd:cd05904 422 PAELEALLLSHPEI----LD---------AAVIPYPD 445
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
105-597 |
1.53e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 150.68 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVV---PLYdTLGAEAATFIISQAEIS 181
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHTDLKPGD--RIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY-TAREMEHQFNDSGAKAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 182 VVIVDSFKKAESLIKNREnmptLKNIIVIDSADELK--DGTAIIDTIR-------------VESLTNALNLGSRYPFTNN 246
Cdd:PRK05677 127 VCLANMAHLAEKVLPKTG----VKHVIVTEVADMLPplKRLLINAVVKhvkkmvpayhlpqAVKFNDALAKGAGQPVTEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 247 LPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGfLKILFAFQpsMIDATQVHISYLPLSH----------MMEQLTH 316
Cdd:PRK05677 203 NPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSN--LNEGCEILIAPLPLYHiyaftfhcmaMMLIGNH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 317 WTLLGfgskigyfrgsiqgltddiktlKPTVFPvvprllnrlydaitskvqqqgfmaklvynfAFARKLSLVK-AGKVGR 395
Cdd:PRK05677 280 NILIS----------------------NPRDLP------------------------------AMVKELGKWKfSGFVGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 396 DTIWDRLVFNKIQQQIG-GKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCA 474
Cdd:PRK05677 308 NTLFVALCNNEAFRKLDfSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPST 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEY 554
Cdd:PRK05677 388 LCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFN 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYVDGDSLERW-----LIAVVVPEPDVLKE 597
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQCAAIGVPDEKSgeaikVFVVVKPGETLTKE 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
99-593 |
1.88e-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: 149.38 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 99 DADYEFLTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQA 178
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQL-AALGIKKGDR--VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 179 EISVVIVDSFKKAESLiknrENMPTLKNIIVidsadELK-DGTAIIDTIRVESLTNALNLGSRYPFTNNlPKPDDNYIIC 257
Cdd:cd05926 86 GSKLVLTPKGELGPAS----RAASKLGLAIL-----ELAlDVGVLIRAPSAESLSNLLADKKNAKSEGV-PLPDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVA---NISGFLKILFAfqpsmiDATQVhisYLPLSHMMEQ----LThwTLLGFGSKIGYFR 330
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAAsatNITNTYKLTPD------DRTLV---VMPLFHVHGLvaslLS--TLAAGGSVVLPPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 331 GSIQGLTDDIKTLKPTVFPVVPR----LLNRlYDAITSKVqqqgfMAKLvynfAFARklslvkagkvgrdtiwdrlvfnk 406
Cdd:cd05926 225 FSASTFWPDVRDYNATWYTAVPTihqiLLNR-PEPNPESP-----PPKL----RFIR----------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 iqqqiggkvdlmvTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWM--GDPSTGHCGAPAPcalVKLGDVPDL 484
Cdd:cd05926 272 -------------SCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPLppGPRKPGSVGKPVG---VEVRILDED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 485 NYFAKDG-KGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQV 563
Cdd:cd05926 336 GEILPPGvVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGV 414
|
490 500 510
....*....|....*....|....*....|...
gi 17556552 564 YIRTPVVQQVYVDG---DSLERWLIAVVVPEPD 593
Cdd:cd05926 415 LLSHPAVLEAVAFGvpdEKYGEEVAAAVVLREG 447
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
106-598 |
6.71e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 148.99 E-value: 6.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLvHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVV---PLYdTLGAEAATFIISQAEISV 182
Cdd:PRK05605 59 TYAELGKQVRRAAAGL-RALGVRPGD--RVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLY-TAHELEHPFEDHGARVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 VivdsFKKAESLI-KNREN--------------MPTLKNI---IVIDSADELKDG--TAIIDTIRVESLTNALNLGSRYP 242
Cdd:PRK05605 135 V----WDKVAPTVeRLRRTtpletivsvnmiaaMPLLQRLalrLPIPALRKARAAltGPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 243 FTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLkilfAFQPSMIDATQVHISYLPLSHMMeQLTHWTLLGF 322
Cdd:PRK05605 211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGK----AWVPGLGDGPERVLAALPMFHAY-GLTLCLTLAV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 323 --GSKIGYF-RGSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAitskvqqqgfmaklvynfAFARKLSLvkagkvgrdtiw 399
Cdd:PRK05605 286 siGGELVLLpAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEA------------------AEERGVDL------------ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 400 drlvfNKIQQQIGGKVDLMVtgsapisSTVLETCRVTlGTTIVEGYGQTECTALAtftwMGDPST-----GHCGAPAPCA 474
Cdd:PRK05605 336 -----SGVRNAFSGAMALPV-------STVELWEKLT-GGLLVEGYGLTETSPII----VGNPMSddrrpGYVGVPFPDT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLGDVPDLNYFAKDGK-GEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGE 553
Cdd:PRK05605 399 EVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGF 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17556552 554 YVAPEKIEQVYIRTPVVQQVYVDG----DSLERWLIAVVVPE-----PDVLKEW 598
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVGlpreDGSEEVVAAVVLEPgaaldPEGLRAY 530
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
251-594 |
1.10e-36 |
|
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: 142.75 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 251 DDNYIICYTSGTTGTPKGVMLTHSNIVANIsgfLKILFAFQPSMIDatqVHISYLPLSHMmEQLTHWTLLGFgskigyFR 330
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNA---VNALAALDLGPDD---VLLVVAPLFHI-GGLGVFTLPTL------LR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 331 GsiqgltddiktlkptVFPVVPRllnrlydaitskvqqqgfmaklvyNFAFARKLSLVKAGKV----GRDTIWDRLvfnk 406
Cdd:cd17631 165 G---------------GTVVILR------------------------KFDPETVLDLIERHRVtsffLVPTMIQAL---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 IQQQIGGKVDL-----MVTGSAPISSTVLETCRVTlGTTIVEGYGQTECTALATFTWMGDPST--GHCGAPAPCALVKLG 479
Cdd:cd17631 202 LQHPRFATTDLsslraVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 480 DvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKlAQGEYVAPEK 559
Cdd:cd17631 281 D-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAE 357
|
330 340 350
....*....|....*....|....*....|....*...
gi 17556552 560 IEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDV 594
Cdd:cd17631 358 VEDVLYEHPAVAEVAVIGVPDEKWgeaVVAVVVPRPGA 395
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
97-593 |
1.14e-35 |
|
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: 141.61 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 97 SGDADYEFLTYDDVHEQAKNLSMTLvHEFGLTPAntTNIGIYARNSPQWLVS--AVACVeqSMVVVPLYDTLGAEAATFI 174
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANAL-RRLGVKPG--DRVATLAWNTHRHLELyyAVPGM--GAVLHTINPRLFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 175 ISQAEISVVIVD-SFkkaESLIKN-RENMPTLKNIIVIDSADELkDGTAIIDTIRVESLtnalnLGSRYPFTNNlPKPDD 252
Cdd:cd12119 93 INHAEDRVVFVDrDF---LPLLEAiAPRLPTVEHVVVMTDDAAM-PEPAGVGVLAYEEL-----LAAESPEYDW-PDFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 253 N--YIICYTSGTTGTPKGVMLTHSNIVanisgflkiLFAFQPSMIDATQVHIS--YLPLSHMMeqltH---WTL----LG 321
Cdd:cd12119 163 NtaAAICYTSGTTGNPKGVVYSHRSLV---------LHAMAALLTDGLGLSESdvVLPVVPMF----HvnaWGLpyaaAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 322 FGSKIGYFRGSIQG--LTDDIKTLKPTVFPVVPRLLnrlydaitskvqqQGFMAKLvynfafarklslvKAGKVGRDTIW 399
Cdd:cd12119 230 VGAKLVLPGPYLDPasLAELIEREGVTFAAGVPTVW-------------QGLLDHL-------------EANGRDLSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 400 dRLVfnkiqqqIGGkvdlmvtgSAPISStVLETCRvTLGTTIVEGYGQTECTALATFTWmgdPSTGHCGAPA-------- 471
Cdd:cd12119 284 -RVV-------IGG--------SAVPRS-LIEAFE-ERGVRVIHAWGMTETSPLGTVAR---PPSEHSNLSEdeqlalra 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 472 ----PCALVKLGDV-PDLNYFAKDGK--GEIRIKGPCVTKGYYKDPERTAElFDEEGFLQTGDIGEMLPNGTIRIIDRKK 544
Cdd:cd12119 343 kqgrPVPGVELRIVdDDGRELPWDGKavGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSK 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 17556552 545 HIFKLAqGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERWL---IAVVVPEPD 593
Cdd:cd12119 422 DVIKSG-GEWISSVELENAIMAHPAVAEAAVIGVPHPKWGerpLAVVVLKEG 472
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
105-597 |
3.91e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 140.73 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVV---PLYDT---------LGAEAAT 172
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQHTDLVPGD--RIAVQMPNVLQYPIAVFGALRAGLIVVntnPLYTAremrhqfkdSGARALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 173 FI-ISQAEISVVIVDSfkKAESLIKNR--ENMPTLKNIIVIDSADELKDGTAIIDTIRVESLTNALNLGSRYPFTNNLPK 249
Cdd:PRK12492 128 YLnMFGKLVQEVLPDT--GIEYLIEAKmgDLLPAAKGWLVNTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFAF----QPSMIDATQVHISYLPLSH----------MMEQLT 315
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgQPLMKEGQEVMIAPLPLYHiyaftancmcMMVSGN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 316 HWTLLGFGSKIGYFrgsiqgltddIKTLKPTVFPVVPRLlNRLYDAItskVQQQGFMaklvyNFAFARkLSLVKAGkvgr 395
Cdd:PRK12492 286 HNVLITNPRDIPGF----------IKELGKWRFSALLGL-NTLFVAL---MDHPGFK-----DLDFSA-LKLTNSG---- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 396 dtiwdrlvfnkiqqqiggkvdlmvtGSAPISSTVLETCRVTlGTTIVEGYGQTECTALATFTWMGDPST-GHCGAPAPCA 474
Cdd:PRK12492 342 -------------------------GTALVKATAERWEQLT-GCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEY 554
Cdd:PRK12492 396 ALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFN 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYVDGDSLERWLIAV---VVP-EPDVLKE 597
Cdd:PRK12492 474 VYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVklfVVArDPGLSVE 520
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
103-577 |
2.19e-34 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 138.26 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 103 EFLTYDDVHEQAKNLSMTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVV---PLY----------DTlGAE 169
Cdd:PRK08974 47 EVMTFRKLEERSRAFAAYLQNGLGLKKGD--RVALMMPNLLQYPIALFGILRAGMIVVnvnPLYtprelehqlnDS-GAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 170 AatfiisqaeisVVIVDSFkkAESLIKNRENMPtLKNIIVIDSADELKDGTAIIDTIRVE---------------SLTNA 234
Cdd:PRK08974 124 A-----------IVIVSNF--AHTLEKVVFKTP-VKHVILTRMGDQLSTAKGTLVNFVVKyikrlvpkyhlpdaiSFRSA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 235 LNLGSRYPFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANIsgfLKILFAFQPSMIDATQVHISYLPLSHMMeQL 314
Cdd:PRK08974 190 LHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL---EQAKAAYGPLLHPGKELVVTALPLYHIF-AL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 315 THWTLLgfgskigYFRGSIQGLTddiktlkptvfpvvprllnrlydaITSKVQQQGFMAKLV-YNFAfarklslvkaGKV 393
Cdd:PRK08974 266 TVNCLL-------FIELGGQNLL------------------------ITNPRDIPGFVKELKkYPFT----------AIT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 394 GRDTIWDRLVFNKIQQQIG-GKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATftwmGDPS-----TGHC 467
Cdd:PRK08974 305 GVNTLFNALLNNEEFQELDfSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVS----VNPYdldyySGSI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 468 GAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIF 547
Cdd:PRK08974 381 GLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI 458
|
490 500 510
....*....|....*....|....*....|
gi 17556552 548 kLAQGEYVAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:PRK08974 459 -LVSGFNVYPNEIEDVVMLHPKVLEVAAVG 487
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
252-634 |
1.01e-32 |
|
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: 131.64 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 252 DNYIICYTSGTTGTPKGVMLTHSNIVANISgflkilfafqpSMIDATQ-------VHIsyLPLSHmmeqlTHWTLLGFGS 324
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVR-----------ALVDAWRwteddvlLHV--LPLHH-----VHGLVNALLC 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 325 KIgYFRGSIQGLT-------DDIKTLKP-TVFPVVPRLLNRLYDAitskvqqqgfmaklvYNFAFARKLSLVKAGKvgrd 396
Cdd:cd05941 152 PL-FAGASVEFLPkfdpkevAISRLMPSiTVFMGVPTIYTRLLQY---------------YEAHFTDPQFARAAAA---- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 397 tiwdrlvfnkiqqqigGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALV 476
Cdd:cd05941 212 ----------------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 477 KLGDVPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKK-HIFKlAQGEYV 555
Cdd:cd05941 276 RIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 556 APEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDV-------LKEWNDKQGSGSRKIEEICndekakefVLSE 625
Cdd:cd05941 355 SALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLRAGAaalsleeLKEWAKQRLAPYKRPRRLI--------LVDE 426
|
410
....*....|.
gi 17556552 626 L--HAIGKANK 634
Cdd:cd05941 427 LprNAMGKVNK 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-594 |
1.96e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 132.03 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 119 MTLVHEFGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYdTLGAEA-ATFIISQAEISVVIVDSFKKAESLIKN 197
Cdd:PRK06188 51 IQAFEALGLGT--GDAVALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGSLDdHAYVLEDAGISTLIVDPAPFVERALAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 198 RENMPTLKNIIVIDSADELKDGTAIIDTIRVESLTNAlnlgsrypftnnlPKPDDNYIICYTSGTTGTPKGVMLTHSNIV 277
Cdd:PRK06188 128 LARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAA-------------ALPPDIAGLAYTGGTTGKPKGVMGTHRSIA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 278 anisGFLKILFA-----FQPSMIDATqvhisylPLSHMMEQLTHWTLLGFGSKIGYFRGSIQGLTDDIKTLKPTVFPVVP 352
Cdd:PRK06188 195 ----TMAQIQLAewewpADPRFLMCT-------PLSHAGGAFFLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 353 RLLNRLYDAITSKvqqqgfmaklvynfafARKLSlvkagkvgrdtiwdrlvfnkiqqqiggKVDLMVTGSAPISSTVLET 432
Cdd:PRK06188 264 TMIYALLDHPDLR----------------TRDLS---------------------------SLETVYYGASPMSPVRLAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 433 CRVTLGTTIVEGYGQTECTALATFTWMGDPSTGH------CGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGY 506
Cdd:PRK06188 301 AIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDpkrltsCGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMDGY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 507 YKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW--- 583
Cdd:PRK06188 380 WNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWgea 457
|
490
....*....|.
gi 17556552 584 LIAVVVPEPDV 594
Cdd:PRK06188 458 VTAVVVLRPGA 468
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
100-642 |
3.46e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 128.05 E-value: 3.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 100 ADYEFLTYDDVHEQAKNLSMTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAE 179
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGE--RIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 180 ISVVIVDsfkkaesliknrenmPTLKNiividSADELKDGTAIIDTIRVESLTNALNlgsRYPFTNNLPKPDDNYIICYT 259
Cdd:PRK06839 101 TTVLFVE---------------KTFQN-----MALSMQKVSYVQRVISITSLKEIED---RKIDNFVEKNESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 260 SGTTGTPKGVMLTHSNIVANIsgfLKILFAFQPSMIDatqVHISYLPLSHMmeqlthwtllgfgSKIGYFrgsiqgltdd 339
Cdd:PRK06839 158 SGTTGKPKGAVLTQENMFWNA---LNNTFAIDLTMHD---RSIVLLPLFHI-------------GGIGLF---------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 ikTLkPTVFP----VVPRllnrlydaitskvqqqgfmaklvyNFAFARKLSLVKAGKV----GRDTIWDRLV----FNKI 407
Cdd:PRK06839 209 --AF-PTLFAggviIVPR------------------------KFEPTKALSMIEKHKVtvvmGVPTIHQALIncskFETT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 408 QQQiggKVDLMVTGSAPisstvletCRVTL-------GTTIVEGYGQTEcTALATFTWMGDPS---TGHCGAPAPCALVK 477
Cdd:PRK06839 262 NLQ---SVRWFYNGGAP--------CPEELmrefidrGFLFGQGFGMTE-TSPTVFMLSEEDArrkVGSIGKPVLFCDYE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 478 LGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAP 557
Cdd:PRK06839 330 LID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 558 EKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPD-VLKEwndkqgsgsRKIEEICNDEKAK-----EFV-LSEL- 626
Cdd:PRK06839 407 LEVEQVINKLSDVYEVAVVGRQHVKWgeiPIAFIVKKSSsVLIE---------KDVIEHCRLFLAKykipkEIVfLKELp 477
|
570
....*....|....*..
gi 17556552 627 -HAIGKANKLNSIEQVK 642
Cdd:PRK06839 478 kNATGKIQKAQLVNQLK 494
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
234-573 |
1.11e-30 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 127.30 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 234 ALNLGSRYPFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfAFQPSMIDATQVHISYLPLSHMMeQ 313
Cdd:PRK08751 191 ALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWL-AGTGKLEEGCEVVITALPLYHIF-A 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 314 LTHWTLLGFgsKIGYFRGSI------QGLTDDIKTLKPTVFPVVPRLLNRLYDAitskvqqQGFmaklvynfafarklsl 387
Cdd:PRK08751 269 LTANGLVFM--KIGGCNHLIsnprdmPGFVKELKKTRFTAFTGVNTLFNGLLNT-------PGF---------------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 388 vkagkvgrdtiwDRLVFNKIQQQIGGkvdlmvtGSApISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMG-DPSTGH 466
Cdd:PRK08751 324 ------------DQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTlKEYNGS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 467 CGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHI 546
Cdd:PRK08751 384 IGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDM 462
|
330 340
....*....|....*....|....*..
gi 17556552 547 FkLAQGEYVAPEKIEQVYIRTPVVQQV 573
Cdd:PRK08751 463 I-LVSGFNVYPNEIEDVIAMMPGVLEV 488
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
106-577 |
4.65e-30 |
|
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: 124.95 E-value: 4.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:cd17642 46 SYAEYLEMSVRLAEAL-KKYGLKQNDR--IAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 dSFKKAESLIKNRENMPTLKNIIVIDSADELKdGTAIIDTIRVESLTNALNlgsRYPFT-NNLPKPDDNYIICYTSGTTG 264
Cdd:cd17642 123 -SKKGLQKVLNVQKKLKIIKTIIILDSKEDYK-GYQCLYTFITQNLPPGFN---EYDFKpPSFDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVANISGFLKILFAFQPsmIDATQVhISYLPLSHMMEQLTHWTLLGFGSKIGYfrgsiqgltddIKTLK 344
Cdd:cd17642 198 LPKGVQLTHKNIVARFSHARDPIFGNQI--IPDTAI-LTVIPFHHGFGMFTTLGYLICGFRVVL-----------MYKFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 345 PTVFpvvprlLNRLYDaitSKVQqqgfMAKLVYN-FAFARKLSLVKagkvgrdtiwdrlvfnkiqqqiggKVDL-----M 418
Cdd:cd17642 264 EELF------LRSLQD---YKVQ----SALLVPTlFAFFAKSTLVD------------------------KYDLsnlheI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 419 VTGSAPISSTVLETCRVTLGTTIV-EGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLNYFAKDGKGEIRI 497
Cdd:cd17642 307 ASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 498 KGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:cd17642 387 KGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG 465
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
250-659 |
2.31e-29 |
|
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: 123.31 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKiLFAFQ----PSMIDatqvhisYLPLSHMM--EQLTHWTLLGFG 323
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQ-TYPFFgeepPVLVD-------WLPWNHTFggNHNFNLVLYNGG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 324 S-KIGYFRGSIQGLTDDIKTLK---PTVFPVVPRLLNRLYDAI-TSKVQQQGFMAKLVYNFAFARKLSlvkagkvgrDTI 398
Cdd:cd05921 236 TlYIDDGKPMPGGFEETLRNLReisPTVYFNVPAGWEMLVAALeKDEALRRRFFKRLKLMFYAGAGLS---------QDV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 399 WDRLvfnkiqQQIGgkvdlmvtgsapisstvLETC--RVTLGTtiveGYGQTECTALATFT-WMGDPStGHCGAPAPCAL 475
Cdd:cd05921 307 WDRL------QALA-----------------VATVgeRIPMMA----GLGATETAPTATFThWPTERS-GLIGLPAPGTE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 476 VKLgdVPdlnyfaKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEML----PNGTIRIIDRKKHIFKLAQ 551
Cdd:cd05921 359 LKL--VP------SGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLAS 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 552 GEYVA--PEKIEQVYIRTPVVQQVYVDGDSLErWLIAVVVPEPDVLKEWNDKQGSGSrkiEEICNDEKAKEFVLSELHAI 629
Cdd:cd05921 431 GTWVSvgPLRARAVAACAPLVHDAVVAGEDRA-EVGALVFPDLLACRRLVGLQEASD---AEVLRHAKVRAAFRDRLAAL 506
|
410 420 430
....*....|....*....|....*....|
gi 17556552 630 GKANKLNSiEQVKKVILTSDTFTVENGLLT 659
Cdd:cd05921 507 NGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
239-611 |
2.45e-29 |
|
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: 121.33 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 239 SRYPFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKilfafqpsmidatqvhisylplsHMM--EQLTH 316
Cdd:cd05903 81 ERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAE-----------------------RLGlgPGDVF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 317 WTllgfGSKIGYFRGSIQGLTddiktlkptvfpvVPRLLNrlydaiTSKVQQQGFMAklvynfafARKLSLVKAGKV--- 393
Cdd:cd05903 138 LV----ASPMAHQTGFVYGFT-------------LPLLLG------APVVLQDIWDP--------DKALALMREHGVtfm 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 394 -GRDTIWDRLVfnKIQQQIGGKV---DLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHC-- 467
Cdd:cd05903 187 mGATPFLTDLL--NAVEEAGEPLsrlRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYtd 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 468 GAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAElFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIF 547
Cdd:cd05903 265 GRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-AAPEGWFRTGDLARLDEDGYLRITGRSKDII 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17556552 548 kLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEP------DVLKEWNDKQGSGSRKIEE 611
Cdd:cd05903 343 -IRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLgerACAVVVTKSgalltfDELVAYLDRQGVAKQYWPE 414
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
141-603 |
3.04e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 122.85 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 141 NSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDS----FKKAESLIKNRENMPTLKNIIVIDSADEl 216
Cdd:PRK13295 89 NWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKtfrgFDHAAMARRLRPELPALRHVVVVGGDGA- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 217 KDGTAIIDTIRVESLTNALNlgsryPFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPSMId 296
Cdd:PRK13295 168 DSFEALLITPAWEQEPDAPA-----ILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVI- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 297 atqvhisylplsHMMEQLTHWTLLGFGSKIGYFRGSIQGLTD--DiktlkptvfpvvPRLLNRLydaitskVQQQGfmak 374
Cdd:PRK13295 242 ------------LMASPMAHQTGFMYGLMMPVMLGATAVLQDiwD------------PARAAEL-------IRTEG---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 375 LVYNFAFARKLS-LVKAGKVGRDTIWDRLVFNkiqqqiggkvdlmvTGSAPISSTVLETCRVTLGTTIVEGYGQTECtAL 453
Cdd:PRK13295 287 VTFTMASTPFLTdLTRAVKESGRPVSSLRTFL--------------CAGAPIPGALVERARAALGAKIVSAWGMTEN-GA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 454 ATFTWMGDP---STGHCGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAElfDEEGFLQTGDIGE 530
Cdd:PRK13295 352 VTLTKLDDPderASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLAR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 531 MLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEP------DVLKEWNDK 601
Cdd:PRK13295 429 IDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLgerACAFVVPRPgqsldfEEMVEFLKA 507
|
..
gi 17556552 602 QG 603
Cdd:PRK13295 508 QK 509
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
105-593 |
1.33e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 120.84 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQECGVRKGD--RVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 V--DSFKKAESLIKNREnmptLKNIIVIDSADELKDGTAI--------------IDTIRVESLTNALNLGSRYPFTNnlP 248
Cdd:PRK08314 114 VgsELAPKVAPAVGNLR----LRHVIVAQYSDYLPAEPEIavpawlraepplqaLAPGGVVAWKEALAAGLAPPPHT--A 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 249 KPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGflkilfAFQPSMIDATQVHISYLPLSHmmeqlthwtLLGFGSKIG- 327
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVG------SVLWSNSTPESVVLAVLPLFH---------VTGMVHSMNa 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 328 --YFRGSIQGLT--------DDIKTLKPTVFPVVPRLlnrLYDaitskvqqqgFMAKLvyNFAfARKLSlvkagkvgrdt 397
Cdd:PRK08314 253 piYAGATVVLMPrwdreaaaRLIERYRVTHWTNIPTM---VVD----------FLASP--GLA-ERDLS----------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 398 iwdRLVFnkiqqqIGGkvdlmvtGSAPISSTVLETCRVTLGTTIVEGYGQTE----------------CTALATF---TW 458
Cdd:PRK08314 306 ---SLRY------IGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTEtmaqthsnppdrpklqCLGIPTFgvdAR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 459 MGDPSTghcGAPAPCalvklGDVpdlnyfakdgkGEIRIKGPCVTKGYYKDPERTAELFDE-EG--FLQTGDIGEMLPNG 535
Cdd:PRK08314 370 VIDPET---LEELPP-----GEV-----------GEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEG 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17556552 536 TIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLER---WLIAVVVPEPD 593
Cdd:PRK08314 431 YFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACVIATPDPRrgeTVKAVVVLRPE 490
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
105-577 |
1.79e-28 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 120.51 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVV---PLY----------DTlGAEAa 171
Cdd:PRK07059 49 ITYGELDELSRALAAWL-QSRGLAKGA--RVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYtprelehqlkDS-GAEA- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 172 tfiisqaeisVVIVDSFKKAESLIKNRENmptLKNIIVIDSADELKDGTAIIDTI--RVESLTNALNLGSRYPFTNNLPK 249
Cdd:PRK07059 124 ----------IVVLENFATTVQQVLAKTA---VKHVVVASMGDLLGFKGHIVNFVvrRVKKMVPAWSLPGHVRFNDALAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 ------------PDDNYIICYTSGTTGTPKGVMLTHSNIVANIsgfLKILFAFQPSMIDATQVH----ISYLPLSHMMeQ 313
Cdd:PRK07059 191 garqtfkpvklgPDDVAFLQYTGGTTGVSKGATLLHRNIVANV---LQMEAWLQPAFEKKPRPDqlnfVCALPLYHIF-A 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 314 LTHWTLLGF-----GSKIGYFRgSIQGLTDDIKTLKPTVFPVVprllNRLYDAitskvqqqgfmakLVYNFAFarklslv 388
Cdd:PRK07059 267 LTVCGLLGMrtggrNILIPNPR-DIPGFIKELKKYQVHIFPAV----NTLYNA-------------LLNNPDF------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 389 kagkvgrdtiwDRLVFNKIQQQIGGkvdlmvtGSApISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPS-TGHC 467
Cdd:PRK07059 322 -----------DKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEfSGTI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 468 GAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIF 547
Cdd:PRK07059 383 GLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
490 500 510
....*....|....*....|....*....|
gi 17556552 548 kLAQGEYVAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:PRK07059 462 -LVSGFNVYPNEIEEVVASHPGVLEVAAVG 490
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
106-602 |
5.80e-28 |
|
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: 117.01 E-value: 5.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLvHEFGLTPAntTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:cd05934 5 TYAELLRESARIAAAL-AALGIRPG--DRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 DSFkkaesliknrenmptlkniividsadelkdgtAIIdtirvesltnalnlgsrypftnnlpkpddnyiicYTSGTTGT 265
Cdd:cd05934 82 DPA--------------------------------SIL----------------------------------YTSGTTGP 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 266 PKGVMLTHSNIVanisgFLKILFAFQpSMIDATQVHISYLPLSHMMEQLTHWTL-LGFGSKIGYF-RGSIQGLTDDIKTL 343
Cdd:cd05934 96 PKGVVITHANLT-----FAGYYSARR-FGLGEDDVYLTVLPLFHINAQAVSVLAaLSVGATLVLLpRFSASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 344 KPTVFPVVPRLLNRLYDAITSKVQqqgfmaklvynfafarklslvKAGKVgrdtiwdRLVFnkiqqqiggkvdlmvtgSA 423
Cdd:cd05934 170 GATVTNYLGAMLSYLLAQPPSPDD---------------------RAHRL-------RAAY-----------------GA 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 424 PISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDvpDLNYFAKDGK-GEIRIK---G 499
Cdd:cd05934 205 PNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD--DDGQELPAGEpGELVIRglrG 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 500 PCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTPVVQQVYV---- 575
Cdd:cd05934 283 WGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREAAVvavp 360
|
490 500 510
....*....|....*....|....*....|..
gi 17556552 576 DGDSLERWLIAVVVPE-----PDVLKEWNDKQ 602
Cdd:cd05934 361 DEVGEDEVKAVVVLRPgetldPEELFAFCEGQ 392
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
258-593 |
6.64e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 118.54 E-value: 6.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISgflKILFAFQPSMIDATqVHISYLPLSHM--MEQLTHWTLLGFGSKIGYFRGSIQG 335
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVANLC---SSLFSVGPEMIGQV-VTLGLIPFFHIygITGICCATLRNKGKVVVMSRFELRT 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 336 LTDDIKTLKPTVFPVVPRLLnrlydaitskvqqqgfmaklvynfafarkLSLVKagkvgrDTIWDRLVFNKIqqqiggKV 415
Cdd:PLN02330 267 FLNALITQEVSFAPIVPPII-----------------------------LNLVK------NPIVEEFDLSKL------KL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 416 DLMVTGSAPISSTVLETCRVTL-GTTIVEGYGQTECTALaTFTwMGDPSTGH-------CGAPAPCALVKLGDVPDLNYF 487
Cdd:PLN02330 306 QAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCI-TLT-HGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSL 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 488 AKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRT 567
Cdd:PLN02330 384 PKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTH 462
|
330 340
....*....|....*....|....*.
gi 17556552 568 PVVQQvyvdgdslerwliAVVVPEPD 593
Cdd:PLN02330 463 PSVED-------------AAVVPLPD 475
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
248-597 |
8.08e-28 |
|
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: 116.29 E-value: 8.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISG------------FLKILFAFqpsmidatqvHISylPLSHMMEQLt 315
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGsalnlglteddnWLCALPLF----------HIS--GLSILMRSV- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 316 hwtLLGFgSKIGYFRGSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAitskvqqqgFMAKLVYNFAfarklslvkagkvgr 395
Cdd:cd05912 141 ---IYGM-TVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEI---------LGEGYPNNLR--------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 396 dtiwdrlvfnkiqqqiggkvdLMVTGSAPISSTVLETCRvTLGTTIVEGYGQTE-CTALATFTW-MGDPSTGHCGAPAPC 473
Cdd:cd05912 193 ---------------------CILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTEtCSQIVTLSPeDALNKIGSAGKPLFP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 474 ALVKLGDvpdlNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGE 553
Cdd:cd05912 251 VELKIED----DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGE 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 17556552 554 YVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDVLKE 597
Cdd:cd05912 325 NIYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvPVAFVVSERPISEE 371
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
90-577 |
1.37e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 118.22 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 90 PCVGTRSSGDADYEFLTYDDVHEQAKNLSMTLVhEFGLTPAntTNIGIYARNSPQWLVSAVACVEQSMVVVPL---YDTL 166
Cdd:PRK12582 66 PWLAQREPGHGQWRKVTYGEAKRAVDALAQALL-DLGLDPG--RPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 167 GAEAAT--FIISQAEISVVIVDS---FKKAesLIKNRENMPTLkniIVIDSADELKDGTAIID------TIRVESLTNAL 235
Cdd:PRK12582 143 SHDHAKlkHLFDLVKPRVVFAQSgapFARA--LAALDLLDVTV---VHVTGPGEGIASIAFADlaatppTAAVAAAIAAI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 236 NlgsrypftnnlpkPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGfLKILFAFQPSmiDATQVHISYLPLSHMM--EQ 313
Cdd:PRK12582 218 T-------------PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAM-QEQLRPREPD--PPPPVSLDWMPWNHTMggNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 314 LTHWTLLGFGSKI--------GYFRGSIQGLTDdiktLKPTVFPVVPRLLNRLYDAItskvQQQGFMAKlvynfAFARKL 385
Cdd:PRK12582 282 NFNGLLWGGGTLYiddgkplpGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAM----EKDDALRR-----SFFKNL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 386 SLVK-AGKVGRDTIWDRlvfnkIQqqiggkvDLMV--TGSapisstvletcRVTLGTtiveGYGQTECTALATFTWMGDP 462
Cdd:PRK12582 349 RLMAyGGATLSDDLYER-----MQ-------ALAVrtTGH-----------RIPFYT----GYGATETAPTTTGTHWDTE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 463 STGHCGAPAPCALVKLGDVPDlnyfakdgKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEML----PNGTIR 538
Cdd:PRK12582 402 RVGLIGLPLPGVELKLAPVGD--------KYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLI 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 17556552 539 IIDRKKHIFKLAQGEYV--APEKIEQVYIRTPVVQQVYVDG 577
Cdd:PRK12582 474 FDGRVAEDFKLSTGTWVsvGTLRPDAVAACSPVIHDAVVAG 514
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
105-582 |
5.14e-27 |
|
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: 114.50 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSmTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKGVRKGD--RVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfkkaesliknrenmptlkniividsadELkdgtaiidtirvesltnalnlgsrypftnnlpkpDDNYIICYTSGTTG 264
Cdd:cd05935 79 VGS---------------------------EL----------------------------------DDLALIPYTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVANISGflkILFAFqpsMIDATQVHISYLPLSHM--MEQLTHWTLLGFGSKIGYFRGSIQGLTDDIKT 342
Cdd:cd05935 98 LPKGCMHTHFSAAANALQ---SAVWT---GLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 343 LKPTVFPVVPRLLNRLydaitskvqqqgfMAKLvyNFAfARKLSLVKagkvgrdtiwdrlvfnkiqqqiggkvdLMVTGS 422
Cdd:cd05935 172 YKVTFWTNIPTMLVDL-------------LATP--EFK-TRDLSSLK---------------------------VLTGGG 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 423 APISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLNYFAKDGKGEIRIKGPCV 502
Cdd:cd05935 209 APMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 503 TKGYYKDPERTAELFDEEG---FLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQVYVDGDS 579
Cdd:cd05935 289 FKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVISVP 367
|
...
gi 17556552 580 LER 582
Cdd:cd05935 368 DER 370
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
250-598 |
2.37e-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.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 110.83 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANiSGFLKILFAFQPSMIDATQVhisylPLSHMmeqlthwtllgFGSKIGYF 329
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIGERLGLTEQDRLCIPV-----PLFHC-----------FGSVLGVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 330 RGSIQGLTddiktlkpTVFPvvprllNRLYDAITSKVQQQGFMAKLVYNFA--FARKLSLVKAGKVGRDTIwdRlvfnki 407
Cdd:cd05917 64 ACLTHGAT--------MVFP------SPSFDPLAVLEAIEKEKCTALHGVPtmFIAELEHPDFDKFDLSSL--R------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 408 qqqiGGkvdlmVTGSAPISSTVLETCRVTLGTT-IVEGYGQTECTALATFTWMGDP------STGHcgaPAPCALVKLGD 480
Cdd:cd05917 122 ----TG-----IMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETSPVSTQTRTDDSiekrvnTVGR---IMPHTEAKIVD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 481 -----VPDLNYfakdgKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYV 555
Cdd:cd05917 190 peggiVPPVGV-----PGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENI 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17556552 556 APEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDV------LKEW 598
Cdd:cd05917 264 YPREIEEFLHTHPKVSDVQVVGVPDERYgeeVCAWIRLKEGAelteedIKAY 315
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
256-582 |
4.80e-26 |
|
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: 109.51 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 256 ICYTSGTTGTPKGVMLTHSNIVAnisgflkiLFAFQPSMIDATQVHiSYL---PLSHMmeqlthwtllgFGSKIGYFRGS 332
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLR--------AAAAWADCADLTEDD-RYLiinPFFHT-----------FGYKAGIVACL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 333 IQGLT-------------DDIKTLKPTVFPVVPRLLNRLYDAITSKvqqqgfmaklvyNFafarKLSLVKAGkvgrdtiw 399
Cdd:cd17638 65 LTGATvvpvavfdvdailEAIERERITVLPGPPTLFQSLLDHPGRK------------KF----DLSSLRAA-------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 400 drlvfnkiqqqiggkvdlmVTGSAPISSTVLETCRVTLG-TTIVEGYGQTECtALATFTWMGDPST---GHCGAPAPCAL 475
Cdd:cd17638 121 -------------------VTGAATVPVELVRRMRSELGfETVLTAYGLTEA-GVATMCRPGDDAEtvaTTCGRACPGFE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 476 VKLGDvpdlnyfakdgKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYV 555
Cdd:cd17638 181 VRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNV 248
|
330 340
....*....|....*....|....*..
gi 17556552 556 APEKIEQVYIRTPVVQQVYVDGDSLER 582
Cdd:cd17638 249 YPAEVEGALAEHPGVAQVAVIGVPDER 275
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
259-633 |
5.73e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 113.05 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 259 TSGTTGTPKGVMLTHSNIVANISGFLKiLFAF----QPSMIDatqvhisYLPLSHmmeqlthwtllGFGSK--IG---YF 329
Cdd:PRK08180 217 TSGSTGLPKAVINTHRMLCANQQMLAQ-TFPFlaeePPVLVD-------WLPWNH-----------TFGGNhnLGivlYN 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 330 RGSI---------QGLTDDIKTLK---PTVFPVVPRLlnrlYDAITSKVQQQgfmAKLVYNFaFARKLSLVKAGKVGRDT 397
Cdd:PRK08180 278 GGTLyiddgkptpGGFDETLRNLReisPTVYFNVPKG----WEMLVPALERD---AALRRRF-FSRLKLLFYAGAALSQD 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 398 IWDRLvfNKIQQQIGGKvdlmvtgsapisstvletcRVTLGTtiveGYGQTECTALATFTWMGDPSTGHCGAPAPCALVK 477
Cdd:PRK08180 350 VWDRL--DRVAEATCGE-------------------RIRMMT----GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVK 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 478 LgdVPDlnyfakDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEML----PNGTIRIIDRKKHIFKLAQGE 553
Cdd:PRK08180 405 L--VPV------GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGT 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 554 YVA--PEKIEQVYIRTPVVQQVYVDGDSLERwLIAVVVPEPDVLKEWNDKQGSGSrkIEEICNDEKAKEFV---LSELHA 628
Cdd:PRK08180 477 WVSvgPLRARAVSAGAPLVQDVVITGHDRDE-IGLLVFPNLDACRRLAGLLADAS--LAEVLAHPAVRAAFrerLARLNA 553
|
....*
gi 17556552 629 IGKAN 633
Cdd:PRK08180 554 QATGS 558
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
105-596 |
1.29e-25 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 111.74 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVeqSM--VVVPLYDTLGAEAATFIISQAEISV 182
Cdd:COG0365 40 LTYAELRREVNRFANAL-RALGVKKGDR--VAIYLPNIPEAVIAMLACA--RIgaVHSPVFPGFGAEALADRIEDAEAKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 VIVDS--------FKKAESLIKNRENMPTLKNIIVIDS-------------ADELKDGTAIIDTIRVESltnalnlgsry 241
Cdd:COG0365 115 LITADgglrggkvIDLKEKVDEALEELPSLEHVIVVGRtgadvpmegdldwDELLAAASAEFEPEPTDA----------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 242 pftnnlpkpDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPsmidaTQVHISYLPLSHMMeqlTHWTL-- 319
Cdd:COG0365 184 ---------DDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKP-----GDVFWCTADIGWAT---GHSYIvy 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 320 --LGFGSKIGYFRGSI-----QGLTDDIKTLKPTVFPVVP---RLLNRLYDAITSKvqqqgfmaklvYNFAfarklSLvk 389
Cdd:COG0365 247 gpLLNGATVVLYEGRPdfpdpGRLWELIEKYGVTVFFTAPtaiRALMKAGDEPLKK-----------YDLS-----SL-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 390 agkvgrdtiwdRLvfnkiqqqiggkvdLMVTGSaPISSTVLETCRVTLGTTIVEGYGQTE-CTALATFTWMGDPSTGHCG 468
Cdd:COG0365 309 -----------RL--------------LGSAGE-PLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFISNLPGLPVKPGSMG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 469 APAPCALVKLGDvPDLNYFAKDGKGEIRIKG--PCVTKGYYKDPERTAELF--DEEGFLQTGDIGEMLPNGTIRIIDRKK 544
Cdd:COG0365 363 KPVPGYDVAVVD-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSD 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 17556552 545 HIFKLAqGEYVAPEKIEQVYIRTPVVQQvyvdgdslerwliAVVVPEPDVLK 596
Cdd:COG0365 442 DVINVS-GHRIGTAEIESALVSHPAVAE-------------AAVVGVPDEIR 479
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
108-577 |
1.95e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 111.02 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 108 DDVHEQAKNLsMTLvhefGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI-VD 186
Cdd:PRK12583 53 DAVDRLARGL-LAL----GVQPGD--RVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIcAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 187 SFKKAE------SLIKNR----------ENMPTLKNIIVIDSAD--------ELKDGTAIIDTIRVESLTNALNlgsryp 242
Cdd:PRK12583 126 AFKTSDyhamlqELLPGLaegqpgalacERLPELRGVVSLAPAPppgflawhELQARGETVSREALAERQASLD------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 243 ftnnlpkPDDNYIICYTSGTTGTPKGVMLTHSNIVANisgflkilfafqpsmidatqvhisylplshmmeqlthwtllgf 322
Cdd:PRK12583 200 -------RDDPINIQYTSGTTGFPKGATLSHHNILNN------------------------------------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 323 gskiGYFRGSIQGLTDDIKTLKPtvfpvVPrllnrLYDAITSKVQQQGFM---AKLVY-NFAFARKLSLVKAGKVGRDTI 398
Cdd:PRK12583 230 ----GYFVAESLGLTEHDRLCVP-----VP-----LYHCFGMVLANLGCMtvgACLVYpNEAFDPLATLQAVEEERCTAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 399 WD--RLVFNKIQQQIGGKVDL--MVTGSAPISSTVLETCRVTLG----TTIVEGYGQTECTALATFTWMGDP---STGHC 467
Cdd:PRK12583 296 YGvpTMFIAELDHPQRGNFDLssLRTGIMAGAPCPIEVMRRVMDemhmAEVQIAYGMTETSPVSLQTTAADDlerRVETV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 468 GAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIF 547
Cdd:PRK12583 376 GRTQPHLEVKVVD-PDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510
....*....|....*....|....*....|
gi 17556552 548 kLAQGEYVAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:PRK12583 455 -IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
121-594 |
3.74e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 109.07 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 121 LVHEFGLTPANTTNIGIYARNSPQWLVSAVACVEQ--SMVVVPLYDTLGAEAATFIISQAEISVVIVDsfKKAESLIKnr 198
Cdd:cd05922 9 ALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlGLVFVPLNPTLKESVLRYLVADAGGRIVLAD--AGAADRLR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 199 enmptlknIIVIDSADelkDGTaiidTIRVESLTNALNLGSRYPftnnlPKPDDNYIICYTSGTTGTPKGVMLTHSNIVA 278
Cdd:cd05922 85 --------DALPASPD---PGT----VLDADGIRAARASAPAHE-----VSHEDLALLLYTSGSTGSPKLVRLSHQNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 279 N---ISGFLKilfafqpsmIDATQVHISYLPLSHM--MEQLTHWTLLGfGSKIGYFRGSI-QGLTDDIKTLKPTVFPVVP 352
Cdd:cd05922 145 NarsIAEYLG---------ITADDRALTVLPLSYDygLSVLNTHLLRG-ATLVLTNDGVLdDAFWEDLREHGATGLAGVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 353 rllnrlydaitskvqqqgfmaklvYNFAfarklslvkagkvgrdtIWDRLVFNKIQ-------QQIGGKVDlmvtgsapi 425
Cdd:cd05922 215 ------------------------STYA-----------------MLTRLGFDPAKlpslrylTQAGGRLP--------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 426 SSTVLETCRVTLGTTIVEGYGQTECTALATFTwmgDP-----STGHCGAPAP-CALVKLGDvpDLNYFAKDGKGEIRIKG 499
Cdd:cd05922 245 QETIARLRELLPGAQVYVMYGQTEATRRMTYL---PPerileKPGSIGLAIPgGEFEILDD--DGTPTPPGEPGEIVHRG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 500 PCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQVYV--DG 577
Cdd:cd05922 320 PNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAARSIGLIIEAAAvgLP 398
|
490
....*....|....*..
gi 17556552 578 DSLERWLIAVVVPEPDV 594
Cdd:cd05922 399 DPLGEKLALFVTAPDKI 415
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
248-594 |
7.75e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 108.54 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGfLKILFAFQPsmiDATQVHisYLPLSHMmeqltHWTLLG-FGS-K 325
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDA-LAEAWQWTA---DDVLVH--GLPLFHV-----HGLVLGvLGPlR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 326 IGyfrGSIqgltddIKTLKPTvfPVvprllnrlydaitskvqqqgfmaklvynfAFARKLSLVKAGKVGRDTIWDRLVFN 405
Cdd:PRK07787 194 IG---NRF------VHTGRPT--PE-----------------------------AYAQALSEGGTLYFGVPTVWSRIAAD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 406 KIQQQIGGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTE----CTALATftwmGDPSTGHCGAPAPCALVKLGDV 481
Cdd:PRK07787 234 PEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTEtlitLSTRAD----GERRPGWVGLPLAGVETRLVDE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 PDlNYFAKDGK--GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDR------KKHIFKLAQGE 553
Cdd:PRK07787 310 DG-GPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17556552 554 yvapekIEQVYIRTPVVQQVYVDG---DSLERWLIAVVVPEPDV 594
Cdd:PRK07787 389 ------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDV 426
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
105-529 |
1.55e-24 |
|
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: 108.09 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHefgLTPANTTnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAA---TFIISQAEIS 181
Cdd:cd05931 25 LTYAELDRRARAIAARLQA---VGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAerlAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 182 VVIVDSfkKAESLIKNRENMPTLKNIIVIDSADELKDGTAiidtirvesltnalnlgsrYPFTNNLPKPDDNYIICYTSG 261
Cdd:cd05931 101 VVLTTA--AALAAVRAFAASRPAAGTPRLLVVDLLPDTSA-------------------ADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 262 TTGTPKGVMLTHSNIVANISGflkILFAFQpsmIDATQVHISYLPLSHMMeqlthwtllgfgskigyfrGSIQGLtddik 341
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQ---IRRAYG---LDPGDVVVSWLPLYHDM-------------------GLIGGL----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 342 tLKPTV--FPVV----------P----RLLNRlYDAITSKVQqqgfmaklvyNFAFArklslvkagkvgrdtiwdrLVFN 405
Cdd:cd05931 210 -LTPLYsgGPSVlmspaaflrrPlrwlRLISR-YRATISAAP----------NFAYD-------------------LCVR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 406 KIQ-QQIGGkVDL-----MVTGSAPISSTVLETCRVTLG------TTIVEGYGQTECTALATFTWMGDPSTGH------- 466
Cdd:cd05931 259 RVRdEDLEG-LDLsswrvALNGAEPVRPATLRRFAEAFApfgfrpEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdal 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 467 -------------------CGAPAPCALVKLGDvPDLNYFAKDGK-GEIRIKGPCVTKGYYKDPERTAELF------DEE 520
Cdd:cd05931 338 agravavaaddpaarelvsCGRPLPDQEVRIVD-PETGRELPDGEvGEIWVRGPSVASGYWGRPEATAETFgalaatDEG 416
|
....*....
gi 17556552 521 GFLQTGDIG 529
Cdd:cd05931 417 GWLRTGDLG 425
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
105-590 |
2.11e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 107.66 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEfGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRS-GLLPGDR--VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSFKKAEsliKNRENMPTLKNIIVIDSADELKDGTAIIDtirvesLTNALNLGSRYPFTNNLpKPDDNYIIcYTSGTTG 264
Cdd:PRK05852 121 IDADGPHD---RAEPTTRWWPLTVNVGGDSGPSGGTLSVH------LDAATEPTPATSTPEGL-RPDDAMIM-FTGGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVANISGflkILFAFQPSMIDATqvhISYLPLSH---MMEQLTHwTLLGFGSKIGYFRGSIQGLT--DD 339
Cdd:PRK05852 190 LPKMVPWTHANIASSVRA---IITGYRLSPRDAT---VAVMPLYHghgLIAALLA-TLASGGAVLLPARGRFSAHTfwDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 IKTLKPTVFPVVPRLLNRLydaitskvqqqgfmaklvynfafarkLSLVKAGKVGRDTIWDRLVfnkiqqqiggkvdlmV 419
Cdd:PRK05852 263 IKAVGATWYTAVPTIHQIL--------------------------LERAATEPSGRKPAALRFI---------------R 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 TGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPcALVKLGDVPDLNYFAKDGK------- 492
Cdd:PRK05852 302 SCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTENPVVST-GLVGRSTGAQIRIVGSDGLplpagav 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:PRK05852 381 GEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVME 458
|
490 500
....*....|....*....|.
gi 17556552 573 VYVDGDSLERW---LIAVVVP 590
Cdd:PRK05852 459 AAVFGVPDQLYgeaVAAVIVP 479
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
251-628 |
3.79e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 107.04 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 251 DDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFafqpSMIDATQVHISYLPLSHmmeqlthwtllgfgskigyfr 330
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLY----NCKEGEEVVLGVLPFFH--------------------- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 331 gsIQGLTddiktlkptvfpvvprllnrlydAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKV----GRDTIWDRLVFNK 406
Cdd:PRK06710 261 --VYGMT-----------------------AVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVtlfpGAPTIYIALLNSP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 IQQQIG-GKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTAL--ATFTWMgDPSTGHCGAPAPCALVKLGDVPD 483
Cdd:PRK06710 316 LLKEYDiSSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVthSNFLWE-KRVPGSIGVPWPDTEAMIMSLET 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 484 LNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQV 563
Cdd:PRK06710 395 GEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEV 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17556552 564 YIRTPVVQQVYVDGdslerwliavvVPEPD---------VLKEwndkqgsgsrkiEEICNDEKAKEFVLSELHA 628
Cdd:PRK06710 473 LYEHEKVQEVVTIG-----------VPDPYrgetvkafvVLKE------------GTECSEEELNQFARKYLAA 523
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
247-577 |
4.11e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 106.85 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 247 LPKP----DDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKilfaFQPSMIDAT---QVHISYLPLSHMME-QLTHWT 318
Cdd:PLN02574 190 VPKPvikqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVR----FEASQYEYPgsdNVYLAALPMFHIYGlSLFVVG 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 319 LLGFGSKIGYFRG-SIQGLTDDIKTLKPTVFPVVPRLLnrlydaitskvqqqgfmaklvynfafarkLSLVKAGKVGRDT 397
Cdd:PLN02574 266 LLSLGSTIVVMRRfDASDMVKVIDRFKVTHFPVVPPIL-----------------------------MALTKKAKGVCGE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 398 IWDRLVfnkiqqqiggkvdLMVTGSAPISSTVLETCRVTLG-TTIVEGYGQTECTALAT--FTWMGDPSTGHCGAPAPCA 474
Cdd:PLN02574 317 VLKSLK-------------QVSCGAAPLSGKFIQDFVQTLPhVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNM 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLGDVPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEY 554
Cdd:PLN02574 384 QAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQ 462
|
330 340
....*....|....*....|...
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:PLN02574 463 IAPADLEAVLISHPEIIDAAVTA 485
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
106-575 |
4.16e-24 |
|
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: 105.43 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLVHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDR--VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 DSfkkaesliKNRENMPTLkniividsadelkDGTAIIDTIRVESLTNALNLGSRypfTNNLPKPDDN-YIIcYTSGTTG 264
Cdd:TIGR01733 79 DS--------ALASRLAGL-------------VLPVILLDPLELAALDDAPAPPP---PDAPSGPDDLaYVI-YTSGSTG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVANISGFLKILFafqpsmIDATQVHISYLPLSH---MMEQLthWTLLGFGSKIGYFRGSIQG----LT 337
Cdd:TIGR01733 134 RPKGVVVTHRSLVNLLAWLARRYG------LDPDDRVLQFASLSFdasVEEIF--GALLAGATLVVPPEDEERDdaalLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 DDIKTLKPTVFPVVPRLLNRLYDAitskvqqqgfmaklvynfAFARKLSLvkagkvgrdtiwdRLVFnkiqqqiggkvdl 417
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAAA------------------LPPALASL-------------RLVI------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 418 mVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALAT-FTWMGDPSTGHC----GAPAPCALVKLGDvPDLNYFAKDGK 492
Cdd:TIGR01733 242 -LGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELF--------DEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVY 564
Cdd:TIGR01733 320 GELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAAL 398
|
490
....*....|.
gi 17556552 565 IRTPVVQQVYV 575
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
105-590 |
1.05e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 105.40 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK08316 37 WTYAELDAAVNRVAAAL-LDLGLKKGD--RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfkkaesliknrENMPTLKNIIVIDSADELKDGTAIIDTIRVESLTNALNLGSRYPFTNNLPKPDDNYI--ICYTSGT 262
Cdd:PRK08316 114 VDP-----------ALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELADDDLaqILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 263 TGTPKGVMLTHSNIVANisgflkilfaFQPSMID----ATQVHISYLPLSH-------MMEQLthwtLLGFGSKIgyfrg 331
Cdd:PRK08316 183 ESLPKGAMLTHRALIAE----------YVSCIVAgdmsADDIPLHALPLYHcaqldvfLGPYL----YVGATNVI----- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 332 siqgltddiktlkpTVFPVVPRLLNRL-YDAITSKvqqqgFMAKLVY-------NFAFARKLSLVKAgkvgrdtiwdrlv 403
Cdd:PRK08316 244 --------------LDAPDPELILRTIeAERITSF-----FAPPTVWisllrhpDFDTRDLSSLRKG------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 404 fnkiqqqiggkvdlmVTGSAPISSTVLETCRVTL-GTTIVEGYGQTECTALATFtwMG----DPSTGHCGAPAPCALVKL 478
Cdd:PRK08316 292 ---------------YYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATV--LGpeehLRRPGSAGRPVLNVETRV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 479 GDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPE 558
Cdd:PRK08316 355 VD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASR 431
|
490 500 510
....*....|....*....|....*....|....*
gi 17556552 559 KIEQVYIRTPVVQQVYVDGDSLERWL---IAVVVP 590
Cdd:PRK08316 432 EVEEALYTHPAVAEVAVIGLPDPKWIeavTAVVVP 466
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
246-591 |
1.36e-23 |
|
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: 104.31 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 246 NLPKPDDN-YIIcYTSGTTGTPKGVMLTHSNIVANISgflkilfaFQPSMIDATqvhisylPLSHMMEQLThwtlLGFGS 324
Cdd:cd17653 100 TTDSPDDLaYII-FTSGSTGIPKGVMVPHRGVLNYVS--------QPPARLDVG-------PGSRVAQVLS----IAFDA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 325 KIG------------YFRGSIQGLTDDIKTLkpTVFPVVPRLLNRLydaitskvqqqgfmaklvynfafarklslvkagk 392
Cdd:cd17653 160 CIGeifstlcnggtlVLADPSDPFAHVARTV--DALMSTPSILSTL---------------------------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 393 vgRDTIWDRLvfnkiqqqiggkvDLMVTGSAPISSTVLETCRvtLGTTIVEGYGQTECTALATFT--WMGDPSTghCGAP 470
Cdd:cd17653 204 --SPQDFPNL-------------KTIFLGGEAVPPSLLDRWS--PGRRLYNAYGPTECTISSTMTelLPGQPVT--IGKP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 471 APCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGF------LQTGDIGEMLPNGTIRIIDRKK 544
Cdd:cd17653 265 IPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGRED 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17556552 545 HIFKLaQGEYVAPEKIEQVYIRT-PVVQQVY--VDGDSlerwLIAVVVPE 591
Cdd:cd17653 344 NQVKV-RGFRINLEEIEEVVLQSqPEVTQAAaiVVNGR----LVAFVTPE 388
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
105-593 |
1.48e-23 |
|
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: 104.15 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEfGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd05930 13 LTYAELDARANRLARYLRER-GVGP--GDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDsfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpkPDDN-YIIcYTSGTT 263
Cdd:cd05930 90 TD---------------------------------------------------------------PDDLaYVI-YTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNIVANISGFLKIL-------FAFQPSMI-DATQVHIsYLPLS-----HMMEQLTHwtllgfgskigyfr 330
Cdd:cd05930 106 GKPKGVMVEHRGLVNLLLWMQEAYpltpgdrVLQFTSFSfDVSVWEI-FGALLagatlVVLPEEVR-------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 331 GSIQGLTDDIKTLKPTVFPVVPRLLNrlydaitskvqqqgfmaklvynfafarklSLVKAGKVGRDTIWDRLvfnkiqqq 410
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLR-----------------------------LLLQELELAALPSLRLV-------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 411 iggkvdlMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGH----CGAPAPC--ALV---KLGDV 481
Cdd:cd05930 214 -------LVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDgrvpIGRPIPNtrVYVldeNLRPV 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 PDlnyfakdGK-GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQ------TGDIGEMLPNGTIRIIDRKKHIFKLAqGEY 554
Cdd:cd05930 287 PP-------GVpGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYR 358
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYV----DGDSLERwLIAVVVPEPD 593
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVvareDGDGEKR-LVAYVVPDEG 400
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
249-562 |
1.89e-23 |
|
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: 104.34 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 249 KPDDNYIICYTSGTTGTPKGVMLTHSNIVANISgflKILFAFQPSMIDatqVHISYLPLSHMMeqlthwtllgfgskigy 328
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVE---QITAIFDPNPED---VVFGALPFFHSF----------------- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 329 frgsiqGLTDDIKTLKPTVFPVV--PRLLNrlydaitskvqqqgfmAKLVYNFAFARKLSLVkagkVGRDTIWDRLVFNK 406
Cdd:cd05909 202 ------GLTGCLWLPLLSGIKVVfhPNPLD----------------YKKIPELIYDKKATIL----LGTPTFLRGYARAA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 IQQQIGGkVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATF-TWMGDPSTGHCGAPAPCALVKLGDVPDLN 485
Cdd:cd05909 256 HPEDFSS-LRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKIVSVETHE 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556552 486 YFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQ 562
Cdd:cd05909 335 EVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIED 409
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
259-598 |
6.34e-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: 100.10 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 259 TSGTTGTPKGVMLTHSNIVANISGFLKiLFAFqpsmiDATQVHISYLPLSHM--MEQLTHWTLLGfgsKIGYFRGSIQGL 336
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAAGLHS-RLGF-----GGGDSWLLSLPLYHVggLAILVRSLLAG---AELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 337 TDDIKTLKPTVFPVVPRLLNRLydaitskvqqqgfmakLVYNFAFARKLSLvkagkvgrdtiwdRLVFnkiqqqIGGkvd 416
Cdd:cd17630 79 AEDLAPPGVTHVSLVPTQLQRL----------------LDSGQGPAALKSL-------------RAVL------LGG--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 417 lmvtgsAPISSTVLETCRvTLGTTIVEGYGQTEcTALATFTW-MGDPSTGHCGAPAPCALVKLgdVPDlnyfakdgkGEI 495
Cdd:cd17630 121 ------APIPPELLERAA-DRGIPLYTTYGMTE-TASQVATKrPDGFGRGGVGVLLPGRELRI--VED---------GEI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 496 RIKGPCVTKGYYKDPERtaELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYV 575
Cdd:cd17630 182 WVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFV 258
|
330 340 350
....*....|....*....|....*....|
gi 17556552 576 DGDSLERW---LIAVVV----PEPDVLKEW 598
Cdd:cd17630 259 VGVPDEELgqrPVAVIVgrgpADPAELRAW 288
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
101-594 |
7.13e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 102.65 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSMTLVHEfGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPL---YdTLgAEAATFIiSQ 177
Cdd:PRK07514 25 DGLRYTYGDLDAASARLANLLVAL-GVKPGD--RVAVQVEKSPEALALYLATLRAGAVFLPLntaY-TL-AELDYFI-GD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 178 AEISVVIVDSfkkaesliknrENMPTLKNIIVidsadelKDGTAIIDTI---RVESLTnALNLGSRYPFTNNLPKPDDNY 254
Cdd:PRK07514 99 AEPALVVCDP-----------ANFAWLSKIAA-------AAGAPHVETLdadGTGSLL-EAAAAAPDDFETVPRGADDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 255 IICYTSGTTGTPKGVMLTHSNIVANiSGFLKILFAFQPsmidaTQVHISYLPLSHMmEQL---THWTLLGFGSKIgyFRG 331
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSN-ALTLVDYWRFTP-----DDVLIHALPIFHT-HGLfvaTNVALLAGASMI--FLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 332 SIQglTDDIKTLKP--TVFPVVPRLLNRLydaitskVQQQGFMAKLVynfafarklslvkagkvgrdtiwdrlvfnkiqq 409
Cdd:PRK07514 231 KFD--PDAVLALMPraTVMMGVPTFYTRL-------LQEPRLTREAA--------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 410 qigGKVDLMVTGSAPIsstVLETCR----VTlGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDLN 485
Cdd:PRK07514 269 ---AHMRLFISGSAPL---LAETHRefqeRT-GHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 486 YFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIfkLAQGEY-VAPEKIEQVY 564
Cdd:PRK07514 342 ELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEGEI 419
|
490 500 510
....*....|....*....|....*....|....
gi 17556552 565 IRTPVVQQVYVDG----DSLERwLIAVVVPEPDV 594
Cdd:PRK07514 420 DELPGVVESAVIGvphpDFGEG-VTAVVVPKPGA 452
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
105-594 |
2.58e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 101.43 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPAntTNIGIYARNSPQWLVSAVACVEQSMVVV---PLYDTlgAEAAtFIISQAEIS 181
Cdd:PRK08315 44 WTYREFNEEVDALAKGL-LALGIEKG--DRVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL--SELE-YALNQSGCK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 182 -VVIVDSFK----------------KAESLIKNRENMPTLKNIIVIDSA--------DELKDGTAIIDTIRVESLTNALN 236
Cdd:PRK08315 118 aLIAADGFKdsdyvamlyelapelaTCEPGQLQSARLPELRRVIFLGDEkhpgmlnfDELLALGRAVDDAELAARQATLD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 237 lgsrypftnnlpkPDDNYIICYTSGTTGTPKGVMLTHSNIVANisgflkilfafqpsmidatqvhisylplshmmeqlth 316
Cdd:PRK08315 198 -------------PDDPINIQYTSGTTGFPKGATLTHRNILNN------------------------------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 317 wtllgfgskiGYFRGSIQGLTDDIKTLKPtvfpvVPrllnrLYD---------AITSKvqqqGfmAKLVY---NFAFARK 384
Cdd:PRK08315 228 ----------GYFIGEAMKLTEEDRLCIP-----VP-----LYHcfgmvlgnlACVTH----G--ATMVYpgeGFDPLAT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 385 LSLVKAGKV----GRDTIW----DRLVFNKIqqqiggkvDL-------MvTGSA-PIsstvlETCR----------VTLG 438
Cdd:PRK08315 282 LAAVEEERCtalyGVPTMFiaelDHPDFARF--------DLsslrtgiM-AGSPcPI-----EVMKrvidkmhmseVTIA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 439 ttivegYGQTECTALATFTWMGDP-----STghCGAPAPCALVKLGDvPDLNYFAKDGK-GEIRIKGPCVTKGYYKDPER 512
Cdd:PRK08315 348 ------YGMTETSPVSTQTRTDDPlekrvTT--VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEK 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 513 TAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVV 589
Cdd:PRK08315 419 TAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYgeeVCAWII 497
|
....*
gi 17556552 590 PEPDV 594
Cdd:PRK08315 498 LRPGA 502
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
57-575 |
2.80e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 101.21 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 57 MENESEDVLTR------FYPEVATLHDVFVKGKTESNGGPCVGTRSSGDAdyefLTYDDVHEQAKNLSMTLvHEFGLTPA 130
Cdd:PLN02246 1 EASASEEFIFRsklpdiYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRV----YTYADVELLSRRVAAGL-HKLGIRQG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 131 NTtnIGIYARNSPQWLVSAVACVEQSMVVV---PLY------DTLGAEAATFIISQAeisvVIVDSFKKaeslIKNRENM 201
Cdd:PLN02246 76 DV--VMLLLPNCPEFVLAFLGASRRGAVTTtanPFYtpaeiaKQAKASGAKLIITQS----CYVDKLKG----LAEDDGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 202 PtlknIIVIDSADElkdgtaiiDTIRVESLTNALNlgsrypftNNLPK----PDDNYIICYTSGTTGTPKGVMLTHSNIV 277
Cdd:PLN02246 146 T----VVTIDDPPE--------GCLHFSELTQADE--------NELPEveisPDDVVALPYSSGTTGLPKGVMLTHKGLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 278 ANIsgflkilfAFQ-----PSM-IDATQVHISYLPLSHMMeQLTHWTLLGF--GSKIGYFRG-SIQGLTDDIKTLKPTVF 348
Cdd:PLN02246 206 TSV--------AQQvdgenPNLyFHSDDVILCVLPMFHIY-SLNSVLLCGLrvGAAILIMPKfEIGALLELIQRHKVTIA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 349 PVVPRLLnrlydaitskvqqqgfmaklvynfafarkLSLVKAGKVGRDTIwdrlvfnkiqqqigGKVDLMVTGSAPISST 428
Cdd:PLN02246 277 PFVPPIV-----------------------------LAIAKSPVVEKYDL--------------SSIRMVLSGAAPLGKE 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 429 VLETCRVTL-GTTIVEGYGQTE-------CTALATftwmgDP---STGHCGAPAPCALVKLGDvPDLNY-FAKDGKGEIR 496
Cdd:PLN02246 314 LEDAFRAKLpNAVLGQGYGMTEagpvlamCLAFAK-----EPfpvKSGSCGTVVRNAELKIVD-PETGAsLPRNQPGEIC 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17556552 497 IKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVYV 575
Cdd:PLN02246 388 IRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLISHPSIADAAV 465
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
105-583 |
6.58e-22 |
|
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: 99.68 E-value: 6.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVhEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd12118 30 YTWRQTYDRCRRLASALA-ALGISRGDT--VAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSFKKAESLIKNRENMPTLkniivIDSADELkdgtaiiDTIrvesltnALNlgsrypftnnlpkpddnyiicYTSGTTG 264
Cdd:cd12118 107 VDREFEYEDLLAEGDPDFEW-----IPPADEW-------DPI-------ALN---------------------YTSGTTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHS----NIVANIsgflkILFAFQPSmidatQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRG-SIQGLTDD 339
Cdd:cd12118 147 RPKGVVYHHRgaylNALANI-----LEWEMKQH-----PVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKvDAKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 IKTLKPTVFPVVPRLLNRLYDAITSKvqqqgfmaklvynfafARKLSlvkagkvgrdtiwdrlvfnkiqqqigGKVDLMV 419
Cdd:cd12118 217 IEKHKVTHFCGAPTVLNMLANAPPSD----------------ARPLP--------------------------HRVHVMT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 TGSAPiSSTVLEtcRVT-LGTTIVEGYGQTECTALATF-----TWMGDPSTGHCGAPAPCALVKLG----DVPDLNYF-- 487
Cdd:cd12118 255 AGAPP-PAAVLA--KMEeLGFDVTHVYGLTETYGPATVcawkpEWDELPTEERARLKARQGVRYVGleevDVLDPETMkp 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 488 -AKDGK--GEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVY 564
Cdd:cd12118 332 vPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVL 409
|
490
....*....|....*....
gi 17556552 565 IRTPVVQQVYVDGDSLERW 583
Cdd:cd12118 410 YKHPAVLEAAVVARPDEKW 428
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
135-597 |
7.14e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 99.50 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 135 IGIYARNSPQWLVSAVACVEQSMVVVPLydtlgaeaaTFIISQAEISVVIVDSfkkaesliknrenMPTLkniIVIDsaD 214
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPL---------NWRLSASELDALLQDA-------------EPRL---LLGD--D 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 215 ELKDGTAI-IDTIRVESLTNALNLGsrypFTNNLPkPDDNYIICYTSGTTGTPKGVMLTHSNI--VANISGFLKILFAFQ 291
Cdd:PRK09088 103 AVAAGRTDvEDLAAFIASADALEPA----DTPSIP-PERVSLILFTSGTSGQPKGVMLSERNLqqTAHNFGVLGRVDAHS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 292 PSMIDATQVHISYLPLSHMMEQLTHWTLL---GFGSKigyfrGSIQGLTDdiKTLKPTVFPVVPRLLNRLYDaitskvqQ 368
Cdd:PRK09088 178 SFLCDAPMFHIIGLITSVRPVLAVGGSILvsnGFEPK-----RTLGRLGD--PALGITHYFCVPQMAQAFRA-------Q 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 369 QGFMAklvynfAFARKLSLVkagkvgrdtiwdrlvfnkiqqqiggkvdlmVTGSAPISSTVLetcRVTL--GTTIVEGYG 446
Cdd:PRK09088 244 PGFDA------AALRHLTAL------------------------------FTGGAPHAAEDI---LGWLddGIPMVDGFG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 447 QTEctALATFTWMGDPS-----TGHCGAPAPCALVKLGDVPDlNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEG 521
Cdd:PRK09088 285 MSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQG-NDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 522 FLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW-----LIAVVVPEPDVLK 596
Cdd:PRK09088 362 WFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgevgyLAIVPADGAPLDL 440
|
.
gi 17556552 597 E 597
Cdd:PRK09088 441 E 441
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
137-593 |
1.41e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 99.08 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 137 IYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDSfKKAESLIKNRENMPTLKNIIVIDSADEl 216
Cdd:PRK07786 72 ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA-ALAPVATAVRDIVPLLSTVVVAGGSSD- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 217 kDGTAIIDTIRVESltnalnlGSRYPFTNnLPKpDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPSMID 296
Cdd:PRK07786 150 -DSVLGYEDLLAEA-------GPAHAPVD-IPN-DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 297 ATQVhisylPLSHMMeqlthwtllGFGSKIGYFRGSIQGLTDDIKTLKPTvfpvvpRLLNRL-YDAITS----KVQQQGF 371
Cdd:PRK07786 220 FVGV-----PLFHIA---------GIGSMLPGLLLGAPTVIYPLGAFDPG------QLLDVLeAEKVTGiflvPAQWQAV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 372 MAKlvyNFAFARKLSLvkagkvgRDTIWdrlvfnkiqqqiggkvdlmvtGSAPISSTVLETCRVTL-GTTIVEGYGQTEC 450
Cdd:PRK07786 280 CAE---QQARPRDLAL-------RVLSW---------------------GAAPASDTLLRQMAATFpEAQILAAFGQTEM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 451 TALaTFTWMGDPST---GHCGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDeEGFLQTGD 527
Cdd:PRK07786 329 SPV-TCMLLGEDAIrklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGD 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17556552 528 IGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPD 593
Cdd:PRK07786 406 LVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRND 473
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
106-594 |
3.75e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 97.90 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLVhEFGLTPANttnigIYARNSPQW---LVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISV 182
Cdd:PRK06087 51 TYSALDHAASRLANWLL-AKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 VIVDS-FKKA--ESLIKN-RENMPTLKNIIVID------SADELKDgtaIIDtiRVESLTNALNLGSrypftnnlpkpDD 252
Cdd:PRK06087 125 FFAPTlFKQTrpVDLILPlQNQLPQLQQIVGVDklapatSSLSLSQ---IIA--DYEPLTTAITTHG-----------DE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 253 NYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfafqpsmidatqvHISYLPLSHMMEQLTHWTllgfgskiGYFRGS 332
Cdd:PRK06087 189 LAAVLFTSGTEGLPKGVMLTHNNILASERAYCARL-------------NLTWQDVFMMPAPLGHAT--------GFLHGV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 333 IqgltddiktlkptvfpvVPRLLNrlydaiTSKVQQQGFMAKlvynfafaRKLSLVKAGKV-----GRDTIWDRLvfNKI 407
Cdd:PRK06087 248 T-----------------APFLIG------ARSVLLDIFTPD--------ACLALLEQQRCtcmlgATPFIYDLL--NLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 408 QQQiggKVDL-----MVTGSAPISSTVLETCRvTLGTTIVEGYGQTECTALA------TFTWMGDPStghcGAPAPCALV 476
Cdd:PRK06087 295 EKQ---PADLsalrfFLCGGTTIPKKVARECQ-QRGIKLLSVYGSTESSPHAvvnlddPLSRFMHTD----GYAAAGVEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 477 KLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVA 556
Cdd:PRK06087 367 KVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENIS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 17556552 557 PEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDV 594
Cdd:PRK06087 445 SREVEDILLQHPKIHDACVVAMPDERLgerSCAYVVLKAPH 485
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
95-594 |
6.80e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 97.33 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 95 RSSGDADYEFLTYDDVHE---QAKNLsmtlVHEFGLTPanTTNIGIYARNSPQwLVSAVACVEQSMVVVPLYDTLGAEAA 171
Cdd:PRK07529 49 DADPLDRPETWTYAELLAdvtRTANL----LHSLGVGP--GDVVAFLLPNLPE-THFALWGGEAAGIANPINPLLEPEQI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 172 TFIISQAEISVVI-------VDSFKKAESLiknRENMPTLKNIIVIDSADELKD-GTAIIDTIRVESLTNALNLGS---R 240
Cdd:PRK07529 122 AELLRAAGAKVLVtlgpfpgTDIWQKVAEV---LAALPELRTVVEVDLARYLPGpKRLAVPLIRRKAHARILDFDAelaR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 241 YP----FTNNLPKPDDnyIICY--TSGTTGTPKGVMLTHSNIVANisGFLKILFAFqpsmIDATQVHISYLPLSHMMEQL 314
Cdd:PRK07529 199 QPgdrlFSGRPIGPDD--VAAYfhTGGTTGMPKLAQHTHGNEVAN--AWLGALLLG----LGPGDTVFCGLPLFHVNALL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 315 ThwTLLG---------FGSKIGYfRGS--IQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSkvqqqgfmaklvynfafAR 383
Cdd:PRK07529 271 V--TGLAplargahvvLATPQGY-RGPgvIANFWKIVERYRINFLSGVPTVYAALLQVPVD-----------------GH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 384 KLSLVKAGkvgrdtiwdrlvfnkiqqqiggkvdlmVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPS 463
Cdd:PRK07529 331 DISSLRYA---------------------------LCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 464 -TGHCGAPAPCALVKLGDV-PDLNYF---AKDGKGEIRIKGPCVTKGYYkDPERTAELFDEEGFLQTGDIGEMLPNGTIR 538
Cdd:PRK07529 384 rIGSVGLRLPYQRVRVVILdDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFW 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 17556552 539 IIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQqvyvdgdslerwlIAVVVPEPDV 594
Cdd:PRK07529 463 LTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA-------------LAAAVGRPDA 504
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
249-593 |
2.22e-20 |
|
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: 94.92 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 249 KPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKIL-------------FAFQPSMIDatqvhisylplshmmeqlt 315
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALgltsesrvlqfasYTFDVSILE------------------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 316 HWTLLGFGskigyfrGSIqgltddiktlkptvfpVVPR---LLNRLydaitskvqqQGFMAKLVYNFAF-----ARKLSL 387
Cdd:cd05918 165 IFTTLAAG-------GCL----------------CIPSeedRLNDL----------AGFINRLRVTWAFltpsvARLLDP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 388 vkagkvgrdtiwdRLVFNkiqqqiggkVDLMVTGSAPISSTVLET--CRVTLgttiVEGYGQTECTALATFTWMGDPSTG 465
Cdd:cd05918 212 -------------EDVPS---------LRTLVLGGEALTQSDVDTwaDRVRL----INAYGPAECTIAATVSPVVPSTDP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 466 HC-GAPAPCA-----------LVKLGDVpdlnyfakdgkGEIRIKGPCVTKGYYKDPERTAELF-DEEGFLQ-------- 524
Cdd:cd05918 266 RNiGRPLGATcwvvdpdnhdrLVPIGAV-----------GELLIEGPILARGYLNDPEKTAAAFiEDPAWLKqegsgrgr 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 525 ----TGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVyIRT--PVVQQVYVD-----GDSLERWLIAVVVPEPD 593
Cdd:cd05918 335 rlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQRVELGEIEHH-LRQslPGAKEVVVEvvkpkDGSSSPQLVAFVVLDGS 412
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
124-670 |
3.62e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.87 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 124 EFGLTPANTtnIGIYARNSP---QWLVsAVACVeqSMVVVPLYDTLGAEAATFIISQAEISVVIVDSFKK--AESLIKNR 198
Cdd:PLN02860 51 RLGLRNGDV--VAIAALNSDlylEWLL-AVACA--GGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSswYEELQNDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 199 enMPTLKNIIVIDSADELKDGTAI----IDTIRVESLTNA-LNLGSrypftnnlpKPDDNYIICYTSGTTGTPKGVMLTH 273
Cdd:PLN02860 126 --LPSLMWQVFLESPSSSVFIFLNsfltTEMLKQRALGTTeLDYAW---------APDDAVLICFTSGTTGRPKGVTISH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 274 SNIVanISGFLKILFAFQPSmiDATQVHISylPLSH----------MMEQLTHWTLLGFGSKIGYfrgsiqgltDDIKTL 343
Cdd:PLN02860 195 SALI--VQSLAKIAIVGYGE--DDVYLHTA--PLCHigglssalamLMVGACHVLLPKFDAKAAL---------QAIKQH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 344 KPTVFPVVPRLlnrlydaitskvqqqgfMAKLVynfAFARKlslvkagkvgrdtiwdrlvfnKIQQQIGGKVDLMVTGSA 423
Cdd:PLN02860 260 NVTSMITVPAM-----------------MADLI---SLTRK---------------------SMTWKVFPSVRKILNGGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 424 PISSTVLETCRVTL-GTTIVEGYGQTE-CTALaTFTWMGDPST----------------------GHC-GAPAPCALVKL 478
Cdd:PLN02860 299 SLSSRLLPDAKKLFpNAKLFSAYGMTEaCSSL-TFMTLHDPTLespkqtlqtvnqtksssvhqpqGVCvGKPAPHVELKI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 479 G-DVPDlnyfaKDGKgeIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKlAQGEYVAP 557
Cdd:PLN02860 378 GlDESS-----RVGR--ILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 558 EKIEQVYIRTPVVQQVYVDG--DS-LERWLIAVVvpepdVLKE---WNDKQGSGSRkieeicndekaKEFVLSE--LHAI 629
Cdd:PLN02860 450 EEVEAVLSQHPGVASVVVVGvpDSrLTEMVVACV-----RLRDgwiWSDNEKENAK-----------KNLTLSSetLRHH 513
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 17556552 630 GKANKLNSIEQVKKVILTSDTFTvenglLTPTLKAKRPQLR 670
Cdd:PLN02860 514 CREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
105-583 |
5.89e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 93.49 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHeFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAA-LGVKKGDR--VALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDsfkkaesliknrenmptlkniividsaDELKDGTAIIDTIRVESL----TNALNLGSRYPFtnnlpkpDDNYIICYTS 260
Cdd:PRK03640 105 TD---------------------------DDFEAKLIPGISVKFAELmngpKEEAEIQEEFDL-------DEVATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 261 GTTGTPKGVMLTHSNIVAN-ISGFLKILFAFQPSMIDATQV-HISylPLSHMMEQLThwtllgFGSKIG-YFRGSIQGLT 337
Cdd:PRK03640 151 GTTGKPKGVIQTYGNHWWSaVGSALNLGLTEDDCWLAAVPIfHIS--GLSILMRSVI------YGMRVVlVEKFDAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 DDIKTLKPTVFPVVPRLLNRLydaiTSKVQQQGfmaklvYNfafarklslvkagkvgrdtiwdrlvfnkiqqqigGKVDL 417
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRL----LERLGEGT------YP----------------------------------SSFRC 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 418 MVTGSAPISSTVLETCRVTlGTTIVEGYGQTE-CTALATFtwmgDPS-----TGHCGAPAPCALVKLGDvpDLNYFAKDG 491
Cdd:PRK03640 259 MLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTEtASQIVTL----SPEdaltkLGSAGKPLFPCELKIEK--DGVVVPPFE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 492 KGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQ 571
Cdd:PRK03640 332 EGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVA 409
|
490
....*....|..
gi 17556552 572 QVYVDGDSLERW 583
Cdd:PRK03640 410 EAGVVGVPDDKW 421
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
141-593 |
6.40e-20 |
|
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: 92.79 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 141 NSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDSfkkaesliknrenmptlkniividsadelkdgt 220
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 221 aiidtirvesltnalnlgsrypftnnlpkpDDNYIICYTSGTTGTPKGVMLTHSnivanisgflkILFAFQPSMIDATQV 300
Cdd:cd05972 81 ------------------------------EDPALIYFTSGTTGLPKGVLHTHS-----------YPLGHIPTAAYWLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 301 HISYLplshmmeqltHWTLlgfgSKIGYFRGsiqgltddikTLKPTVFPV---VPRLLNRLydaitskvqqQGFMAKLVY 377
Cdd:cd05972 120 RPDDI----------HWNI----ADPGWAKG----------AWSSFFGPWllgATVFVYEG----------PRFDAERIL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 378 nfafaRKLSLVKAGKV-GRDTIWDRLVFNKIQQQIGGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTA-LAT 455
Cdd:cd05972 166 -----ELLERYGVTSFcGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLtVGN 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 456 FTWMgDPSTGHCGAPAPCALVKLGD------VPdlnyfAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIG 529
Cdd:cd05972 241 FPDM-PVKPGSMGRPTPGYDVAIIDddgrelPP-----GEEGDIAIKLPPPGLFLGYVGDPEKTEASI-RGDYYLTGDRA 313
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17556552 530 EMLPNGTIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTPVVQQvyvdgdslerwliAVVVPEPD 593
Cdd:cd05972 314 YRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAE-------------AAVVGSPD 363
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
105-594 |
8.07e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 93.41 E-value: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVP------------LYDTLGAEAat 172
Cdd:PRK07798 29 LTYAELEERANRLAHYL-IAQGLGPGD--HVGIYARNRIEYVEAMLGAFKARAVPVNvnyryvedelryLLDDSDAVA-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 173 fIISQAEISVVIVDSfkkaesliknRENMPTLKNIIVID--SADELKDGtaiidtirVESLTNALNLGS-RYPFTNnlPK 249
Cdd:PRK07798 104 -LVYEREFAPRVAEV----------LPRLPKLRTLVVVEdgSGNDLLPG--------AVDYEDALAAGSpERDFGE--RS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIIcYTSGTTGTPKGVMLTHSNIVAniSGFLKILFAFQPSMID----ATQVH----ISYLPLSHMMEQLTHWTLLG 321
Cdd:PRK07798 163 PDDLYLL-YTGGTTGMPKGVMWRQEDIFR--VLLGGRDFATGEPIEDeeelAKRAAagpgMRRFPAPPLMHGAGQWAAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 322 fgskiGYFRGSiqgltddiktlkPTVFPVVPRLlnrlyDA--ITSKVQQQGFMAKLVYNFAFARklSLVKAGKVGRDTIW 399
Cdd:PRK07798 240 -----ALFSGQ------------TVVLLPDVRF-----DAdeVWRTIEREKVNVITIVGDAMAR--PLLDALEARGPYDL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 400 DRLVfnkiqqqiggkvdLMVTGSAPISSTVLET-CRVTLGTTIVEGYGQTECTALATFtwMGDPSTGHCGAP--APCALV 476
Cdd:PRK07798 296 SSLF-------------AIASGGALFSPSVKEAlLELLPNVVLTDSIGSSETGFGGSG--TVAKGAVHTGGPrfTIGPRT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 477 KLGDvPDLNyFAKDGKGEI-RI-KGPCVTKGYYKDPERTAELF---DEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAq 551
Cdd:PRK07798 361 VVLD-EDGN-PVEPGSGEIgWIaRRGHIPLGYYKDPEKTAETFptiDGVRYAIPGDRARVEADGTITLLGRGSVCINTG- 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 17556552 552 GEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDV 594
Cdd:PRK07798 438 GEKVFPEEVEEALKAHPDVADALVVGVPDERWgqeVVAVVQLREGA 483
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
158-562 |
8.66e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 94.61 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 158 VVVPLYDTLGAEAATFIISQAEISVVIVdSFKKAESLiKNRENMPTLKNIIVIDSADELKDGTAIIDTIRveSLTNALNL 237
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVIT-SRKFLEKL-KNKGFDLELPENVKVIYLEDLKAKISKVDKLT--ALLAARLL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 238 GSRY--PFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfafqpsMIDATQVHISYLPLSHMMeqlt 315
Cdd:PRK08633 767 PARLlkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVF------NLRNDDVILSSLPFFHSF---- 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 316 hwtllgfgskigyfrgsiqGLTddIKTLKPTV--FPVV--PRLLnrlyDAITskvqqqgfMAKLV--YN----FAFARKL 385
Cdd:PRK08633 837 -------------------GLT--VTLWLPLLegIKVVyhPDPT----DALG--------IAKLVakHRatilLGTPTFL 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 386 SL-VKAGKVgrdtiwDRLVFNKIqqqiggkvDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALAT--------- 455
Cdd:PRK08633 884 RLyLRNKKL------HPLMFASL--------RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASvnlpdvlaa 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 456 -FTWMGDPSTGHCGAPAPCALVKlgdVPDLNYFAKDGKGE---IRIKGPCVTKGYYKDPERTAEL---FDEEGFLQTGDI 528
Cdd:PRK08633 950 dFKRQTGSKEGSVGMPLPGVAVR---IVDPETFEELPPGEdglILIGGPQVMKGYLGDPEKTAEVikdIDGIGWYVTGDK 1026
|
410 420 430
....*....|....*....|....*....|....
gi 17556552 529 GEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQ 562
Cdd:PRK08633 1027 GHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVEE 1059
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
103-592 |
1.25e-19 |
|
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: 92.31 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 103 EFLTYDDVHEQAKNLSMTLVHefgLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISV 182
Cdd:cd05945 15 RTLTYRELKERADALAAALAS---LGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 VIVDsfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpkPDDNYIICYTSGT 262
Cdd:cd05945 92 LIAD---------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 263 TGTPKGVMLTHSNIVANISGFLKiLFAFQPSmidatQVHISYLPLS---HMMEQLTHWTLLGfgskigyfrgsiqgltdd 339
Cdd:cd05945 109 TGRPKGVQISHDNLVSFTNWMLS-DFPLGPG-----DVFLNQAPFSfdlSVMDLYPALASGA------------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 ikTLKPtvfpvVPRllnrlydaitskvQQQGFMAKLvynFAFARKLSLvkAGKVGRDTIWDrlvfnkiqqqiggkvdlMV 419
Cdd:cd05945 165 --TLVP-----VPR-------------DATADPKQL---FRFLAEHGI--TVWVSTPSFAA-----------------MC 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 TGSAPISSTVLETCRVTL-------------------GTTIVEGYGQTECTALATFT-WMGDPSTGHcgAPAPCALVKlg 479
Cdd:cd05945 203 LLSPTFTPESLPSLRHFLfcgevlphktaralqqrfpDARIYNTYGPTEATVAVTYIeVTPEVLDGY--DRLPIGYAK-- 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 480 dvPDLNYFAKDG---------KGEIRIKGPCVTKGYYKDPERTAE-LFDEEGFL--QTGDIGEMLPNGTIRIIDRKKHIF 547
Cdd:cd05945 279 --PGAKLVILDEdgrpvppgeKGELVISGPSVSKGYLNNPEKTAAaFFPDEGQRayRTGDLVRLEADGLLFYRGRLDFQV 356
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 17556552 548 KLaQGEYVAPEKIEQVYIRTPVVQQVYV----DGDSLERwLIAVVVPEP 592
Cdd:cd05945 357 KL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKP 403
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
94-544 |
2.34e-19 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 91.96 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 94 TRSSGDADYEFLTYDDVHEQAKNLSmTLVHEFGLTPANTTnigIYARNSPQWLVSAV-ACVEQSMVVVPL-----YDTLG 167
Cdd:cd05906 29 TYIDADGSEEFQSYQDLLEDARRLA-AGLRQLGLRPGDSV---ILQFDDNEDFIPAFwACVLAGFVPAPLtvpptYDEPN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 168 AEAATF--IISQAEISVVIVDS-----FKKAESLIKNREnmptlkniIVIDSADELKDgtaiidtirVESLTNALNlgsr 240
Cdd:cd05906 105 ARLRKLrhIWQLLGSPVVLTDAelvaeFAGLETLSGLPG--------IRVLSIEELLD---------TAADHDLPQ---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 241 ypftnnlPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGflkilfAFQPSMIDATQVHISYLPLSHMMeQLTHWTLL 320
Cdd:cd05906 164 -------SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG------KIQHNGLTPQDVFLNWVPLDHVG-GLVELHLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 321 GFgskigyFRGS--IQGLTDDIkTLKPTVFPvvpRLLNRLYDAITskvqqqgFMAklvyNFAFARKLSLVKAGKVGRdti 398
Cdd:cd05906 230 AV------YLGCqqVHVPTEEI-LADPLRWL---DLIDRYRVTIT-------WAP----NFAFALLNDLLEEIEDGT--- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 399 WD----RLVFNkiqqqiGGKvdlmvtgsapisSTVLETCRVTLG---------TTIVEGYGQTECTALATFTwMGDPSTG 465
Cdd:cd05906 286 WDlsslRYLVN------AGE------------AVVAKTIRRLLRllepyglppDAIRPAFGMTETCSGVIYS-RSFPTYD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 466 H--------CGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGeMLPNGTI 537
Cdd:cd05906 347 HsqalefvsLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNL 424
|
....*..
gi 17556552 538 RIIDRKK 544
Cdd:cd05906 425 TITGRTK 431
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
444-594 |
2.16e-18 |
|
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: 86.97 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 444 GYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFL 523
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWH 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17556552 524 QTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDV 594
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVIGVPDPRWaqsVKAIVVLKPGA 292
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
252-592 |
2.78e-18 |
|
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: 86.55 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 252 DNYIICYTSGTTGTPKGVMLTHSNIV-ANISgflkilfaFQPSM-IDATQVHISYLPLSHMMeqlthwtllGFGSkigyf 329
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANLQ--------LIHAMgLTEADVYLNMLPLFHIA---------GLNL----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 330 rgsiqGLTddiktlkptvfpvvprllnrlydaitskVQQQGFMAKLVYNFAFARKLSLVKAGKVgrdTIWDR---LVFNK 406
Cdd:cd17637 59 -----ALA----------------------------TFHAGGANVVMEKFDPAEALELIEEEKV---TLMGSfppILSNL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 IQQQIGGKVDL----MVTG-SAPissTVLETCRVTLGTTIVEGYGQTECTALATFTwmgdPST---GHCGAPAPCALVKL 478
Cdd:cd17637 103 LDAAEKSGVDLsslrHVLGlDAP---ETIQRFEETTGATFWSLYGQTETSGLVTLS----PYRerpGSAGRPGPLVRVRI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 479 GDvpDLNYFAKDGK-GEIRIKGPCVTKGYYKDPERTAELFDeEGFLQTGDIGEMLPNGTIRIIDRK--KHIFKlAQGEYV 555
Cdd:cd17637 176 VD--DNDRPVPAGEtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENV 251
|
330 340 350
....*....|....*....|....*....|....*..
gi 17556552 556 APEKIEQVYIRTPVVQQVYVDGdslerwliavvVPEP 592
Cdd:cd17637 252 YPAEVEKVILEHPAIAEVCVIG-----------VPDP 277
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
252-572 |
3.03e-18 |
|
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: 86.55 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 252 DNYIICYTSGTTGTPKGVMLTHSNIVANisgfLKILFAFQPSmIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRG 331
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAV----PDILQKEGLN-WVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 332 SIQ--GLTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQqqgfmaklvynfaFARKLSLVKAGkvgrdtiwdrlvfnkiqq 409
Cdd:cd17635 77 NTTykSLFKILTTNAVTTTCLVPTLLSKLVSELKSANA-------------TVPSLRLIGYG------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 410 qiggkvdlmvtGSAPISSTVlETCRVTLGTTIVEGYGQTECTAlATFTWMGDPST--GHCGAPAPCALVKLGDVpDLNYF 487
Cdd:cd17635 126 -----------GSRAIAADV-RFIEATGLTNTAQVYGLSETGT-ALCLPTDDDSIeiNAVGRPYPGVDVYLAAT-DGIAG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 488 AKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRT 567
Cdd:cd17635 192 PSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEGV 269
|
....*
gi 17556552 568 PVVQQ 572
Cdd:cd17635 270 SGVQE 274
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
250-565 |
3.04e-18 |
|
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: 88.31 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILfafqpsMIDATQVHISYLPLSHMMeqlthwtllgfgskigyf 329
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST------EWKTKDRILSWMPLTHDM------------------ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 330 rGSIQG-LTDDIKTLKPTVFPV---VPRLLNRLYDAITSKVQQQGfmaklVYNFAFARKLSLVKAGKVGRdtiWDRLVFN 405
Cdd:cd05908 161 -GLIAFhLAPLIAGMNQYLMPTrlfIRRPILWLKKASEHKATIVS-----SPNFGYKYFLKTLKPEKAND---WDLSSIR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 406 KIqqqiggkvdlmVTGSAPISStvlETCRVTLG---------TTIVEGYGQTECTALATFTWMGDPST----GH----CG 468
Cdd:cd05908 232 MI-----------LNGAEPIDY---ELCHEFLDhmskyglkrNAILPVYGLAEASVGASLPKAQSPFKtitlGRrhvtHG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 469 APAP--------CA-LVKLGD---------VPDLNYFAKDGK-GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIG 529
Cdd:cd05908 298 EPEPevdkkdseCLtFVEVGKpidetdiriCDEDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG 377
|
330 340 350
....*....|....*....|....*....|....*.
gi 17556552 530 EMLpNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYI 565
Cdd:cd05908 378 FIR-NGRLVITGREKDII-FVNGQNVYPHDIERIAE 411
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
98-599 |
1.32e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 86.76 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 98 GDADYEFLTYDDVHEQAKNLSMTLVHEFGLTPANTTNIGIYARNSPQWLVSAVACVeqSMVVVPLYDTLGAEAATFIISQ 177
Cdd:PRK05620 32 GGAEQEQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACM--GAVFNPLNKQLMNDQIVHIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 178 AEISVVIVDSfKKAESLIKNRENMPTLKNIIVIDSADELKDGTAIIDTIRVESLTNALNLGSR-YPFtnnlPKPDDN--Y 254
Cdd:PRK05620 110 AEDEVIVADP-RLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTvYDW----PELDETtaA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 255 IICYTSGTTGTPKGVMLTHSNIvanisgflkILFAFQPSMIDATQVH--ISYL---PLSHmmeqlthwtLLGFGSKIGYF 329
Cdd:PRK05620 185 AICYSTGTTGAPKGVVYSHRSL---------YLQSLSLRTTDSLAVThgESFLccvPIYH---------VLSWGVPLAAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 330 RGSiqgltddiktlKPTVFP---VVPRLLNRLYDAITSKVQQqgfmaklvynfafarklslvkagkvGRDTIWDRLVFNK 406
Cdd:PRK05620 247 MSG-----------TPLVFPgpdLSAPTLAKIIATAMPRVAH-------------------------GVPTLWIQLMVHY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 IQ--------QQIggkvdlmVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATftwMGDPSTGHCGAPAPCALVKL 478
Cdd:PRK05620 291 LKnppermslQEI-------YVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGT---VARPPSGVSGEARWAYRVSQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 479 GDVP-DLNY-FAKDGK---------GEIRIKGPCVTKGYYKDP----------------ERTAELFDEEGFLQTGDIGEM 531
Cdd:PRK05620 361 GRFPaSLEYrIVNDGQvmestdrneGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSV 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17556552 532 LPNGTIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERWL---IAVVVPEPDVlkEWN 599
Cdd:PRK05620 441 TRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGerpLAVTVLAPGI--EPT 508
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
250-589 |
1.40e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 86.59 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANISGflkilfafqpsMIDATQ------VHISYLPLSHMMeqlthwTLLGFG 323
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNLYANAEA-----------MFVAAEfdvetdVMVSWLPLFHDM------GMVGFL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 324 SkIGYFRGSiqgltdDIKTLKPTVF---PVV-PRLLNRLYDAITSKVqqqgfmaklvyNFAFARklslvkagkVGRdtiw 399
Cdd:PRK07768 214 T-VPMYFGA------ELVKVTPMDFlrdPLLwAELISKYRGTMTAAP-----------NFAYAL---------LAR---- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 400 dRLVfnkiQQQIGGKVDL-----MVTGSAPISSTVLET-----CRVTLG-TTIVEGYGQTECTALATFtwmGDPSTG--- 465
Cdd:PRK07768 263 -RLR----RQAKPGAFDLsslrfALNGAEPIDPADVEDlldagARFGLRpEAILPAYGMAEATLAVSF---SPCGAGlvv 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 466 -----------HCGAPAPC----ALVKLGD-VPDLN--YFAKDGK-------GEIRIKGPCVTKGyYKDPERTAELFDEE 520
Cdd:PRK07768 335 devdadllaalRRAVPATKgntrRLATLGPpLPGLEvrVVDEDGQvlpprgvGVIELRGESVTPG-YLTMDGFIPAQDAD 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17556552 521 GFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQ-----VYVD-GDSLERwlIAVVV 589
Cdd:PRK07768 414 GWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIERAAARVEGVRPgnavaVRLDaGHSREG--FAVAV 485
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
105-593 |
1.46e-17 |
|
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: 87.60 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPAntTNIGIYARNSPQWLVSAVAcveqsmVV------VPLYDTLGAEAATFIISQA 178
Cdd:COG1020 502 LTYAELNARANRLAHHL-RALGVGPG--DLVGVCLERSLEMVVALLA------VLkagaayVPLDPAYPAERLAYMLEDA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 179 EISVVIVDSfkkaesliknrenmptlkniiviDSADELKDGTAiiDTIRVESLTNAlnlgsRYPFTNNLPKPD-DN--YI 255
Cdd:COG1020 573 GARLVLTQS-----------------------ALAARLPELGV--PVLALDALALA-----AEPATNPPVPVTpDDlaYV 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 256 IcYTSGTTGTPKGVMLTHSNIVANISGFLKiLFAFQPSmiD-ATQVH-----IS----YLPLS-----HMMEQLTHWtll 320
Cdd:COG1020 623 I-YTSGSTGRPKGVMVEHRALVNLLAWMQR-RYGLGPG--DrVLQFAslsfdASvweiFGALLsgatlVLAPPEARR--- 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 321 gfgskigyfrgSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAitskvqqqgfmaklvynfAFARKLSLvkagkvgrdtiwd 400
Cdd:COG1020 696 -----------DPAALAELLARHRVTVLNLTPSLLRALLDA------------------APEALPSL------------- 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 401 RLVFnkiqqqIGGkvdlmvtgsapisstvlETCRVTL---------GTTIVEGYGQTECTALATFTWMGDPSTGhcGAPA 471
Cdd:COG1020 734 RLVL------VGG-----------------EALPPELvrrwrarlpGARLVNLYGPTETTVDSTYYEVTPPDAD--GGSV 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 472 P--------CALV---KLGDVPDlnyfakdG-KGEIRIKGPCVTKGYYKDPERTAELF--DEEGFLQ-----TGDIGEML 532
Cdd:COG1020 789 PigrpiantRVYVldaHLQPVPV-------GvPGELYIGGAGLARGYLNRPELTAERFvaDPFGFPGarlyrTGDLARWL 861
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17556552 533 PNGTIRIIDRKKHifklaQ----------GEyvapekIEQVYIRTPVVQQVYV---DGDSLERWLIAVVVPEPD 593
Cdd:COG1020 862 PDGNLEFLGRADD-----QvkirgfrielGE------IEAALLQHPGVREAVVvarEDAPGDKRLVAYVVPEAG 924
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
158-592 |
2.27e-17 |
|
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: 85.62 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 158 VVVPLYDTLGAEAATFIISQAEISVVIVDSFKKAESLIKN-RENMPTLKNIIVIdsADELKDGTaiidtIRVESLTNALN 236
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKaAPECPSKPKLVWV--GDPVPEGW-----IDFRKLIKNAS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 237 LGSRYPFTNNLPKPDDNYIICYTSGTTGTPKgvMLTHSNivanisgflkilfafqpsmidatqvhiSYlPLSHMM----- 311
Cdd:cd05970 171 PDFERPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDF---------------------------TY-PLGHIVtakyw 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 312 ----EQLTHWTL--LGFGSKIGyfrGSIQGltddiktlkptvfpvvprllnrlydaitskvQQQGFMAKLVYNFA-FARK 384
Cdd:cd05970 221 qnvrEGGLHLTVadTGWGKAVW---GKIYG-------------------------------QWIAGAAVFVYDYDkFDPK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 385 LSLVKAGKVG------RDTIWDRLVFNKIQQQIGGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECT-ALATFT 457
Cdd:cd05970 267 ALLEKLSKYGvttfcaPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTlTIATFP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 458 WMgDPSTGHCGAPAPCALVKLGDvPDLNYFAKDGKGEIRI---KGPCVT--KGYYKDPERTAELFdEEGFLQTGDIGEML 532
Cdd:cd05970 347 WM-EPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIrtsKGKPVGlfGGYYKDAEKTAEVW-HDGYYHTGDAAWMD 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 533 PNGTIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTPVVQQVYVDGdslerwliavvVPEP 592
Cdd:cd05970 424 EDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
135-592 |
3.79e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 84.94 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 135 IGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDSFKKAesliknreNMPTLKNIIVIDSAd 214
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDA--------IVALETPKIVIDAA- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 215 elkdgtAIIDTIRVESltNALNLGSRYPftnnlPKPDDNYIICYTSGTTGTPKGVMLTHSNIvanisgflkilfafqpsm 294
Cdd:PRK06145 126 ------AQADSRRLAQ--GGLEIPPQAA-----VAPTDLVRLMYTSGTTDRPKGVMHSYGNL------------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 295 idatqvhisylplshmmeqltHWTllGFGSKIGYfrgsiqGLTDDIKTLkptvfpVVPRLLN-RLYDAITSKVQQQGFMA 373
Cdd:PRK06145 175 ---------------------HWK--SIDHVIAL------GLTASERLL------VVGPLYHvGAFDLPGIAVLWVGGTL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 374 KLVYNF-------AFARK------LSLVKAGKVGRDTIWDRLVFNKIQQQIGGkvdlmvtGSAPISSTVLETCRVTLGTT 440
Cdd:PRK06145 220 RIHREFdpeavlaAIERHrltcawMAPVMLSRVLTVPDRDRFDLDSLAWCIGG-------GEKTPESRIRDFTRVFTRAR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 441 IVEGYGQTECTALATFTWMGDP--STGHCGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFd 518
Cdd:PRK06145 293 YIDAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF- 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556552 519 EEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEP 592
Cdd:PRK06145 371 YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWgerITAVVVLNP 446
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
105-594 |
4.16e-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: 84.56 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEfGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd12117 23 LTYAELNERANRLARRLRAA-GVGPGDV--VGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfkkaesliknrenmptlkniiviDSADELKDGTAIIDTIRVESLTNALNLGSRypftnnlPKPDD-NYIIcYTSGTT 263
Cdd:cd12117 100 TDR-----------------------SLAGRAGGLEVAVVIDEALDAGPAGNPAVP-------VSPDDlAYVM-YTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNIVAnisgflkilFAFQPSMIDATQvhisylplshmmeqltHWTLLGFGSkigyfrgsiqgLTDDIKTL 343
Cdd:cd12117 149 GRPKGVAVTHRGVVR---------LVKNTNYVTLGP----------------DDRVLQTSP-----------LAFDASTF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 344 KptVFpvVPrLLN--RLYDAITSKVQQQGFMAKLVynfafarklslvKAGKVgrDTIWdrL---VFNKIQQQI----GGK 414
Cdd:cd12117 193 E--IW--GA-LLNgaRLVLAPKGTLLDPDALGALI------------AEEGV--TVLW--LtaaLFNQLADEDpecfAGL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 415 VDLMVTG---SAPISSTVLETCRvtlGTTIVEGYGQTECTALATFTWM--GDPSTGHC--GAPAPCALVKLGDvpdlnyf 487
Cdd:cd12117 252 RELLTGGevvSPPHVRRVLAACP---GLRLVNGYGPTENTTFTTSHVVteLDEVAGSIpiGRPIANTRVYVLD------- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 488 aKDGK-------GEIRIKGPCVTKGYYKDPERTAELFDEEGFL------QTGDIGEMLPNGTIRIIDRKKHIFKLaQGEY 554
Cdd:cd12117 322 -EDGRpvppgvpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFR 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYV---DGDSLERWLIAVVVPEPDV 594
Cdd:cd12117 400 IELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
250-570 |
4.86e-17 |
|
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: 83.30 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANiSGFLKILFAFQPsmidaTQVHISYLPLSHMMEQLThwTLLG-------- 321
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLFDP-----DDVLLCGLPLFHVNGSVV--TLLTplasgahv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 322 -FGSKIGYfRGsiQGLTDDIKTL----KPTVFPVVPRLLnrlydAITSKVqqqgfmaklvynfafarklslvkagKVGRD 396
Cdd:cd05944 73 vLAGPAGY-RN--PGLFDNFWKLveryRITSLSTVPTVY-----AALLQV-------------------------PVNAD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 397 TiwdrlvfnkiqqqigGKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPS-TGHCGAPAPCAL 475
Cdd:cd05944 120 I---------------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPDGPKrPGSVGLRLPYAR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 476 VKL----GDVPDLNYFAKDGKGEIRIKGPCVTKGYYKDpERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQ 551
Cdd:cd05944 185 VRIkvldGVGRLLRDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRG 262
|
330
....*....|....*....
gi 17556552 552 GEYVAPEKIEQVYIRTPVV 570
Cdd:cd05944 263 GHNIDPALIEEALLRHPAV 281
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
248-588 |
5.28e-17 |
|
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: 83.20 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKPDDNYIIcYTSGTTGTPKGVMLTHSNI---VANISGFLKILFAFQPSMIDATQ-----VHISYLPLSHMMEQLTHWTL 319
Cdd:cd05924 1 RSADDLYIL-YTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPSEDAHKAAAaaagtVMFPAPPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 320 LGFGSKIgyfrgsiqgltddiktlkptvfpVVPRLlnRLY-DAITSKVQQQGFMAKLVYNFAFARklSLVKAGKVGRDTI 398
Cdd:cd05924 80 LLGGQTV-----------------------VLPDD--RFDpEEVWRTIEKHKVTSMTIVGDAMAR--PLIDALRDAGPYD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 399 WDRLVfnkiqqqiggkvdLMVTGSAPISSTVLET-CRVTLGTTIVEGYGQTECTALAT-FTWMGDPSTGHCGAPAPCALV 476
Cdd:cd05924 133 LSSLF-------------AISSGGALLSPEVKQGlLELVPNITLVDAFGSSETGFTGSgHSAGSGPETGPFTRANPDTVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 477 KlgdVPDLNYFAK--DGKGEIRIKGpCVTKGYYKDPERTAELFDEEG---FLQTGDIGEMLPNGTIRIIDRKKHIFKLAq 551
Cdd:cd05924 200 L---DDDGRVVPPgsGGVGWIARRG-HIPLGYYGDEAKTAETFPEVDgvrYAVPGDRATVEADGTVTLLGRGSVCINTG- 274
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17556552 552 GEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVV 588
Cdd:cd05924 275 GEKVFPEEVEEALKSHPAVYDVLVVGRPDERWgqeVVAVV 314
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
105-602 |
7.25e-17 |
|
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: 83.92 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd17655 23 LTYRELNERANQLARTL-REKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfkkaesliknrenmPTLKNIIVIDSADELKDgtaiiDTIRVESLTNalnlgsrypfTNNLPKPDD-NYIIcYTSGTT 263
Cdd:cd17655 100 TQS--------------HLQPPIAFIGLIDLLDE-----DTIYHEESEN----------LEPVSKSDDlAYVI-YTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNIVANISGFLKilfafqpSMIDATQVHIS-YLPLSHMMEQLTHWTLLGFGSKIGYFR----GSIQGLTD 338
Cdd:cd17655 150 GKPKGVMIEHRGVVNLVEWANK-------VIYQGEHLRVAlFASISFDASVTEIFASLLSGNTLYIVRketvLDGQALTQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 339 DIKTLKPTVFPVVPRLLNRLydaitskvqqqgfmaklvynfafarklslvkagkvgrdtiwdrlvfNKIQQQIGGKVDLM 418
Cdd:cd17655 223 YIRQNRITIIDLTPAHLKLL----------------------------------------------DAADDSEGLSLKHL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 419 VTGSAPISSTVLE--TCRVTLGTTIVEGYGQTECTALATfTWMGDPSTG-----HCGAPAPCALVKLGDvpdlnyfaKDG 491
Cdd:cd17655 257 IVGGEALSTELAKkiIELFGTNPTITNAYGPTETTVDAS-IYQYEPETDqqvsvPIGKPLGNTRIYILD--------QYG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 492 K-------GEIRIKGPCVTKGYYKDPERTAELFDEEGFL------QTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPE 558
Cdd:cd17655 328 RpqpvgvaGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELG 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 17556552 559 KIEQVYIRTPVVQQVYV---DGDSLERWLIAVVVPEPDV----LKEWNDKQ 602
Cdd:cd17655 407 EIEARLLQHPDIKEAVViarKDEQGQNYLCAYIVSEKELpvaqLREFLARE 457
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
135-575 |
1.67e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.14 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 135 IGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDsfkkaesliknRENMPTLKNIIVIDSAD 214
Cdd:PLN03102 67 VSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD-----------RSFEPLAREVLHLLSSE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 215 ELKDGTAIIDTIRVESLTNALNLGSRYP--FTNNLPKPD------------DNYIICYTSGTTGTPKGVMLTHSnivani 280
Cdd:PLN03102 136 DSNLNLPVIFIHEIDFPKRPSSEELDYEclIQRGEPTPSlvarmfriqdehDPISLNYTSGTTADPKGVVISHR------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 281 SGFLKILFAFQPSMIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFRG-SIQGLTDDIKTLKPTVFPVVPRllnrly 359
Cdd:PLN03102 210 GAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHvTAPEIYKNIEMHNVTHMCCVPT------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 360 daitskvqqqgfmaklVYNFafarklsLVKAGKVGrdtiwdrlvfnkiQQQIGGKVDLMVTGSAPISSTVLETCRvtLGT 439
Cdd:PLN03102 284 ----------------VFNI-------LLKGNSLD-------------LSPRSGPVHVLTGGSPPPAALVKKVQR--LGF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 440 TIVEGYGQTECTALATFT-----WMGDPSTGHCGAPAPCALVKLG----DVPD---LNYFAKDGK--GEIRIKGPCVTKG 505
Cdd:PLN03102 326 QVMHAYGLTEATGPVLFCewqdeWNRLPENQQMELKARQGVSILGladvDVKNketQESVPRDGKtmGEIVIKGSSIMKG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 506 YYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYV 575
Cdd:PLN03102 406 YLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYPKVLETAV 473
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
93-596 |
2.65e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.58 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 93 GTRSS---GDADYeflTYDDVHEQAKNLSMTLVHEfGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAE 169
Cdd:PLN02479 34 PTRKSvvhGSVRY---TWAQTYQRCRRLASALAKR-SIGPGST--VAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 170 AATFIISQAEISVVIVD---------SFKKAESLIKNRENMPTLkniIVIdsADELKDGTAIIDTIRVESLTNALNLGSR 240
Cdd:PLN02479 108 TIAFLLEHSKSEVVMVDqefftlaeeALKILAEKKKSSFKPPLL---IVI--GDPTCDPKSLQYALGKGAIEYEKFLETG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 241 YPFTNNLPKPD--DNYIICYTSGTTGTPKGVMLTHSNivanisgflKILFAFQPSMI---DATQVHISYLPLSHMMEQLT 315
Cdd:PLN02479 183 DPEFAWKPPADewQSIALGYTSGTTASPKGVVLHHRG---------AYLMALSNALIwgmNEGAVYLWTLPMFHCNGWCF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 316 HWTLLGF-GSKIGYFRGSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSkvqqqgfmaklvynfafarklslvkagkvg 394
Cdd:PLN02479 254 TWTLAALcGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKS------------------------------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 395 rDTIwdrLVFNKIqqqiggkVDLMVTGSAPISSTVLETC----RVTLGTTIVEGYGQTECTALATfTWMGDPSTGHCGAP 470
Cdd:PLN02479 304 -ETI---LPLPRV-------VHVMTAGAAPPPSVLFAMSekgfRVTHTYGLSETYGPSTVCAWKP-EWDSLPPEEQARLN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 471 APCALVKLG----DVPDLNYFA---KDGK--GEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIID 541
Cdd:PLN02479 372 ARQGVRYIGleglDVVDTKTMKpvpADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKD 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 17556552 542 RKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDVLK 596
Cdd:PLN02479 451 RSKDII-ISGGENISSLEVENVVYTHPAVLEASVVARPDERWgesPCAFVTLKPGVDK 507
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
248-598 |
3.78e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 82.01 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFAfqpsmIDATQVHISYLPLshmmeqltHWtllgfgskig 327
Cdd:PRK06178 206 PALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVV-----GGEDSVFLSFLPE--------FW---------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 328 yfrgsIQGltDDIKTLKPTVF--PVVprLLNRlYDAitskvqqQGFMAkLVYNFAFARKLSLVKagkvGRDTIWDRLVFn 405
Cdd:PRK06178 263 -----IAG--ENFGLLFPLFSgaTLV--LLAR-WDA-------VAFMA-AVERYRVTRTVMLVD----NAVELMDHPRF- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 406 kiqqqigGKVDLMVTGSAPISSTVL-------ETCRVTLGTTIVEG-YGQTECTALATFT---------WMGDPStgHCG 468
Cdd:PRK06178 320 -------AEYDLSSLRQVRVVSFVKklnpdyrQRWRALTGSVLAEAaWGMTETHTCDTFTagfqdddfdLLSQPV--FVG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 469 APAPCALVKLGDVPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFK 548
Cdd:PRK06178 391 LPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17556552 549 LaQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLER---WLIAVVVPEPD------VLKEW 598
Cdd:PRK06178 470 V-NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDkgqVPVAFVQLKPGadltaaALQAW 527
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
105-594 |
9.54e-16 |
|
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: 80.60 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVhefGLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:TIGR03098 26 LTYAALSERVLALASGLR---GLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfkkaESLIKNRENMPT---LKNIIVIDSADELKDGTAIIDTIRVESLtnaLNLGSRYPFTNNLPkpDDNYIICYTSG 261
Cdd:TIGR03098 103 TSS----ERLDLLHPALPGchdLRTLIIVGDPAHASEGHPGEEPASWPKL---LALGDADPPHPVID--SDMAAILYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 262 TTGTPKGVMLTHSNIVA---NISGFLKI-----LFAFQPSMIDA------TQVHI--SYLPLSHMMEQlthwtllgfgsk 325
Cdd:TIGR03098 174 STGRPKGVVLSHRNLVAgaqSVATYLENrpddrLLAVLPLSFDYgfnqltTAFYVgaTVVLHDYLLPR------------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 326 igyfrgsiqgltDDIKTLKP---TVFPVVPRLLNRLydaitskvqqqgfmAKLVYNFAFARKLslvkagkvgrdtiwdRL 402
Cdd:TIGR03098 242 ------------DVLKALEKhgiTGLAAVPPLWAQL--------------AQLDWPESAAPSL---------------RY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 403 VFNKiqqqiGGKVDLMVTgsAPISSTVLETcRVTLgttiveGYGQTECTAlATFTwmgDPST-----GHCGAPAPCALVK 477
Cdd:TIGR03098 281 LTNS-----GGAMPRATL--SRLRSFLPNA-RLFL------MYGLTEAFR-STYL---PPEEvdrrpDSIGKAIPNAEVL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 478 LGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELF-------DE----EGFLQTGDIGEMLPNGTIRIIDRKKHI 546
Cdd:TIGR03098 343 VLR-EDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrplppfpGElhlpELAVWSGDTVRRDEEGFLYFVGRRDEM 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 17556552 547 FKLAqGEYVAPEKIEQVYIRTPVVQQVYVDG---DSLERWLIAVVVPEPDV 594
Cdd:TIGR03098 422 IKTS-GYRVSPTEVEEVAYATGLVAEAVAFGvpdPTLGQAIVLVVTPPGGE 471
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
84-597 |
9.98e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 80.57 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 84 TESNGGPCVGTrssgdadyeflTYDDVHEQAKNLSMTLVHEfGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLY 163
Cdd:PRK06018 30 TRSVEGPIVRT-----------TYAQIHDRALKVSQALDRD-GIKLGD--RVATIAWNTWRHLEAWYGIMGIGAICHTVN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 164 DTLGAEAATFIISQAEISVVIVD-SFKKAESLIKNRenMPTLKNIIVIDSADELKDgTAIIDTIRVESLTNALNLGSRYP 242
Cdd:PRK06018 96 PRLFPEQIAWIINHAEDRVVITDlTFVPILEKIADK--LPSVERYVVLTDAAHMPQ-TTLKNAVAYEEWIAEADGDFAWK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 243 -FTNNLPKPddnyiICYTSGTTGTPKGVMLTHSnivaniSGFLKILFAFQPsmiDAtqvhisylplshmmeqlthwtlLG 321
Cdd:PRK06018 173 tFDENTAAG-----MCYTSGTTGDPKGVLYSHR------SNVLHALMANNG---DA----------------------LG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 322 FGSKigyfrgsiqgltddiktlkPTVFPVVPrllnrLYDA----ITSKVQQQGfmAKLVYNFAF---ARKLSLVKAGKV- 393
Cdd:PRK06018 217 TSAA-------------------DTMLPVVP-----LFHAnswgIAFSAPSMG--TKLVMPGAKldgASVYELLDTEKVt 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 394 ---GRDTIWDRLVfnKIQQQIGGKV---DLMVTGSAPISSTVLETCrVTLGTTIVEGYGQTECTALATFTWMGDPSTGHC 467
Cdd:PRK06018 271 ftaGVPTVWLMLL--QYMEKEGLKLphlKMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTEMSPLGTLAALKPPFSKLP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 468 GAPAPCALVKLGDVP----------DLNYFAKDGK--GEIRIKGPCVTKGYYKDperTAELFDEEGFLQTGDIGEMLPNG 535
Cdd:PRK06018 348 GDARLDVLQKQGYPPfgvemkitddAGKELPWDGKtfGRLKVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYG 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556552 536 TIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW-----LIAVVVPEPDVLKE 597
Cdd:PRK06018 425 YMRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWderplLIVQLKPGETATRE 490
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
250-598 |
1.12e-15 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 80.49 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPSmidatQVHISYLPLSHMMeqlthwtllGFGSKIgYF 329
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIRED-----DVCFSAAKLFFAY---------GLGNSL-TF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 330 RGSIQGLT-------------DDIKTLKPTVFPVVPRLLNRLYDAITSKvqqqgfmaklvynfafARKLSLVKagkvgrd 396
Cdd:cd05959 227 PLSVGATTvlmperptpaavfKRIRRYRPTVFFGVPTLYAAMLAAPNLP----------------SRDLSSLR------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 397 tiwdrlvfnkiqqqiggkvdLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTEctALATF--TWMGDPSTGHCGAPAPCA 474
Cdd:cd05959 284 --------------------LCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGY 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKlAQGEY 554
Cdd:cd05959 342 EVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIW 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYV----DGDSLERwLIAVVVPEP---------DVLKEW 598
Cdd:cd05959 419 VSPFEVESALVQHPAVLEAAVvgveDEDGLTK-PKAFVVLRPgyedsealeEELKEF 474
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
105-591 |
1.42e-15 |
|
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: 79.64 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVhEFGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd12116 13 LSYAELDERANRLAARLR-ARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDsfkkaesliknrenmptlkniividsaDELKDGTAIIDTirvesLTNALNLGSRYPFTNNLPKPDDN---YIIcYTSG 261
Cdd:cd12116 90 TD---------------------------DALPDRLPAGLP-----VLLLALAAAAAAPAAPRTPVSPDdlaYVI-YTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 262 TTGTPKGVMLTHSNIVANISGFLKiLFAFQPS--MIDATQV--HISYLPLshmmeqltHWTLLGFGSKIGYFRGSI---Q 334
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSMRE-RLGLGPGdrLLAVTTYafDISLLEL--------LLPLLAGARVVIAPRETQrdpE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 335 GLTDDIKTLKPTVF---PVVPRLLnrlydaitskvqqqgfmaklvynfafarklslVKAGKVGRDTiwdrlvfnkiqqqi 411
Cdd:cd12116 208 ALARLIEAHSITVMqatPATWRML--------------------------------LDAGWQGRAG-------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 412 ggkVDLMVTGSApiSSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTG-HCGAPAPCALVKLGDvPDLNYFAKD 490
Cdd:cd12116 242 ---LTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPiPIGRPLANTQVYVLD-AALRPVPPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 491 GKGEIRIKGPCVTKGYYKDPERTAELFDEEGFL-------QTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQV 563
Cdd:cd12116 316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgpgsrlyRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAA 394
|
490 500 510
....*....|....*....|....*....|
gi 17556552 564 YIRTPVVQQ--VYVDGDSLERWLIAVVVPE 591
Cdd:cd12116 395 LAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
105-594 |
2.07e-15 |
|
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: 79.31 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVhefGLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd17651 21 LTYAELDRRANRLAHRLR---ARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDsfkkaesliknrenmptlkniiviDSADELKDGTAIIDTIRVESLTNALNLGSRYPFTNnlpkPDD-NYIIcYTSGTT 263
Cdd:cd17651 98 TH------------------------PALAGELAVELVAVTLLDQPGAAAGADAEPDPALD----ADDlAYVI-YTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNiVANISGFLKILFAFQPSmiDATQvhiSYLPLSHMMEQLTHWTLLGFGskigyfrGSIQGLTDDIKTl 343
Cdd:cd17651 149 GRPKGVVMPHRS-LANLVAWQARASSLGPG--ARTL---QFAGLGFDVSVQEIFSTLCAG-------ATLVLPPEEVRT- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 344 kptvfpvVPRLLNRLYDA--ITskvqqQGFMAklvynFAFARklSLVKAGKVGRDTIWD-RLVFnkiqqqIGGKvdlmvt 420
Cdd:cd17651 215 -------DPPALAAWLDEqrIS-----RVFLP-----TVALR--ALAEHGRPLGVRLAAlRYLL------TGGE------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 421 gSAPISSTVLETCRVTLGTTIVEGYGQTEcTALATFTWM-GDPS----TGHCGAPAPCALVKLGD-----VPDlnyfakD 490
Cdd:cd17651 264 -QLVLTEDLREFCAGLPGLRLHNHYGPTE-THVVTALSLpGDPAawpaPPPIGRPIDNTRVYVLDaalrpVPP------G 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 491 GKGEIRIKGPCVTKGYYKDPERTAELFDEEGFL------QTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVY 564
Cdd:cd17651 336 VPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAAL 414
|
490 500 510
....*....|....*....|....*....|...
gi 17556552 565 IRTPVVQQVYV---DGDSLERWLIAVVVPEPDV 594
Cdd:cd17651 415 ARHPGVREAVVlarEDRPGEKRLVAYVVGDPEA 447
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
106-592 |
2.35e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 79.34 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQ---AKNLSMTLvhefGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEIS- 181
Cdd:PRK08008 39 SYLELNEEinrTANLFYSL----GIRKGD--KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 182 VVIVDSFKKAESLIKnRENMPTLKNIIVIDSADELKDGTAIIDTIRVESltnALNLGSRYPFTnnlpkPDDNYIICYTSG 261
Cdd:PRK08008 113 LVTSAQFYPMYRQIQ-QEDATPLRHICLTRVALPADDGVSSFTQLKAQQ---PATLCYAPPLS-----TDDTAEILFTSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 262 TTGTPKGVMLTHSNIVanisgFLKILFAFQPSMiDATQVHISYLPLSHMMEQLTH-WTLLGFGSK-IGYFRGSIQGLTDD 339
Cdd:PRK08008 184 TTSRPKGVVITHYNLR-----FAGYYSAWQCAL-RDDDVYLTVMPAFHIDCQCTAaMAAFSAGATfVLLEKYSARAFWGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 IKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVYnfafarKLSLVKAGKvgrDTIWDRlvFNkiqqqiggkvdlmv 419
Cdd:PRK08008 258 VCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMF------YLNLSDQEK---DAFEER--FG-------------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 tgsapisstvletcrVTLGTTivegYGQTEctalaTFTWM-GDPSTGH-----CGAPAPCALVKLGDVpDLNYFAKDGKG 493
Cdd:PRK08008 313 ---------------VRLLTS----YGMTE-----TIVGIiGDRPGDKrrwpsIGRPGFCYEAEIRDD-HNRPLPAGEIG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 494 EIRIKG-PCVT--KGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVV 570
Cdd:PRK08008 368 EICIKGvPGKTifKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKI 446
|
490 500
....*....|....*....|....*
gi 17556552 571 QQVYVDG--DSLERWLI-AVVVPEP 592
Cdd:PRK08008 447 QDIVVVGikDSIRDEAIkAFVVLNE 471
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
247-590 |
4.26e-15 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 78.28 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 247 LPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKI--LFAFQPSMIDATQVHISYLPLSHMMEQLTHWTLLGFGS 324
Cdd:cd17650 89 LTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREyeLDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 325 KIgyfRGSIQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQGFMAKLVynfafarklslvkagkVGRDTIwdrlvf 404
Cdd:cd17650 169 EV---KLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLI----------------VGSDGC------ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 405 nkiqqqiggkvdlmvtgsaPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDpsTGHCGApapcALVKLGD-VPD 483
Cdd:cd17650 224 -------------------KAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGR--DPLGDS----ANVPIGRpLPN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 484 LNYFAKDGK---------GEIRIKGPCVTKGYYKDPERTAELFDEEGF------LQTGDIGEMLPNGTIRIIDRKKHIFK 548
Cdd:cd17650 279 TAMYVLDERlqpqpvgvaGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVK 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 17556552 549 LaQGEYVAPEKIEQVYIRTPVVQQVYV---DGDSLERWLIAVVVP 590
Cdd:cd17650 359 I-RGFRIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVA 402
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
221-597 |
5.12e-15 |
|
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: 78.32 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 221 AIID-TIRVESLTNALNLGSRYPFTNNL----PKPDDNYIICYTSGTTGTPKGVMLTHSNIVAnisgflKILFAfqpsmi 295
Cdd:cd05923 115 AIFQsGVRVLALSDLVGLGEPESAGPLIedppREPEQPAFVFYTSGTTGLPKGAVIPQRAAES------RVLFM------ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 296 dATQVHISY---------LPLSHMMeqlthwtllGF-----GSKIgyFRGSIQGLTDD--------IKTLKPTVFPVVPR 353
Cdd:cd05923 183 -STQAGLRHgrhnvvlglMPLYHVI---------GFfavlvAALA--LDGTYVVVEEFdpadalklIEQERVTSLFATPT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 354 LlnrlYDAITSKVQQQGfmaklvynfafaRKLSLVkagkvgrdtiwDRLVFnkiqqqiggkvdlmvtGSAPISSTVLETC 433
Cdd:cd05923 251 H----LDALAAAAEFAG------------LKLSSL-----------RHVTF----------------AGATMPDAVLERV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 434 RVTLGTTIVEGYGQTEctaLATFTWMGDPSTGHCGAP---APCALVKLGDVPDlnYFAKDG-KGEIRIK--GPCVTKGYY 507
Cdd:cd05923 288 NQHLPGEKVNIYGTTE---AMNSLYMRDARTGTEMRPgffSEVRIVRIGGSPD--EALANGeEGELIVAaaADAAFTGYL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 508 KDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---L 584
Cdd:cd05923 363 NQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWgqsV 440
|
410
....*....|...
gi 17556552 585 IAVVVPEPDVLKE 597
Cdd:cd05923 441 TACVVPREGTLSA 453
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
106-577 |
6.84e-15 |
|
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: 77.47 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:cd05971 8 TFKELKTASNRFANVL-KEIGLEKGDR--VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 DSfkkaesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpkPDDNYIICYTSGTTGT 265
Cdd:cd05971 85 DG--------------------------------------------------------------SDDPALIIYTSGTTGP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 266 PKGVMLTHSNIVANISGfLKILFAFQPSMIDatqvhISYLPlshmmeqlTHWtllgfgskigyfrGSIQGLTDdikTLKP 345
Cdd:cd05971 103 PKGALHAHRVLLGHLPG-VQFPFNLFPRDGD-----LYWTP--------ADW-------------AWIGGLLD---VLLP 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 346 TVFPVVPRLLNRLydaitskvqqQGF--------MAKLVYNFAF--ARKLSLVKAGKVGRDTiWDRlvfnkiqqqiggKV 415
Cdd:cd05971 153 SLYFGVPVLAHRM----------TKFdpkaaldlMSRYGVTTAFlpPTALKMMRQQGEQLKH-AQV------------KL 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 416 DLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALAT-FTWMGDPSTGHCGAPAPCALVKLGDvPDLNYFAKDGKGE 494
Cdd:cd05971 210 RAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGnCSALFPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 495 IRIKGPCVTK--GYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:cd05971 289 IAVELPDPVAflGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLM 366
|
....*
gi 17556552 573 VYVDG 577
Cdd:cd05971 367 AAVVG 371
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
103-591 |
1.54e-14 |
|
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: 76.70 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 103 EFLTYDDVHEQAKNLSMTLVHefgLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISV 182
Cdd:cd17644 24 QQLTYEELNTKANQLAHYLQS---LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 vivdsfkkaesLIKNRENMPtlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpkpddnYIIcYTSGT 262
Cdd:cd17644 101 -----------LLTQPENLA---------------------------------------------------YVI-YTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 263 TGTPKGVMLTHSNIVANISGFLKILFAFQPSMIdatqvhisylplshmmeqlthwtlLGFGSkIGyFRGSIQGLTDDIkt 342
Cdd:cd17644 118 TGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRV------------------------LQFAS-IA-FDVAAEEIYVTL-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 343 LKPTVFPVVPRLLNRLYDAITSKVQQQgfmaKL-VYNFAFArklslvkagkvgrdtIWDRLVFNKIQQQIGG--KVDLMV 419
Cdd:cd17644 170 LSGATLVLRPEEMRSSLEDFVQYIQQW----QLtVLSLPPA---------------YWHLLVLELLLSTIDLpsSLRLVI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 420 TGSAPISSTVLETCRVTLGTTI--VEGYGQTECTALATFTWMGDPSTGHCGAPA---PCALVK-------LGDVPdlnyf 487
Cdd:cd17644 231 VGGEAVQPELVRQWQKNVGNFIqlINVYGPTEATIAATVCRLTQLTERNITSVPigrPIANTQvyildenLQPVP----- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 488 aKDGKGEIRIKGPCVTKGYYKDPERTAELF--------DEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEK 559
Cdd:cd17644 306 -VGVPGELHIGGVGLARGYLNRPELTAEKFishpfnssESERLYKTGDLARYLPDGNIEYLGRIDNQVKI-RGFRIELGE 383
|
490 500 510
....*....|....*....|....*....|....*
gi 17556552 560 IEQVYIRTPVVQQVYV---DGDSLERWLIAVVVPE 591
Cdd:cd17644 384 IEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPH 418
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
166-593 |
2.24e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.52 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 166 LGAEAATFIISQAEISVVIVDS-----FKKAESLIKNrenmptlKNIIVIDSADELKDGTAIIDTIRVESLtnalnLGSR 240
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTefaevAREALALLPG-------PKPLVIDVDDPEYPGGRFIGALDYEAF-----LASG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 241 YP-FTNNLPKPD-DNYIICYTSGTTGTPKGVMLTHS----NIVANIsgflkILFAFQPsmidatqvHISYLplshmmeql 314
Cdd:PRK08162 170 DPdFAWTLPADEwDAIALNYTSGTTGNPKGVVYHHRgaylNALSNI-----LAWGMPK--------HPVYL--------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 315 thWTLLGFGSKIGYFRGSIQGLTDDIKTLKPtvfpVVPRLLnrlYDAI-TSKVQQQGfMAKLVYNFafarklsLVKAGKV 393
Cdd:PRK08162 228 --WTLPMFHCNGWCFPWTVAARAGTNVCLRK----VDPKLI---FDLIrEHGVTHYC-GAPIVLSA-------LINAPAE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 394 GRDTIwdrlvfnkiqqqiGGKVDLMVTGSAPiSSTVLETCRvTLGTTIVEGYGQTECTALATFT-----W---------- 458
Cdd:PRK08162 291 WRAGI-------------DHPVHAMVAGAAP-PAAVIAKME-EIGFDLTHVYGLTETYGPATVCawqpeWdalplderaq 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 459 ----------------MGDPSTGhcgAPAPcalvklgdvpdlnyfaKDGK--GEIRIKGPCVTKGYYKDPERTAELFdEE 520
Cdd:PRK08162 356 lkarqgvryplqegvtVLDPDTM---QPVP----------------ADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AG 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17556552 521 GFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVqqvyvdgdslerwLIAVVVPEPD 593
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVLYRHPAV-------------LVAAVVAKPD 474
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
258-615 |
2.25e-14 |
|
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: 75.96 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPSmiDATqvhisyLPLSHMmeqlthwtLLGFGSKIGYFRGSIQGLT 337
Cdd:cd05919 98 YSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPG--DRV------FSSAKM--------FFGYGLGNSLWFPLAVGAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 --------------DDIKTLKPTVFPVVPRLLNRLydaITSKVQQQGFMAKLvynfafarklslvkagkvgrdtiwdRLV 403
Cdd:cd05919 162 avlnpgwptaervlATLARFRPTVLYGVPTFYANL---LDSCAGSPDALRSL-------------------------RLC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 404 fnkiqqqiggkvdlmVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDvPD 483
Cdd:cd05919 214 ---------------VSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 484 LNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQV 563
Cdd:cd05919 278 GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESL 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17556552 564 YIRTPVVQQVYV----DGDSLERwLIAVVVPEPDVlkewnDKQGSGSRKIEEICND 615
Cdd:cd05919 356 IIQHPAVAEAAVvavpESTGLSR-LTAFVVLKSPA-----APQESLARDIHRHLLE 405
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
105-594 |
6.47e-14 |
|
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: 74.61 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd12114 13 LTYGELAERARRVAGAL-KAAGVRPGDL--VAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfkkaeSLIKNREnmPTLKNIIVIDSADELKDgtaiidtirvesltnalnlgsryPFTNNLPKPDD-NYIIcYTSGTT 263
Cdd:cd12114 90 TDG-----PDAQLDV--AVFDVLILDLDALAAPA-----------------------PPPPVDVAPDDlAYVI-FTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 264 GTPKGVMLTHSNIVANIsgfLKILFAFQpsmIDATQVHISYLPLSHMMEQLTHWTLLGFGSKI----GYFRGSIQGLTDD 339
Cdd:cd12114 139 GTPKGVMISHRAALNTI---LDINRRFA---VGPDDRVLALSSLSFDLSVYDIFGALSAGATLvlpdEARRRDPAHWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 340 IKTLKPTVFPVVPRLLNRLYDAITSkvqqqgfmaklvynfAFARKLSLvkagkvgrdtiwdRLVF---NKIQQQIGGKVD 416
Cdd:cd12114 213 IERHGVTLWNSVPALLEMLLDVLEA---------------AQALLPSL-------------RLVLlsgDWIPLDLPARLR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 417 LMVTGSAPISstvletcrvtLGttivegyGQTECTalatfTWmgdpSTGHCGAPAPCALV------------------KL 478
Cdd:cd12114 265 ALAPDARLIS----------LG-------GATEAS-----IW----SIYHPIDEVPPDWRsipygrplanqryrvldpRG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 479 GDVPDLnyfakdGKGEIRIKGPCVTKGYYKDPERTAELF----DEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEY 554
Cdd:cd12114 319 RDCPDW------VPGELWIGGRGVALGYLGDPELTAARFvthpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYR 391
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 17556552 555 VAPEKIEQVYIRTPVVQQ--VYVDGDSLERWLIAVVVPEPDV 594
Cdd:cd12114 392 IELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDG 433
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
249-554 |
8.81e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 74.55 E-value: 8.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 249 KPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGfLKILFAFQPSMID-ATqvhisyLPLSHMmeqltHWTLLGFGSKIG 327
Cdd:PRK09274 172 APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LREDYGIEPGEIDlPT------FPLFAL-----FGPALGMTSVIP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 328 YFRGSiqgltddiktlKP-TVFPvvprllNRLYDAItskvQQQGfmaklVYNFAFARKLslvkAGKVGRDTIWDRLVFNK 406
Cdd:PRK09274 240 DMDPT-----------RPaTVDP------AKLFAAI----ERYG-----VTNLFGSPAL----LERLGRYGEANGIKLPS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 407 IQQQIGGkvdlmvtgSAPISSTVLETCRVTL--GTTIVEGYGQTEC---------TALATFTWMGDPSTGHC-GAPAPCA 474
Cdd:PRK09274 290 LRRVISA--------GAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiesrEILFATRAATDNGAGICvGRPVDGV 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVK---LGDVP-----DLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAE--LFDEEG--FLQTGDIGEMLPNGTIRIIDR 542
Cdd:PRK09274 362 EVRiiaISDAPipewdDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGR 441
|
330
....*....|..
gi 17556552 543 KKHIFKLAQGEY 554
Cdd:PRK09274 442 KAHRVETAGGTL 453
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
254-597 |
1.30e-13 |
|
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: 73.59 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 254 YIIcYTSGTTGTPKGVMLTHSNIVANISGFLKILFAFQPSMiDATQVHISYLpLSHMMEQLTHwTLLGfGSKIGYfrgsi 333
Cdd:cd17648 98 YAI-YTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD-EAVLFFSNYV-FDFFVEQMTL-ALLN-GQKLVV----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 334 qgLTDDIKTLKPTVFPVVPRllNRL-YDAITSKVQQQgfmaklvynFAFARKLSLVKAGKVGRDtiWDRLVFNKIQQQIG 412
Cdd:cd17648 168 --PPDEMRFDPDRFYAYINR--EKVtYLSGTPSVLQQ---------YDLARLPHLKRVDAAGEE--FTAPVFEKLRSRFA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 413 GKvdlmvtgsapisstvletcrvtlgttIVEGYGQTEC--TALATFTWMGDPSTGHCGAPAP-CALVKLGDvpDLNYFAK 489
Cdd:cd17648 233 GL--------------------------IINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRnTKCYVLND--AMKRVPV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 490 DGKGEIRIKGPCVTKGYYKDPERTAELFDEEGF--------------LQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYV 555
Cdd:cd17648 285 GAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQVKI-RGQRI 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17556552 556 APEKIEQVYIRTPVVQQVYV-------DGDSLE-RWLIAVVVPEPDVLKE 597
Cdd:cd17648 364 EPGEVEAALASYPGVRECAVvakedasQAQSRIqKYLVGYYLPEPGHVPE 413
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
91-681 |
1.45e-13 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 74.51 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 91 CVG-TRSSGDAdyEFLTYDDVHEQAKNLSMTLVhEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLydtlGAE 169
Cdd:PTZ00297 445 CLGqTSESGES--EWLTYGTVDARARELGSGLL-ALGVRPGDV--IGVDCEASRNIVILEVACALYGFTTLPL----VGK 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 170 AATF--IISQAEISVVIVDSFKKAESLIKNRENMPTLKNiiVIDSADELKDGTAIIDTIRVESLTNALNLGSRYPFtnnL 247
Cdd:PTZ00297 516 GSTMrtLIDEHKIKVVFADRNSVAAILTCRSRKLETVVY--THSFYDEDDHAVARDLNITLIPYEFVEQKGRLCPV---P 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKP--DDNYIICYTSGTTGTPKG-----VMLTHSNIVANISgfLKILFAFQPSMIDATQVhISYLPLSHMMEQLTHWTLL 320
Cdd:PTZ00297 591 LKEhvTTDTVFTYVVDNTTSASGdglavVRVTHADVLRDIS--TLVMTGVLPSSFKKHLM-VHFTPFAMLFNRVFVLGLF 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 321 GFGSKIGYFRGSiqGLTDDIKTLKPTVFPVVPRLLNrlydaiTSKVQ----QQGFMAklVYNFAFAR--KLSLVKAGKVG 394
Cdd:PTZ00297 668 AHGSAVATVDAA--HLQRAFVKFQPTILVAAPSLFS------TSRLQlsraNERYSA--VYSWLFERafQLRSRLINIHR 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 395 RDTIWDRLVFNK-IQQQIGGKVDLMVTGSAPISSTVletcrvTLGTTIVEGYgqTECTALATFTwmgdPSTGHC---GAP 470
Cdd:PTZ00297 738 RDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTSF------SLLEHISVCY--VPCLREVFFL----PSEGVFcvdGTP 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 471 APCALVKLGDVPDLNYFAKDGKGEIRIKGpcvtkgyykDPERTAELfdeeGFLQTGDigemlpnGTIRIIDRKKHIFKLA 550
Cdd:PTZ00297 806 APSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI----AAQWKRD-------RTLRLLGPPLGILLPV 865
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 551 QGEYVAPEKIEQVYIRTPVVQQVYVDGDSLeRWLIAVVVPEPDVLK-EWNDKQ-----GSGSRKIEEICNDEKAKEFVLS 624
Cdd:PTZ00297 866 AYEYVIAAELERIFSQSRYVNDIFLYADPS-RPIIAIVSPNRDTVEfEWRQSHcmgegGGPARQLGWTELVAYASSLLTA 944
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 17556552 625 ELHAIGKANKLNSIEQVKKVILTSDTFTVENGLLTPTLKAKRPQLRLKYKDGMAKVY 681
Cdd:PTZ00297 945 DFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
397-596 |
2.71e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 72.60 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 397 TIWDRLvfnkIQQQIGG-KVDL--MVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPC 473
Cdd:cd05974 185 TVWRML----IQQDLASfDVKLreVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 474 ALVKLGDvPDLNYfAKDGK-----GEIRIKGpcVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFK 548
Cdd:cd05974 261 YRVALLD-PDGAP-ATEGEvaldlGDTRPVG--LMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17556552 549 lAQGEYVAPEKIEQVYIRTPVVQQvyvdgdslerwliAVVVPEPDVLK 596
Cdd:cd05974 336 -SSDYRISPFELESVLIEHPAVAE-------------AAVVPSPDPVR 369
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
254-598 |
3.39e-13 |
|
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: 72.40 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 254 YIIcYTSGTTGTPKGVMLTHSNIVANIsgflkilfafqpsmidatQVHISYLPLSHMMEQLtHWTLLGF-GSKIGYFRGS 332
Cdd:cd17649 98 YVI-YTSGSTGTPKGVAVSHGPLAAHC------------------QATAERYGLTPGDREL-QFASFNFdGAHEQLLPPL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 333 IQGLTddiktlkptvfpVVPRLLNRLYDA--ITSKVQQQGF-MAKL--VYNFAFARKLslvkagkvgRDTIWDRlvfnki 407
Cdd:cd17649 158 ICGAC------------VVLRPDELWASAdeLAEMVRELGVtVLDLppAYLQQLAEEA---------DRTGDGR------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 408 qqqiGGKVDLMVTGSAPISSTVLE---TCRVTLgttiVEGYGQTECTALATfTWMGDPSTGHCGAPAPCALVkLGDV--- 481
Cdd:cd17649 211 ----PPSLRLYIFGGEALSPELLRrwlKAPVRL----FNAYGPTEATVTPL-VWKCEAGAARAGASMPIGRP-LGGRsay 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 ---PDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGF-------LQTGDIGEMLPNGTIRIIDRKKHIFKLaQ 551
Cdd:cd17649 281 ildADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgapgsrlYRTGDLARWRDDGVIEYLGRVDHQVKI-R 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17556552 552 GEYVAPEKIEQVYIRTPVVQQVYV---DGDSLERwLIAVVVPE-PDVLKEW 598
Cdd:cd17649 360 GFRIELGEIEAALLEHPGVREAAVvalDGAGGKQ-LVAYVVLRaAAAQPEL 409
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
247-598 |
6.06e-13 |
|
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: 71.43 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 247 LPKPDDNYIICYTSGTTGTPKGVMLTHSNIVaNISGFLKILFAFQPSmiDATQVHISYLPLSHMMEQLTHWTLlgfGSKI 326
Cdd:cd17645 100 LTNPDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPA--DKSLVYASFSFDASAWEIFPHLTA---GAAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 327 GYF----RGSIQGLTDDIKTLKPTVfpvvprllnrlyDAITSKVQQQgFMAklVYNFAFARKLSlvkagkvGRDtiwdrl 402
Cdd:cd17645 174 HVVpserRLDLDALNDYFNQEGITI------------SFLPTGAAEQ-FMQ--LDNQSLRVLLT-------GGD------ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 403 VFNKIQQQiggkvdlmvtgsapisstvletcrvtlGTTIVEGYGQTECTALATFTWMgDPSTGHCGAPAPCALVKLGDVP 482
Cdd:cd17645 226 KLKKIERK---------------------------GYKLVNNYGPTENTVVATSFEI-DKPYANIPIGKPIDNTRVYILD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 483 DLNYFAKDG-KGEIRIKGPCVTKGYYKDPERTAELFDEEGFL------QTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYV 555
Cdd:cd17645 278 EALQLQPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRI 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17556552 556 APEKIEQVYIRTPVVQQVYV----DGDSlERWLIAVVVP----EPDVLKEW 598
Cdd:cd17645 357 EPGEIEPFLMNHPLIELAAVlakeDADG-RKYLVAYVTApeeiPHEELREW 406
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
417-592 |
1.16e-12 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 70.82 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 417 LMVTGSAPISSTVLETCRVTLGTTIVEGYGQTEctALATFTWMGDPSTGHC---GAPA-PCALVKLGDvPDLNYFAKDGK 492
Cdd:cd05920 259 LLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTRLDDPDEVIIhtqGRPMsPDDEIRVVD-EEGNPVPPGEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRHPAVHD 414
|
170 180
....*....|....*....|...
gi 17556552 573 VYVDGDSLERW---LIAVVVPEP 592
Cdd:cd05920 415 AAVVAMPDELLgerSCAFVVLRD 437
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
141-592 |
1.76e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 70.16 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 141 NSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV-DSFKK---AESLIK-NRENMPTLKNIIVIDSADE 215
Cdd:PRK06164 69 NCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVwPGFKGidfAAILAAvPPDALPPLRAIAVVDDAAD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 216 LKDGTAIIDTIRVEsltnALNLGSRYPFTNNLPKPDDNYIICYT-SGTTGTPKGVM------LTHSNIVANISGflkilf 288
Cdd:PRK06164 149 ATPAPAPGARVQLF----ALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLhrqatlLRHARAIARAYG------ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 289 afqpsmIDATQVHISYLPLShmmeqlthwTLLGFGSKIGYFRGSiqgltddiktlkptvfpvVPRLLNRLYDAitskvqq 368
Cdd:PRK06164 219 ------YDPGAVLLAALPFC---------GVFGFSTLLGALAGG------------------APLVCEPVFDA------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 369 qgfmaklvynfafARKLSLVKAGKV----GRDTIWDRlvfnkIQQQIGGKVD---LMVTGSA---PISSTVLETCRVTlG 438
Cdd:PRK06164 259 -------------ARTARALRRHRVthtfGNDEMLRR-----ILDTAGERADfpsARLFGFAsfaPALGELAALARAR-G 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 439 TTIVEGYGQTECTALATFTWMGDPSTGHC---GAPA-PCALVKLGDVPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTA 514
Cdd:PRK06164 320 VPLTGLYGSSEVQALVALQPATDPVSVRIeggGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 515 ELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVV---QQVYVDGDSLERwLIAVVVPE 591
Cdd:PRK06164 400 RALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVaaaQVVGATRDGKTV-PVAFVIPT 477
|
.
gi 17556552 592 P 592
Cdd:PRK06164 478 D 478
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
105-593 |
1.85e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 70.04 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHEfGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd12115 25 LTYAELNRRANRLAARLRAA-GVGPESR--VGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSFKKAesliknrenmptlkniividsadelkdgtaiidtirvesltnalnlgsrypftnnlpkpddnYIIcYTSGTTG 264
Cdd:cd12115 102 TDPDDLA--------------------------------------------------------------YVI-YTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVAnisgFLK-ILFAFQP----SMIDATQV--HIS----YLPLSHmmeqlthwtllgfGSKIGyfrgsi 333
Cdd:cd12115 119 RPKGVAIEHRNAAA----FLQwAAAAFSAeelaGVLASTSIcfDLSvfelFGPLAT-------------GGKVV------ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 334 qgLTDDIKTLkptvfPVVPR-----LLNRLYDAITSKVQQQGFMAKLvynfafaRKLSLvkAGKVGRDTIWDRlvfnkIQ 408
Cdd:cd12115 176 --LADNVLAL-----PDLPAaaevtLINTVPSAAAELLRHDALPASV-------RVVNL--AGEPLPRDLVQR-----LY 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 409 QQIGGKVdlmvtgsapisstvletcrvtlgttIVEGYGQTECTALATFTWM--GDPSTGHCGAPAPCALVKLGD-----V 481
Cdd:cd12115 235 ARLQVER-------------------------VVNLYGPSEDTTYSTVAPVppGASGEVSIGRPLANTQAYVLDralqpV 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 PDlnyfakdG-KGEIRIKGPCVTKGYYKDPERTAELFDEEGFL------QTGDIGEMLPNGTIRIIDRKKHIFKLaQGEY 554
Cdd:cd12115 290 PL-------GvPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFR 361
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 17556552 555 VAPEKIEQVYIRTPVVQQ--VYVDGDSL-ERWLIAVVVPEPD 593
Cdd:cd12115 362 IELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAEPG 403
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
93-592 |
3.09e-12 |
|
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: 69.48 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 93 GTRSSGDADYEFLTYDDVHEQAKNLSMTLvHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAAT 172
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAAL-RRLGVKREE--RVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 173 FIISQAEISVVIVDS-----FKKAESliknreNMPTLKNIIVIDSADELKDgtaiidtirveSLTNALNLGSRYpFTNNL 247
Cdd:TIGR02262 96 YMLEDSRARVVFVSGallpvIKAALG------KSPHLEHRVVVGRPEAGEV-----------QLAELLATESEQ-FKPAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKPDDNYIICYTSGTTGTPKGVMLTHSNIVA-------NISGF---------LKILFAFQ-------PSMIDATQVHISY 304
Cdd:TIGR02262 158 TQADDPAFWLYSSGSTGMPKGVVHTHSNPYWtaelyarNTLGIreddvcfsaAKLFFAYGlgnaltfPMSVGATTVLMGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 305 LPLSHMMeqlthwtllgfgskigyfrgsiqglTDDIKTLKPTVFPVVPRLLNRLYDAITSKVQQQgfmaklvynfafark 384
Cdd:TIGR02262 238 RPTPDAV-------------------------FDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQ--------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 385 lslvkagkvgrdtiwDRLvfnkiqqqiggkvDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPST 464
Cdd:TIGR02262 278 ---------------VRL-------------RLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRY 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 465 GHCGAPAPCALVKL-----GDVPDlnyfakDGKGEIRIKGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRI 539
Cdd:TIGR02262 330 GTSGKPVPGYRLRLvgdggQDVAD------GEPGELLISGPSSATMYWNNRAKSRDTF-QGEWTRSGDKYVRNDDGSYTY 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 17556552 540 IDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERWLI---AVVVPEP 592
Cdd:TIGR02262 403 AGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIkpkAFVVLRP 457
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
237-562 |
4.47e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.61 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 237 LGSRYP-FTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVANisgflkilfAFQ-PSMIDATQVHISY--LPLSHMMe 312
Cdd:PRK06814 778 LAGRFPlVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLAN---------RAQvAARIDFSPEDKVFnaLPVFHSF- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 313 QLTHWTLLG--FGSKIgYFRGSiqgltddiktlkPTVFPVVPRLlnrLYDA-ITSKVQQQGFM---AKLVYNFAFaRKLS 386
Cdd:PRK06814 848 GLTGGLVLPllSGVKV-FLYPS------------PLHYRIIPEL---IYDTnATILFGTDTFLngyARYAHPYDF-RSLR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 387 LVKAG--KVGRDTiwDRLVFNKiqqqiggkvdlmvtgsapisstvletcrvtLGTTIVEGYGQTECT-ALATFTWMGDPS 463
Cdd:PRK06814 911 YVFAGaeKVKEET--RQTWMEK------------------------------FGIRILEGYGVTETApVIALNTPMHNKA 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 464 tGHCGAPAPCALVKLGDVPDLNyfakDGkGEIRIKGPCVTKGYYKdPERTAELFD-EEGFLQTGDIGEMLPNGTIRIIDR 542
Cdd:PRK06814 959 -GTVGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGYLR-AENPGVLEPpADGWYDTGDIVTIDEEGFITIKGR 1031
|
330 340
....*....|....*....|
gi 17556552 543 KKHIFKLAqGEYVAPEKIEQ 562
Cdd:PRK06814 1032 AKRFAKIA-GEMISLAAVEE 1050
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
121-600 |
5.85e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 68.53 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 121 LVHEF---GLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDS-FkkAESLIK 196
Cdd:PRK07470 45 LAAALaarGVRKGD--RILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHAdF--PEHAAA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 197 NRENMPTLKNIIVIDSADELKDGTAIIdtirvesltnALNLGSRYPftNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNI 276
Cdd:PRK07470 121 VRAASPDLTHVVAIGGARAGLDYEALV----------ARHLGARVA--NAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 277 VANISGFLKILfafqpsMIDATQVHISYL--PLSHmmeqlthwtllGFGskigyfrgsIQGLTDDIKTLKpTVFPVVPRL 354
Cdd:PRK07470 189 AFVITNHLADL------MPGTTEQDASLVvaPLSH-----------GAG---------IHQLCQVARGAA-TVLLPSERF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 355 LnrlYDAITSKVQQQGfmaklVYNFaFA----RKLsLVKAGKVGR-DTIWDRLVfnkiqqqiggkvdlmVTGSAPISSTV 429
Cdd:PRK07470 242 D---PAEVWALVERHR-----VTNL-FTvptiLKM-LVEHPAVDRyDHSSLRYV---------------IYAGAPMYRAD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 430 LETCRVTLGTTIVEGYGQTECTALATFTwmgdPSTGH------------CGAPAPCALVKLGDvPDLNYFAKDGKGEIRI 497
Cdd:PRK07470 297 QKRALAKLGKVLVQYFGLGEVTGNITVL----PPALHdaedgpdarigtCGFERTGMEVQIQD-DEGRELPPGETGEICV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 498 KGPCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:PRK07470 372 IGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
490 500 510
....*....|....*....|....*....|..
gi 17556552 578 DSLERW---LIAVVV------PEPDVLKEWND 600
Cdd:PRK07470 450 VPDPVWgevGVAVCVardgapVDEAELLAWLD 481
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
249-685 |
7.83e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.04 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 249 KPDDNYIICYTSGTTGTPKGVMLTHSNIVANIsgfLKILFAFQpsmIDAT--QVHISYLPLSHMMeqlthwtllgfgski 326
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANE---QLIRHGFG---IDLNpdDVIVSWLPLYHDM--------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 327 gyfrGSIQGLtddiktLKPtVFPVVPRLLnrlydaitskvqqqgfMAKlvyNFAFARKLSLVKAGKVGRDTIWD------ 400
Cdd:PRK05691 223 ----GLIGGL------LQP-IFSGVPCVL----------------MSP---AYFLERPLRWLEAISEYGGTISGgpdfay 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 401 RLVFNKIQQQIGGKVDL-----MVTGSAPISSTVLET-------CRVTlGTTIVEGYGQTECTALATFTWMG-------- 460
Cdd:PRK05691 273 RLCSERVSESALERLDLsrwrvAYSGSEPIRQDSLERfaekfaaCGFD-PDSFFASYGLAEATLFVSGGRRGqgipalel 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 461 ----------DPSTGH----CGAPAPCALVKLGDVPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELF---DEEGFL 523
Cdd:PRK05691 352 daealarnraEPGTGSvlmsCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 524 QTGDIGeMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVY------IRTPVVQQVYVDGDSLERWLIAVVVpepdvlke 597
Cdd:PRK05691 432 RTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVerevevVRKGRVAAFAVNHQGEEGIGIAAEI-------- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 598 wndkqgsgSRKIEEICndeKAKEFVLSELHAIGKAnklnsIEQVKKVILtsdtfTVENGLL--TPTLKAKRPQLRLKYKD 675
Cdd:PRK05691 502 --------SRSVQKIL---PPQALIKSIRQAVAEA-----CQEAPSVVL-----LLNPGALpkTSSGKLQRSACRLRLAD 560
|
490
....*....|
gi 17556552 676 GMAKVYKQFP 685
Cdd:PRK05691 561 GSLDSYALFP 570
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
224-592 |
7.95e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 67.38 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 224 DTIRVESLTNALNLGsrypftnnLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVAN-------ISGFLKILFAFQPSMID 296
Cdd:PRK07824 16 DERRAALLRDALRVG--------EPIDDDVALVVATSGTTGTPKGAMLTAAALTASadathdrLGGPGQWLLALPAHHIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 297 ATQVHIS---------YLPLSHmmeqlthwtllGFgsKIGYFRGSIQGLTDDiktlkptvfpvvprllnRLYdaiTSKVQ 367
Cdd:PRK07824 88 GLQVLVRsviagsepvELDVSA-----------GF--DPTALPRAVAELGGG-----------------RRY---TSLVP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 368 QQgfMAKLVYNFAFARKLSLvkagkvgrdtiwdrlvfnkiqqqiggkVDLMVTGSAPISSTVLETCRvTLGTTIVEGYGQ 447
Cdd:PRK07824 135 MQ--LAKALDDPAATAALAE---------------------------LDAVLVGGGPAPAPVLDAAA-AAGINVVRTYGM 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 448 TEcTAlatftwmgdpstGHC---GAPAPCALVKLGDvpdlnyfakdgkGEIRIKGPCVTKGYYKDPERTAelFDEEGFLQ 524
Cdd:PRK07824 185 SE-TS------------GGCvydGVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVDPDP--FAEPGWFR 237
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17556552 525 TGDIGEmLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQQVYVDG---DSLERWLIAVVVPEP 592
Cdd:PRK07824 238 TDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDG 306
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
250-591 |
1.11e-11 |
|
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: 67.33 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDD-NYIIcYTSGTTGTPKGVMLTHSNIVAnisgflkiLFAFQPSMIDA------TQVHISYLPLShMMEQlthWTLLGF 322
Cdd:cd17643 92 PDDlAYVI-YTSGSTGRPKGVVVSHANVLA--------LFAATQRWFGFneddvwTLFHSYAFDFS-VWEI---WGALLH 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 323 GSKIgyfrgsiqgltddiktlkptvfPVVPRLLNRLYDAITSKVQQQGFMaklVYN---FAFARKLSLVKAGKVGRDTIw 399
Cdd:cd17643 159 GGRL----------------------VVVPYEVARSPEDFARLLRDEGVT---VLNqtpSAFYQLVEAADRDGRDPLAL- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 400 dRLVfnkiqqqiggkvdlmVTGSAPISSTVLETCRVTLG---TTIVEGYGQTECTALATFTWM-------GDPSTghCGA 469
Cdd:cd17643 213 -RYV---------------IFGGEALEAAMLRPWAGRFGldrPQLVNMYGITETTVHVTFRPLdaadlpaAAASP--IGR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 470 PAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGF-------LQTGDIGEMLPNGTIRIIDR 542
Cdd:cd17643 275 PLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGR 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17556552 543 KKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVYV---DGDSLERWLIAVVVPE 591
Cdd:cd17643 354 ADEQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVAD 404
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
101-590 |
1.75e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.88 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSMTLVHEfGLTPAntTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEI 180
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAA-GVGPD--VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVDSfkkaesliknrenmptlkniividsadELKDGTAIIDTIRVESLTNALNLGSRYPFTNNLPKPD-DN--YIIc 257
Cdd:PRK12467 611 RLLLTQS---------------------------HLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALDpDNlaYVI- 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSnivaNISGFLKILFAFQPSMIDAtqvhiSYLPLSHMMEQLTHWTLLGfgskiGYFRGsiqglt 337
Cdd:PRK12467 663 YTSGSTGQPKGVAISHG----ALANYVCVIAERLQLAADD-----SMLMVSTFAFDLGVTELFG-----ALASG------ 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 ddiKTLKptvfpVVPRLLNRLYDAITSKVQQQGFMaklVYNFAFARKLSLVKAGKVGRDTIWDRLVFnkiqqqiGGKVdL 417
Cdd:PRK12467 723 ---ATLH-----LLPPDCARDAEAFAALMADQGVT---VLKIVPSHLQALLQASRVALPRPQRALVC-------GGEA-L 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 418 MVTGSAPISstvletcRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLG----DvPDLNYFAKDGKG 493
Cdd:PRK12467 784 QVDLLARVR-------ALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGlyilD-HYLNPVPVGVVG 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 494 EIRIKGPCVTKGYYKDPERTAELF-------DEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIR 566
Cdd:PRK12467 856 ELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGRLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLA 934
|
490 500
....*....|....*....|....*..
gi 17556552 567 TPVVQQVYV---DGDSlERWLIAVVVP 590
Cdd:PRK12467 935 QPGVREAVVlaqPGDA-GLQLVAYLVP 960
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
249-563 |
3.32e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 66.66 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 249 KPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGfLKILFAFQPSmidatQVHISYLPLSHmmeqlthwtllGFGSKIGY 328
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ-IKTIADFTPN-----DRFMSALPLFH-----------SFGLTVGL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 329 FRGSIQGlTDDIKTLKPTVFPVVPRLLnrlYDAI------TSKVQqqGFMAKLVYNFAFARklslvkagkvgrdtiwdrl 402
Cdd:PRK08043 426 FTPLLTG-AEVFLYPSPLHYRIVPELV---YDRNctvlfgTSTFL--GNYARFANPYDFAR------------------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 403 vfnkiqqqiggkVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVP 482
Cdd:PRK08043 481 ------------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 483 DLnyfaKDGkGEIRIKGPCVTKGYYK--DPER----TAElfDEEGFLQ-----TGDIGEMLPNGTIRIIDRKKHIFKLAq 551
Cdd:PRK08043 549 GI----EQG-GRLQLKGPNIMNGYLRveKPGVlevpTAE--NARGEMErgwydTGDIVRFDEQGFVQIQGRAKRFAKIA- 620
|
330
....*....|..
gi 17556552 552 GEYVAPEKIEQV 563
Cdd:PRK08043 621 GEMVSLEMVEQL 632
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
254-593 |
3.41e-11 |
|
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: 65.74 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 254 YIIcYTSGTTGTPKGVMLTHSNIvanisgflkilfafqPSMIDATQVHISYLPLSHMmeqlthwtlLGFGSKigYFRGSI 333
Cdd:cd17652 97 YVI-YTSGSTGRPKGVVVTHRGL---------------ANLAAAQIAAFDVGPGSRV---------LQFASP--SFDASV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 334 QGLTDDIKTLKPTVfpVVPRLLNRLYDAITSKVQQQGFMAKLVYNFAfarkLSLVKAGKV-GRDTiwdrlvfnkiqqqig 412
Cdd:cd17652 150 WELLMALLAGATLV--LAPAEELLPGEPLADLLREHRITHVTLPPAA----LAALPPDDLpDLRT--------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 413 gkvdLMVTGSAPISSTVLETCRvtlGTTIVEGYGQTECTALATftwMGDPSTGH----CGAPAPCALVKLGD-----VPD 483
Cdd:cd17652 209 ----LVVAGEACPAELVDRWAP---GRRMINAYGPTETTVCAT---MAGPLPGGgvppIGRPVPGTRVYVLDarlrpVPP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 484 lnyfakdG-KGEIRIKGPCVTKGYYKDPERTAELFDEEGF-------LQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYV 555
Cdd:cd17652 279 -------GvPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKI-RGFRI 350
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17556552 556 APEKIEQVYIRTPVVQQVYV---DGDSLERWLIAVVVPEPD 593
Cdd:cd17652 351 ELGEVEAALTEHPGVAEAVVvvrDDRPGDKRLVAYVVPAPG 391
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
69-598 |
3.72e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.90 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 69 YPEVATLHDVFVKGKTESNGGPCVgtrSSGDadyEFLTYDDVHEQAKNLSMTLVhEFGLTPANTtnIGIYARNSPQWLVS 148
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPAL---AFGE---ETLDYAELNRRANRLAHALI-ERGVGPDVL--VGVAMERSIEMVVA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 149 AVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDSFKKAEsliknrenMPTLKNIIVIDsadeLKDGTAIIDTIRV 228
Cdd:PRK12316 578 LLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRK--------LPLAAGVQVLD----LDRPAAWLEGYSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 229 ESLTNALNlgsrypfTNNLPkpddnYIIcYTSGTTGTPKGVMLTHSNIVANISGFLKilfAFQPSMIDAT-QVHISYLPL 307
Cdd:PRK12316 646 ENPGTELN-------PENLA-----YVI-YTSGSTGKPKGAGNRHRALSNRLCWMQQ---AYGLGVGDTVlQKTPFSFDV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 308 SHMMeqlTHWTLLGFGSKI----GYFRgSIQGLTDDIKTLKPTVFPVVPRLLNRLydaitskvQQQGFMAKLvynfafar 383
Cdd:PRK12316 710 SVWE---FFWPLMSGARLVvaapGDHR-DPAKLVELINREGVDTLHFVPSMLQAF--------LQDEDVASC-------- 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 384 kLSLVKAGKVGRDTIWDrlvfnkIQQQIGGKvdlmvtgsapisstvLETCRvtlgttIVEGYGQTECTALAT-FTWM--- 459
Cdd:PRK12316 770 -TSLRRIVCSGEALPAD------AQEQVFAK---------------LPQAG------LYNLYGPTEAAIDVThWTCVeeg 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 460 -GDPSTGHCGAPAPCALV--KLGDVPdlnyfaKDGKGEIRIKGPCVTKGYYKDPERTAELF------DEEGFLQTGDIGE 530
Cdd:PRK12316 822 gDSVPIGRPIANLACYILdaNLEPVP------VGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLAR 895
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556552 531 MLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVYV---DGdsleRWLIAVVVPE------PDVLKEW 598
Cdd:PRK12316 896 YRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVlavDG----KQLVGYVVLEseggdwREALKAH 967
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
103-277 |
5.10e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 65.69 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 103 EFLTYDDVHEQAKNLSMTLVHefgLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISV 182
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDS---LKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 VIvdsfkkaesliknrenmptlkniividSADELKDGTAIIDTIRVESLTNALNLGSRYPFTNNLpKPDDNYIICYTSGT 262
Cdd:PRK04813 103 II---------------------------ATEELPLEILGIPVITLDELKDIFATGNPYDFDHAV-KGDDNYYIIFTSGT 154
|
170
....*....|....*
gi 17556552 263 TGTPKGVMLTHSNIV 277
Cdd:PRK04813 155 TGKPKGVQISHDNLV 169
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-598 |
6.19e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.13 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVhEFGLTPAntTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-ARGVGPE--VRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 vdsfkkAESLIKNRENMPTLKNIIVIDSADELKDgtaiidtirvesltnalnlgsrYPFTNNLPK--PDD-NYIIcYTSG 261
Cdd:PRK12316 2106 ------TQRHLLERLPLPAGVARLPLDRDAEWAD----------------------YPDTAPAVQlaGENlAYVI-YTSG 2156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 262 TTGTPKGVMLTHSNIVANISGflkilfAFQPSMIDATQVHISYLPLShmmeqlthwtllgfgskigyFRGSIQGL-TDDI 340
Cdd:PRK12316 2157 STGLPKGVAVSHGALVAHCQA------AGERYELSPADCELQFMSFS--------------------FDGAHEQWfHPLL 2210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 341 KTLKPTVFPVVPRLLNRLYDAItskvQQQGFMaklVYNFAFARKLSLVKAGKVGRDTIwdrlvfnkiqqqiggKVDLMVT 420
Cdd:PRK12316 2211 NGARVLIRDDELWDPEQLYDEM----ERHGVT---ILDFPPVYLQQLAEHAERDGRPP---------------AVRVYCF 2268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 421 GSAPISSTVLETCRVTLGTT-IVEGYGQTEcTALATFTWMGDPSTGhCGAPAPCALVKLGDV------PDLNYFAKDGKG 493
Cdd:PRK12316 2269 GGEAVPAASLRLAWEALRPVyLFNGYGPTE-AVVTPLLWKCRPQDP-CGAAYVPIGRALGNRrayildADLNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 494 EIRIKGPCVTKGYYKDPERTAELFDEEGF-------LQTGDIGEMLPNGTIRIIDRKKHI-----FKLAQGEYVApEKIE 561
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQvkirgFRIELGEIEA-RLQA 2425
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 17556552 562 QVYIRTPVVqqVYVDGDSLERwLIAVVVPE------PDVLKEW 598
Cdd:PRK12316 2426 HPAVREAVV--VAQDGASGKQ-LVAYVVPDdaaedlLAELRAW 2465
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
106-594 |
1.46e-10 |
|
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: 64.04 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLVHEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:cd05958 12 TYRDLLALANRIANVLVGELGIVPGN--RVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 DsfkkaesliknrenmptlkniividsadelkdgtaiidtirvESLTNAlnlgsrypftnnlpkpDDNYIICYTSGTTGT 265
Cdd:cd05958 90 A------------------------------------------HALTAS----------------DDICILAFTSGTTGA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 266 PKGVMLTHSNIVANISGFLKILFAFQPSmidatQVHISYLPLShmmeqlthwtlLGFG-------------SKIGYFRGS 332
Cdd:cd05958 112 PKATMHFHRDPLASADRYAVNVLRLRED-----DRFVGSPPLA-----------FTFGlggvllfpfgvgaSGVLLEEAT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 333 IQGLTDDIKTLKPTVfpvvprllnrLYDAITSkvqqqgfMAKLVYNFAFArklslvkagkvgrdtiwdrlvfnkiqQQIG 412
Cdd:cd05958 176 PDLLLSAIARYKPTV----------LFTAPTA-------YRAMLAHPDAA--------------------------GPDL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 413 GKVDLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDvpDLNYFAKDGK 492
Cdd:cd05958 213 SSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDGT 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 -GEIRIKGPcvTKGYYKDPERTAELFDEeGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQVYIRTPVVQ 571
Cdd:cd05958 291 iGRLAVRGP--TGCRYLADKRQRTYVQG-GWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVA 366
|
490 500
....*....|....*....|....*.
gi 17556552 572 QVYVDGDSLERWLI---AVVVPEPDV 594
Cdd:cd05958 367 ECAVVGHPDESRGVvvkAFVVLRPGV 392
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
141-563 |
1.52e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.26 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 141 NSPQWLVSAVACVEQSMVVVPLYDTLgaEAATfIISQAEISvvivdsfkKAESLIKNRENMptlkniivIDSAdELKDGT 220
Cdd:PRK05857 75 NGPETYLSVLACAKLGAIAVMADGNL--PIAA-IERFCQIT--------DPAAALVAPGSK--------MASS-AVPEAL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 221 AIIDTIRVESLTN----ALNLGSRYPFTNNLPKPDDNYIICYTSGTTGTPKGVMLTHSNIVAnisgFLKILFAFQPSMID 296
Cdd:PRK05857 135 HSIPVIAVDIAAVtresEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFA----VPDILQKEGLNWVT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 297 ATQVHISYLPLShmmeqLTH-----WTLLGFGSKIGYFRGSIQG--LTDDIKTLKPTVFPVVPRLLnrlydaitskvqqq 369
Cdd:PRK05857 211 WVVGETTYSPLP-----ATHigglwWILTCLMHGGLCVTGGENTtsLLEILTTNAVATTCLVPTLL-------------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 370 gfmAKLVYNFAFArklslvkagkvgrDTIWDRLVFnkiqqqiggkvdLMVTGSAPISSTVLETCRVTLGTTIVEGYGQTE 449
Cdd:PRK05857 272 ---SKLVSELKSA-------------NATVPSLRL------------VGYGGSRAIAADVRFIEATGVRTAQVYGLSETG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 450 CTALATFTWMGDPS---TGHCGAPAPCALVKLGDVPDLNYFAKDGK-----GEIRIKGPCVTKGYYKDPERTAELFdEEG 521
Cdd:PRK05857 324 CTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 17556552 522 FLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQV 563
Cdd:PRK05857 403 WVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI 443
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
493-593 |
1.55e-10 |
|
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: 64.01 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKK-HIFKlaQGEYVAPEKIEQVYIRTPVVQ 571
Cdd:COG1021 381 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENLLLAHPAVH 458
|
90 100
....*....|....*....|..
gi 17556552 572 QvyvdgdslerwliAVVVPEPD 593
Cdd:COG1021 459 D-------------AAVVAMPD 467
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
248-593 |
1.66e-10 |
|
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: 63.83 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKPDD-NYIIcYTSGTTGTPKGVMLTHSNIVANISGF-------------LKILFAFQPSMIDAtqvhisYLPLSH---- 309
Cdd:cd17646 135 PRPDNlAYVI-YTSGSTGRPKGVMVTHAGIVNRLLWMqdeyplgpgdrvlQKTPLSFDVSVWEL------FWPLVAgarl 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 310 -MMEQLTHwtllgfgSKIGYfrgsiqgLTDDIKTLKPTVFPVVPRLLnrlydaitskvqqQGFMAKLvynfAFARKLSLv 388
Cdd:cd17646 208 vVARPGGH-------RDPAY-------LAALIREHGVTTCHFVPSML-------------RVFLAEP----AAGSCASL- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 389 kagkvgrdtiwdRLVFnkiqqqIGGKVdlmvtgsapISSTVLETCRVTLGTTIVEGYGQTECTALATFtWMGDPSTGH-- 466
Cdd:cd17646 256 ------------RRVF------CSGEA---------LPPELAARFLALPGAELHNLYGPTEAAIDVTH-WPVRGPAETps 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 467 --CGAPAPCALVKLGDvPDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQ------TGDIGEMLPNGTIR 538
Cdd:cd17646 308 vpIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALE 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17556552 539 IIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVYV---DGDSLERWLIAVVVPEPD 593
Cdd:cd17646 387 FLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
95-273 |
3.84e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.99 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 95 RSSGDADYEFLTYDDVHEQAkNLSMTLVHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAatfI 174
Cdd:PRK04319 64 RYLDASRKEKYTYKELKELS-NKFANVLKELGVEKGDR--VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEA---V 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 175 ISQAEIS--VVIVDSFKKAESLIKNRenMPTLKNIIVIDSADELKDGTaiidtIRVESLTNALNLGSRYPFTnnlpKPDD 252
Cdd:PRK04319 138 RDRLEDSeaKVLITTPALLERKPADD--LPSLKHVLLVGEDVEEGPGT-----LDFNALMEQASDEFDIEWT----DRED 206
|
170 180
....*....|....*....|.
gi 17556552 253 NYIICYTSGTTGTPKGVMLTH 273
Cdd:PRK04319 207 GAILHYTSGSTGKPKGVLHVH 227
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
421-605 |
4.25e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 62.32 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 421 GSAPISSTVLETCRvTLGTTIVEGYGQTEcTA--LATFT----WMGDPSTGHcgaPAPCALVKLGDVPDlnyfakdgkGE 494
Cdd:PRK07445 238 GGAPAWPSLLEQAR-QLQLRLAPTYGMTE-TAsqIATLKpddfLAGNNSSGQ---VLPHAQITIPANQT---------GN 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 495 IRIKGPCVTKGYYkdPErtaeLFDEEGFLQTGDIGEMLPNGTIRIIDR--KKHIfklAQGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:PRK07445 304 ITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAILATGLVQD 374
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17556552 573 VYVDGDSLERW---LIAVVVPEPDV-----LKEWNDKQGSG 605
Cdd:PRK07445 375 VCVLGLPDPHWgevVTAIYVPKDPSisleeLKTAIKDQLSP 415
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
248-570 |
4.97e-10 |
|
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: 62.09 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 248 PKPDDNYIICYTSGTTGTPKGVMLTHSNIVANISGfLKILFAFQPSMIDatqvhisyLPlshmmeqlthwTLLGFGskig 327
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDA-LRQLYGIRPGEVD--------LA-----------TFPLFA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 328 yFRGSIQGLTddikTLKPTVFPVVPrllnrlydAITSKVQQQGFMAKLVYNFAFarklslvkagkvGRDTIWDRLVFNKI 407
Cdd:cd05910 138 -LFGPALGLT----SVIPDMDPTRP--------ARADPQKLVGAIRQYGVSIVF------------GSPALLERVARYCA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 408 QQQIG-GKVDLMVTGSAPISSTVLETCRVTL--GTTIVEGYGQTEC---------TALATFTWMGDPSTGHC-GAPAPCA 474
Cdd:cd05910 193 QHGITlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTCvGRPIPGV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 475 LVKLGDVPDLNYFAKDGK--------GEIRIKGPCVTKGYYKDPERTA--ELFDE-EGFL-QTGDIGEMLPNGTIRIIDR 542
Cdd:cd05910 273 RVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATAlaKIDDNsEGFWhRMGDLGYLDDEGRLWFCGR 352
|
330 340
....*....|....*....|....*...
gi 17556552 543 KKHIFKLAQGEYVApEKIEQVYIRTPVV 570
Cdd:cd05910 353 KAHRVITTGGTLYT-EPVERVFNTHPGV 379
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
105-598 |
5.33e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 62.25 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQaknlSMTLVHEF---GLTPanTTNIGIYARNSpQWLVSAVACVEQSMVVVPLYDT-LGAEAATFIISQAEI 180
Cdd:PRK07788 75 LTYAELDEQ----SNALARGLlalGVRA--GDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVDS-FkkAESLIKNRENMPTLKNIIVIDSADELKDGTaiidtirVESLTNALNLGSRYPftnnLPKPDDN-YIICY 258
Cdd:PRK07788 148 KALVYDDeF--TDLLSALPPDLGRLRAWGGNPDDDEPSGST-------DETLDDLIAGSSTAP----LPKPPKPgGIVIL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 259 TSGTTGTPKGVMLTHSNIVANISGFLkilfafqpsmidatqvhiSYLPL-SHMMEQLT----------HWTL-LGFGSKI 326
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLAPLAGLL------------------SRVPFrAGETTLLPapmfhatgwaHLTLaMALGSTV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 327 GYFRG-SIQGLTDDIKTLKPTVFPVVPRLLNRLydaitskvqqqgfmaklvynfafarkLSLVKAGKVGRDTIWDRLVFn 405
Cdd:PRK07788 277 VLRRRfDPEATLEDIAKHKATALVVVPVMLSRI--------------------------LDLGPEVLAKYDTSSLKIIF- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 406 kiqqqiggkvdlmVTGSA---PISSTVLEtcrvTLGTTIVEGYGQTECtALATFTWMGD----PSTGhcGAPAPCALVKL 478
Cdd:PRK07788 330 -------------VSGSAlspELATRALE----AFGPVLYNLYGSTEV-AFATIATPEDlaeaPGTV--GRPPKGVTVKI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 479 GDvpdlnyfaKDGK-------GEIRIKGPCVTKGYY--KDPERtaelfdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkL 549
Cdd:PRK07788 390 LD--------ENGNevprgvvGRIFVGNGFPFEGYTdgRDKQI------IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-V 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 17556552 550 AQGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEP------DVLKEW 598
Cdd:PRK07788 455 SGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFgqrLRAFVVKAPgaaldeDAIKDY 512
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
127-594 |
5.34e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 62.39 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 127 LTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIVDsfkkaesliknRENMPTLkn 206
Cdd:PRK07867 49 LDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTE-----------SAHAELL-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 207 iividsaDELKDGTAIIDtirVESL----TNALNLGSRYPFTNnlPKPDDNYIICYTSGTTGTPKGVMLTHSNIvanisg 282
Cdd:PRK07867 116 -------DGLDPGVRVIN---VDSPawadELAAHRDAEPPFRV--ADPDDLFMLIFTSGTSGDPKAVRCTHRKV------ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 283 flkilfAFQPSM------IDATQVHISYLPLSHMMEQLTHWTL-LGFGSKIGYFRG-SIQGLTDDIKTLKPTVFPVVPRL 354
Cdd:PRK07867 178 ------ASAGVMlaqrfgLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIALRRKfSASGFLPDVRRYGATYANYVGKP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 355 LNrlYDAITSKVQQQgfmaklvynfafarklslvkagkvgRDTIWdRLVF-NKiqqqiGGKVDlmvtgsapisstvLETC 433
Cdd:PRK07867 252 LS--YVLATPERPDD-------------------------ADNPL-RIVYgNE-----GAPGD-------------IARF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 434 RVTLGTTIVEGYGQTEcTALAtFTWMGDPSTGHCGAPAP------------CALVKLGDVPDLNyfAKDGKGE-IRIKGP 500
Cdd:PRK07867 286 ARRFGCVVVDGFGSTE-GGVA-ITRTPDTPPGALGPLPPgvaivdpdtgteCPPAEDADGRLLN--ADEAIGElVNTAGP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 501 CVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTI----RIIDRKKhifklAQGEYVAPEKIEQVYIRTPVVQQVYV- 575
Cdd:PRK07867 362 GGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAyfagRLGDWMR-----VDGENLGTAPIERILLRYPDATEVAVy 435
|
490 500
....*....|....*....|....*
gi 17556552 576 ---D---GDSlerwLIAVVVPEPDV 594
Cdd:PRK07867 436 avpDpvvGDQ----VMAALVLAPGA 456
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
419-570 |
6.51e-10 |
|
Eukaryotic 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. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 62.10 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 419 VTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDVPDlNYFAKDGKGEIRIK 498
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNG-NVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17556552 499 -GP----CVTKGYYKDPERTAELFDEEgFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVV 570
Cdd:cd05928 376 vKPirpfGLFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAV 450
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
438-594 |
1.15e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 61.25 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 438 GTTIVEGYGQTECTALATFT---WMGDPSTghCGAPAPCALVK-LGDvpDLNYFAKDGKGEI--RIKG-PCVTkgYYKDP 510
Cdd:PRK12406 296 GPVIYEYYGSTESGAVTFATsedALSHPGT--VGKAAPGAELRfVDE--DGRPLPQGEIGEIysRIAGnPDFT--YHNKP 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 511 ERTAELfDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQVYVDG--DS-LERWLIAV 587
Cdd:PRK12406 370 EKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipDAeFGEALMAV 447
|
....*..
gi 17556552 588 VVPEPDV 594
Cdd:PRK12406 448 VEPQPGA 454
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
105-645 |
2.76e-09 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 60.20 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVHefgLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:cd05968 92 LTYGELLYEVKRLANGLRA---LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 V-DSFKKAESLIKNREN-------MPTLKNIIVIDSAdelkdGTAIIDTiRVESLTNALNLGSRYPFTNNLpKPDDNYII 256
Cdd:cd05968 169 TaDGFTRRGREVNLKEEadkacaqCPTVEKVVVVRHL-----GNDFTPA-KGRDLSYDEEKETAGDGAERT-ESEDPLMI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 257 CYTSGTTGTPKGVMLTHsnivaniSGF-LKILF--AFQPSMIDATQVhISYLPLSHMMEQlthWTLLG---FGSKIGYFR 330
Cdd:cd05968 242 IYTSGTTGKPKGTVHVH-------AGFpLKAAQdmYFQFDLKPGDLL-TWFTDLGWMMGP---WLIFGgliLGATMVLYD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 331 GS--------IQGLTDDiktLKPTVFPVVPRLLNRLYDAITSKVQQQGfmaklvynfafarKLSLVKAGKVGRDtiWDRL 402
Cdd:cd05968 311 GApdhpkadrLWRMVED---HEITHLGLSPTLIRALKPRGDAPVNAHD-------------LSSLRVLGSTGEP--WNPE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 403 VFNKIQQQIGGkvdlmvtGSAPIsstvletCRVTLGTTIVEG-YGQTECTALAtftwmgdPSTGHCGAPAPCALVklgdV 481
Cdd:cd05968 373 PWNWLFETVGK-------GRNPI-------INYSGGTEISGGiLGNVLIKPIK-------PSSFNGPVPGMKADV----L 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 PDLNYFAKDGKGEIRIKGPCV--TKGYYKDPERTAELFDE--EGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAP 557
Cdd:cd05968 428 DESGKPARPEVGELVLLAPWPgmTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVA-GKRVGP 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 558 EKIEQVYIRTPVVQQVyvdgdslerwlIAVVVPEP---------DVLKEWNDKQGSGSRKIEEICNDEKAKEFVLSELHA 628
Cdd:cd05968 507 AEIESVLNAHPAVLES-----------AAIGVPHPvkgeaivcfVVLKPGVTPTEALAEELMERVADELGKPLSPERILF 575
|
570
....*....|....*..
gi 17556552 629 IGKANKLNSIEQVKKVI 645
Cdd:cd05968 576 VKDLPKTRNAKVMRRVI 592
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-602 |
4.59e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 101 DYEFLTYDDVHEQAKNLSMTLVhEFGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEI 180
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALI-ARGVGP--EVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGA 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIvdsfkkAESLIKNRENMPTLKNIIVIDSADELKDgtaiidtirvesltnalnlgsrYPFTNNLPKPD-DN--YIIc 257
Cdd:PRK12316 4650 ALLL------TQSHLLQRLPIPDGLASLALDRDEDWEG----------------------FPAHDPAVRLHpDNlaYVI- 4700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISGFLKilfAFQPSMIDatqvhiSYLPLSHMMEQLTHWTLLGfgskiGYFRGSIQGLT 337
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHGSLVNHLHATGE---RYELTPDD------RVLQFMSFSFDGSHEGLYH-----PLINGASVVIR 4766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 DDIKTLKPTVFPVVPRLLNRLYDAITSKVQQqgfmakLVYNFAFARKLSLVKAGKVGRDTIwdrlvfnkiqqqIGGKVDL 417
Cdd:PRK12316 4767 DDSLWDPERLYAEIHEHRVTVLVFPPVYLQQ------LAEHAERDGEPPSLRVYCFGGEAV------------AQASYDL 4828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 418 MVTGSAPISstvletcrvtlgttIVEGYGQTECTALATfTW------MGDPSTGHCGAPAPCALVKLGDVpDLNYFAKDG 491
Cdd:PRK12316 4829 AWRALKPVY--------------LFNGYGPTETTVTVL-LWkardgdACGAAYMPIGTPLGNRSGYVLDG-QLNPLPVGV 4892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 492 KGEIRIKGPCVTKGYYKDPERTAEL-----FDEEG--FLQTGDIGEMLPNGTIRIIDRKKHI-----FKLAQGEYVAPEK 559
Cdd:PRK12316 4893 AGELYLGGEGVARGYLERPALTAERfvpdpFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQvkirgFRIELGEIEARLR 4972
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 17556552 560 iEQVYIRTPVVqqVYVDGdSLERWLIAVVVPEPDVLKEWNDKQ 602
Cdd:PRK12316 4973 -EHPAVREAVV--IAQEG-AVGKQLVGYVVPQDPALADADEAQ 5011
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
493-575 |
5.06e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 59.11 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAeLFDEEGFLQTGDIGEMLpNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQ 572
Cdd:PRK09029 305 GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQ 381
|
...
gi 17556552 573 VYV 575
Cdd:PRK09029 382 VFV 384
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
493-570 |
5.91e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 59.23 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHifklaQ----GEYVAPEKIEQVYIRTP 568
Cdd:PRK10946 381 GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLRHP 455
|
..
gi 17556552 569 VV 570
Cdd:PRK10946 456 AV 457
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
103-594 |
1.21e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 58.16 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 103 EFLTYDDVHEQAKNLSmTLVHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFII--SQAEI 180
Cdd:PRK13391 23 EVVTYRELDERSNRLA-HLFRSLGLKRGDH--VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVddSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 181 SVVIVDSFKKAESLIKNrenMPTLKNIIVIDSADELKdgtaiidtiRVESLTNALnlgSRYPFTnnlPKPDDNY--IICY 258
Cdd:PRK13391 100 LITSAAKLDVARALLKQ---CPGVRHRLVLDGDGELE---------GFVGYAEAV---AGLPAT---PIADESLgtDMLY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 259 TSGTTGTPKGVM--LTHSNIVA--NISGFLKILFAFQPSMidatqVHISYLPLSHMMEQlthwtllgfgskigyfrgsiq 334
Cdd:PRK13391 162 SSGTTGRPKGIKrpLPEQPPDTplPLTAFLQRLWGFRSDM-----VYLSPAPLYHSAPQ--------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 335 gltddiktlkptvfpvvprllnrlydAITSKVQQQGFMAKLVYNFAFARKLSLVKAGKVGRD----TIWDRLVfnKIQQQ 410
Cdd:PRK13391 216 --------------------------RAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTqlvpTMFSRML--KLPEE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 411 IGGKVDL-----MVTGSAPISSTVLETCRVTLGTTIVEGYGQTE---CTALATFTWMGDPST-GHcgapapcalVKLGDV 481
Cdd:PRK13391 268 VRDKYDLsslevAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEglgFTACDSEEWLAHPGTvGR---------AMFGDL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 ----PDLNYFAKDGKGEIRIKG--PCVtkgYYKDPERTAELFDEEGFLQT-GDIGEMLPNGTIRIIDRKKHIFkLAQGEY 554
Cdd:PRK13391 339 hildDDGAELPPGEPGTIWFEGgrPFE---YLNDPAKTAEARHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMI-ISGGVN 414
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYVDG---DSLERWLIAVVVPEPDV 594
Cdd:PRK13391 415 IYPQEAENLLITHPKVADAAVFGvpnEDLGEEVKAVVQPVDGV 457
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
258-577 |
1.48e-08 |
|
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: 57.83 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISGflkiLFAFQPSMIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFR--GSIQG 335
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRALVLHSLA----ASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGprLDPAS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 336 LTDDIKTLKPTVFPVVPRLLNRLYDAitskvqqqgfmaklvynfafarklslvkagkvgRDTIwdrlvfnkiQQQIGGKV 415
Cdd:cd05915 236 LVELFDGEGVTFTAGVPTVWLALADY---------------------------------LEST---------GHRLKTLR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 416 DLMVTGSAPisSTVLETCRVTLGTTIVEGYGQTECTALATFT-WMGDPSTghcgAPAPCALvKLGDVPDLNYFAK----- 489
Cdd:cd05915 274 RLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETSPVVVQNfVKSHLES----LSEEEKL-TLKAKTGLPIPLVrlrva 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 490 ---------DGKG--EIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPE 558
Cdd:cd05915 347 deegrpvpkDGKAlgEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSV 425
|
330
....*....|....*....
gi 17556552 559 KIEQVYIRTPVVQQVYVDG 577
Cdd:cd05915 426 DLENALMGHPKVKEAAVVA 444
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
258-636 |
1.83e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 57.64 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVAN----ISGFLKILFAFQPSmiDATQVhiSYLPLSHMMeqlthwtllgfgskigyfrGSI 333
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANfeqlMSDYFGDTGGVPPP--DTTVV--SWLPFYHDM-------------------GLV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 334 QGLTDDIKTLKPTVF--PVV----P----RLLNRLYDAITSKVqqqgfmaklvyNFAF---ARKLSlvKAGKVGRDTiwd 400
Cdd:PRK05850 224 LGVCAPILGGCPAVLtsPVAflqrParwmQLLASNPHAFSAAP-----------NFAFelaVRKTS--DDDMAGLDL--- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 401 rlvfnkiqqqigGKVDLMVTGSAPISSTVLET-----CRVTLGTTIVE-GYGQTECTA-LATFTWMGDP----------S 463
Cdd:PRK05850 288 ------------GGVLGIISGSERVHPATLKRfadrfAPFNLRETAIRpSYGLAEATVyVATREPGQPPesvrfdyeklS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 464 TGH---CGAPAPCALVKLG----------DvPDLNYFAKDGK-GEIRIKGPCVTKGYYKDPERTAELFD----------E 519
Cdd:PRK05850 356 AGHakrCETGGGTPLVSYGsprsptvrivD-PDTCIECPAGTvGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtP 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 520 EG-FLQTGDIG-----EMLPNGTIR---IIDRKKHifklaqgeyvAPEKIE---QVYIRTPVVqQVYVDGDSLERwLIAV 587
Cdd:PRK05850 435 EGpWLRTGDLGfisegELFIVGRIKdllIVDGRNH----------YPDDIEatiQEITGGRVA-AISVPDDGTEK-LVAI 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 17556552 588 VvpEpdvLKEWNDKQGSGSRKIEEICNDekakefVLSelhAIGKANKLN 636
Cdd:PRK05850 503 I--E---LKKRGDSDEEAMDRLRTVKRE------VTS---AISKSHGLS 537
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
238-577 |
4.02e-08 |
|
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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 55.99 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 238 GSRYPFTN--NLPKPDDN-YIICYTSGTTGTPKGVMLThsnivanisgfLKILFAFQPSMIDATQVHisylplshmmEQL 314
Cdd:cd05973 72 GARLVVTDaaNRHKLDSDpFVMMFTSGTTGLPKGVPVP-----------LRALAAFGAYLRDAVDLR----------PED 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 315 THWTLLGFGSKIGYFRGSIQGLTDDIKTL---KPTVFPVVPRLLNRLydAITskvqqqgfmaklvyNFAfarklslvkag 391
Cdd:cd05973 131 SFWNAADPGWAYGLYYAITGPLALGHPTIlleGGFSVESTWRVIERL--GVT--------------NLA----------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 392 kvGRDTIWDRLVFNKIQQQIGGKVDLMVTGSA--PISSTVLETCRVTLGTTIVEGYGQTEC-TALATFTWMGDP-STGHC 467
Cdd:cd05973 184 --GSPTAYRLLMAAGAEVPARPKGRLRRVSSAgePLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPvHAGSA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 468 GAPAPCALVKLGDVpDLNYFAKDGKGEIRI---KGPCVT-KGYYKDPERTAelfdEEGFLQTGDIGEMLPNGTIRIIDRK 543
Cdd:cd05973 262 GRAMPGWRVAVLDD-DGDELGPGEPGRLAIdiaNSPLMWfRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRA 336
|
330 340 350
....*....|....*....|....*....|....
gi 17556552 544 KHIFKLAqGEYVAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:cd05973 337 DDVITMS-GYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
105-594 |
5.00e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 55.92 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvheFGLTPANTTNIGIYARNSPQWLVSAVAcveqsmvvvplYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK13382 69 LTWRELDERSDALAAAL---QALPIGEPRVVGIMCRNHRGFVEALLA-----------ANRIGADILLLNTSFAGPALAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSFKKAESLIKNRENMPTLkniiviDSA-DELKDGTAIID------TIRVESLTNAlNLGSRYPftnnlPKPDDNYIIC 257
Cdd:PRK13382 135 VVTREGVDTVIYDEEFSATV------DRAlADCPQATRIVAwtdedhDLTVEVLIAA-HAGQRPE-----PTGRKGRVIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANISGFLK--ILFAFQPSMIDATQVH---ISYLPLSHMMEqlthwtllgfGSKIGYFRGS 332
Cdd:PRK13382 203 LTSGTTGTPKGARRSGPGGIGTLKAILDrtPWRAEEPTVIVAPMFHawgFSQLVLAASLA----------CTIVTRRRFD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 333 IQGLTDDIKTLKPTVFPVVPRLLNRLYDAITSkvqqqgfmaklVYNFAFARKLSLVKAgkvgrdtiwdrlvfnkiqqqig 412
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDLPAE-----------VRNRYSGRSLRFAAA---------------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 413 gkvdlmvTGSaPISSTVLETCRVTLGTTIVEGYGQTECTALATFT---WMGDPSTGhcGAPAPCALVKLGDvPDLNYFAK 489
Cdd:PRK13382 320 -------SGS-RMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATpadLRAAPDTA--GRPAEGTEIRILD-QDFREVPT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 490 DGKGEIRIKGPCVTKGYykDPERTAELFDeeGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPV 569
Cdd:PRK13382 389 GEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPD 463
|
490 500
....*....|....*....|....*...
gi 17556552 570 VQQVYVDGDSLERW---LIAVVVPEPDV 594
Cdd:PRK13382 464 VAEAAVIGVDDEQYgqrLAAFVVLKPGA 491
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
254-592 |
6.94e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 55.56 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 254 YIIcYTSGTTGTPKGVMLTHSNIVANISGFLK--------ILFAFQPSMIDATQVHISylplshmMEQLTHWTLLGFGSK 325
Cdd:cd17654 122 YVI-HTSGTTGTPKIVAVPHKCILPNIQHFRSlfnitsedILFLTSPLTFDPSVVEIF-------LSLSSGATLLIVPTS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 326 IGYFRGSIQGLTDDIKtlKPTVFPVVPRLLNRlydaitskvqqqgFMAKLVYNFAFARKLSLvkagkvgrdtiwdRLvfn 405
Cdd:cd17654 194 VKVLPSKLADILFKRH--RITVLQATPTLFRR-------------FGSQSIKSTVLSATSSL-------------RV--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 406 kiqqqiggkvdLMVTGSAPISSTVLETCR-VTLGTTIVEGYGQTECTALATFTWMGD-PSTGHCGAPapcALVKLGDVPD 483
Cdd:cd17654 243 -----------LALGGEPFPSLVILSSWRgKGNRTRIFNIYGITEVSCWALAYKVPEeDSPVQLGSP---LLGTVIEVRD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 484 LNYFakDGKGEIRIKGpcVTKGYYKDPERTAELFDeegFLQTGDIGEmLPNGTIRIIDRKKHIFKLAqGEYVAPEKIEQV 563
Cdd:cd17654 309 QNGS--EGTGQVFLGG--LNRVCILDDEVTVPKGT---MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLIQQV 379
|
330 340
....*....|....*....|....*....
gi 17556552 564 YIRTPVVQQVYVDGDSLERwLIAVVVPEP 592
Cdd:cd17654 380 IESCLGVESCAVTLSDQQR-LIAFIVGES 407
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
105-591 |
7.79e-08 |
|
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: 55.17 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLvHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVi 184
Cdd:cd17656 14 LTYRELNERSNQLARFL-REKGVKKDSI--VAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSFKKAESLIKNREnmptlknIIVIDSADELKDGTAIIDTIRVEsltnalnlgsrypftnnlpkpDDNYIICYTSGTTG 264
Cdd:cd17656 90 LTQRHLKSKLSFNKS-------TILLEDPSISQEDTSNIDYINNS---------------------DDLLYIIYTSGTTG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVMLTHSNIVaNIsgflkILFAFQPSMIDATQVHISYLPLS-HMMEQLTHWTLLgfgskigyFRGSIQGLTDDIKTL 343
Cdd:cd17656 142 KPKGVQLEHKNMV-NL-----LHFEREKTNINFSDKVLQFATCSfDVCYQEIFSTLL--------SGGTLYIIREETKRD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 344 KPTVFPVVPRllNRLYDAI--TSKVQQQGFMAKLVYNFAFARKlSLVKAGkvgrdtiwDRLVFNKIQQQIGGKVDLMVTG 421
Cdd:cd17656 208 VEQLFDLVKR--HNIEVVFlpVAFLKFIFSEREFINRFPTCVK-HIITAG--------EQLVITNEFKEMLHEHNVHLHN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 422 S-APISSTVLETCRVTLGTTIVEgYGQTECTALATFTWMGDpstgHCGAPAPCALVklgdvpdlnyfakdgkGEIRIKGP 500
Cdd:cd17656 277 HyGPSETHVVTTYTINPEAEIPE-LPPIGKPISNTWIYILD----QEQQLQPQGIV----------------GELYISGA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 501 CVTKGYYKDPERTAELFDEEGF------LQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQ-- 572
Cdd:cd17656 336 SVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEav 414
|
490 500
....*....|....*....|
gi 17556552 573 VYVDGDSL-ERWLIAVVVPE 591
Cdd:cd17656 415 VLDKADDKgEKYLCAYFVME 434
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
106-594 |
1.07e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 55.10 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLVhEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:PRK07008 41 TYRDCERRAKQLAQALA-ALGVEPGD--RVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 D-SFKKAESLIKNRenMPTLKNIIVIDSADELKDGTaiIDTIRVESLTNALNlgSRYPFtnnlPKPDDNYI--ICYTSGT 262
Cdd:PRK07008 118 DlTFLPLVDALAPQ--CPNVKGWVAMTDAAHLPAGS--TPLLCYETLVGAQD--GDYDW----PRFDENQAssLCYTSGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 263 TGTPKGVMLTHSNIVanisgflkiLFAFQPSMIDAtqvhisyLPLSHMmeqlthwtllgfgskigyfrgsiqgltddikt 342
Cdd:PRK07008 188 TGNPKGALYSHRSTV---------LHAYGAALPDA-------MGLSAR-------------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 343 lkPTVFPVVPRL-LNRLydAITSKVQQQGfmAKLVYNfafARKL------SLVKAGKV----GRDTIWDRLV-------- 403
Cdd:PRK07008 220 --DAVLPVVPMFhVNAW--GLPYSAPLTG--AKLVLP---GPDLdgkslyELIEAERVtfsaGVPTVWLGLLnhmreagl 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 404 -FNKIQQQIGGkvdlmvtGSApISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHCGAPAPCALVKLGDV- 481
Cdd:PRK07008 291 rFSTLRRTVIG-------GSA-CPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPLDEQRKLLEKQGRVi 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 --PDLNYFAKDGK---------GEIRIKGPCVTKGYYKDpeRTAELFDeeGFLQTGDIGEMLPNGTIRIIDRKKHIFKlA 550
Cdd:PRK07008 363 ygVDMKIVGDDGRelpwdgkafGDLQVRGPWVIDRYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIK-S 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17556552 551 QGEYVAPEKIEQVYIRTPVVQQVYVDGDSLERWL---IAVVVPEPDV 594
Cdd:PRK07008 438 GGEWISSIDIENVAVAHPAVAEAACIACAHPKWDerpLLVVVKRPGA 484
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
258-594 |
1.64e-07 |
|
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: 54.31 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANIsgFLKILFAFQPSMiDATQVHISYLPLSHMMEQLT-HWTLLGFGSKIGYFRGSIQGL 336
Cdd:cd05929 132 YSGGTTGRPKGIKRGLPGGPPDN--DTLMAAALGFGP-GADSVYLSPAPLYHAAPFRWsMTALFMGGTLVLMEKFDPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 337 TDDIKTLKPTVFPVVPRLLNRlydaitskvqqqgfMAKLVYNFAFARKLSLVKAgkvgrdtiwdrlvfnkiqqqiggkvd 416
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVR--------------LLKLPEAVRNAYDLSSLKR-------------------------- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 417 lMVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFT---WMGDPstGHCGAPAPCALVKLGDvpDLNYFAKDGKG 493
Cdd:cd05929 249 -VIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINgeeWLTHP--GSVGRAVLGKVHILDE--DGNEVPPGEIG 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 494 EIRIKGPcVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTPVVQQV 573
Cdd:cd05929 324 EVYFANG-PGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDA 401
|
330 340
....*....|....*....|....
gi 17556552 574 YVDG---DSLERWLIAVVVPEPDV 594
Cdd:cd05929 402 AVVGvpdEELGQRVHAVVQPAPGA 425
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
105-604 |
2.04e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.78 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVhEFGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLI-ALGVGP--EVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 vdsfkkAESLIKNRENMPTLKNIIVIDSADELKDGtaiidtirvesltnalnlgsrYPFTNNLPKPDDN---YIIcYTSG 261
Cdd:PRK12467 1677 ------TQSHLQARLPLPDGLRSLVLDQEDDWLEG---------------------YSDSNPAVNLAPQnlaYVI-YTSG 1728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 262 TTGTPKGVMLTHSNIVANISGFLKilfAFQpsmIDATQVHISYLPLSHmmeQLTHWTLLG---FGSKIGYFRGSI----Q 334
Cdd:PRK12467 1729 STGRPKGAGNRHGALVNRLCATQE---AYQ---LSAADVVLQFTSFAF---DVSVWELFWpliNGARLVIAPPGAhrdpE 1799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 335 GLTDDIKTLKPTVFPVVPRLLNRLydaitskvqqqgfmaklvynfafarklsLVKAGKVGRDTIWDRLVFnkiqqqiGGK 414
Cdd:PRK12467 1800 QLIQLIERQQVTTLHFVPSMLQQL----------------------------LQMDEQVEHPLSLRRVVC-------GGE 1844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 415 VdLMVTGSAPisstVLEtcrvTLGTT-IVEGYGQTECTALATFtW---MGDPSTGHC---GAPapcalvklgdVPDLNYF 487
Cdd:PRK12467 1845 A-LEVEALRP----WLE----RLPDTgLFNLYGPTETAVDVTH-WtcrRKDLEGRDSvpiGQP----------IANLSTY 1904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 488 AKDGK---------GEIRIKGPCVTKGYYKDPERTAELFDEEGF-------LQTGDIGEMLPNGTIRIIDRKKHI----- 546
Cdd:PRK12467 1905 ILDASlnpvpigvaGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQvkirg 1984
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 17556552 547 FKLAQGEYVApEKIEQVYIRTPVVqqVYVDGDSlERWLIAVVVPEPDVLKEWNDKQGS 604
Cdd:PRK12467 1985 FRIELGEIEA-RLREQGGVREAVV--IAQDGAN-GKQLVAYVVPTDPGLVDDDEAQVA 2038
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
254-591 |
3.26e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.01 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 254 YIIcYTSGTTGTPKGVMLTHSNIV-------------ANISGFLKILFAFqpsmiDATQvhisylplshmmEQLtHWTLL 320
Cdd:PRK12467 3241 YVI-YTSGSTGKPKGVGVRHGALAnhlcwiaeayeldANDRVLLFMSFSF-----DGAQ------------ERF-LWTLI 3301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 321 GFGSKIgyFRGsiqgltddiktlkptvfpvvprllNRLYDAiTSKVQQQGFMAKLVYNFAFARKLSLVKAGKVGRdtiwd 400
Cdd:PRK12467 3302 CGGCLV--VRD------------------------NDLWDP-EELWQAIHAHRISIACFPPAYLQQFAEDAGGAD----- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 401 rlvfnkiqqqiGGKVDLMVTGSAPISSTVLETCRVTLG-TTIVEGYGQTECTAlaTFTWMGDPSTGHCGAPApcalVKLG 479
Cdd:PRK12467 3350 -----------CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVV--TVTLWKCGGDAVCEAPY----APIG 3412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 480 -DVPDLNYFAKDGK---------GEIRIKGPCVTKGYYKDPERTAELFDEEGFL-------QTGDIGEMLPNGTIRIIDR 542
Cdd:PRK12467 3413 rPVAGRSIYVLDGQlnpvpvgvaGELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIEYLGR 3492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17556552 543 KKHIFKLaQGEYVAPEKIEQVYIRTPVVQQ-VYVDGDSLE-RWLIAVVVPE 591
Cdd:PRK12467 3493 IDHQVKI-RGFRIELGEIEARLLQHPSVREaVVLARDGAGgKQLVAYVVPA 3542
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
105-592 |
6.78e-07 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 52.45 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSMTLVhEFGLTPANttNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK06155 47 WTYAEAARAAAAAAHALA-AAGVKRGD--RVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VDSfkkaesliknrenmPTLKNIIVIDSADELKDGTAIIDTIRVESLTNALNLGSRYPFTNNLP----KPDDNYIICYTS 260
Cdd:PRK06155 124 VEA--------------ALLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPaaavQPGDTAAILYTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 261 GTTGTPKGVMLTHSNIV---ANISGFLKIlfafqpsmiDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYF-RGSIQGL 336
Cdd:PRK06155 190 GTTGPSKGVCCPHAQFYwwgRNSAEDLEI---------GADDVLYTTLPLFHTNALNAFFQALLAGATYVLEpRFSASGF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 337 TDDIKTLKPTVFPVVprllnrlydaitskvqqqGFMAKLvynfafarklsLVKAGKVGRDTiwdrlvfnkiqqqiGGKVD 416
Cdd:PRK06155 261 WPAVRRHGATVTYLL------------------GAMVSI-----------LLSQPARESDR--------------AHRVR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 417 LMVTGSAPisSTVLETCRVTLGTTIVEGYGQTECTALATFTWmGDPSTGHCGAPAPCALVKLGD-----VPDlnyfakDG 491
Cdd:PRK06155 298 VALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTH-GSQRPGSMGRLAPGFEARVVDehdqeLPD------GE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 492 KGEI--RIKGP-CVTKGYYKDPERTAELFDEEGFlQTGDIGEMLPNGTIRIIDRKKHIFKlAQGEYVAPEKIEQVYIRTP 568
Cdd:PRK06155 369 PGELllRADEPfAFATGYFGMPEKTVEAWRNLWF-HTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHP 446
|
490 500
....*....|....*....|....*..
gi 17556552 569 VVQQ--VY-VDGDSLERWLIAVVVPEP 592
Cdd:PRK06155 447 AVAAaaVFpVPSELGEDEVMAAVVLRD 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
103-597 |
8.55e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 103 EFLTYDDVHEQAKNLSMTLVhEFGLTPanTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISV 182
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLI-ERGVGP--DVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQL 3157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 183 VIVDSFKKAESliknrenmptlkniividsadelKDGTAIIDTIRvesltNALNLGSRYPFTNNLPKpDDNYIIcYTSGT 262
Cdd:PRK12316 3158 LLSQSHLRLPL-----------------------AQGVQVLDLDR-----GDENYAEANPAIRTMPE-NLAYVI-YTSGS 3207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 263 TGTPKGVMLTHSNIVANISGFLkilfafQPSMIDATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYfrgSIQGLTDDIKT 342
Cdd:PRK12316 3208 TGKPKGVGIRHSALSNHLCWMQ------QAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL---AGPEDWRDPAL 3278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 343 LKPTVFPVVPRLLNRLYDAITSKVQQQGfmaklvynfafARKLSLVKAGKVGRDTIwdrlvfnkiqqqiggKVDLMVtgs 422
Cdd:PRK12316 3279 LVELINSEGVDVLHAYPSMLQAFLEEED-----------AHRCTSLKRIVCGGEAL---------------PADLQQ--- 3329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 423 apisstvletcRVTLGTTIVEGYGQTECTALATFTWMGDP--STGHCGAPAPCALVKLGDVpDLNYFAKDGKGEIRIKGP 500
Cdd:PRK12316 3330 -----------QVFAGLPLYNLYGPTEATITVTHWQCVEEgkDAVPIGRPIANRACYILDG-SLEPVPVGALGELYLGGE 3397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 501 CVTKGYYKDPERTAELFDEEGF------LQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVY 574
Cdd:PRK12316 3398 GLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAV 3476
|
490 500
....*....|....*....|....*....
gi 17556552 575 VDGDSLERwLIAVVVPE------PDVLKE 597
Cdd:PRK12316 3477 VLAVDGRQ-LVAYVVPEdeagdlREALKA 3504
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
250-565 |
2.45e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.58 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVANISGFLKIlfaFQPSMIDatqVHISYLPLSHMMeqlthwtllGFGSkigyf 329
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF---FSPKEDD---VMMSFLPPFHAY---------GFNS----- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 330 rgsiqgltddiktlkPTVFPVVprllnrlydaitskvqqQGFMAKLVYNFAFARKL-SLVKAGKV---GRDTIWDRLVFN 405
Cdd:PRK06334 242 ---------------CTLFPLL-----------------SGVPVVFAYNPLYPKKIvEMIDEAKVtflGSTPVFFDYILK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 406 KIQQQIGGKVDL---MVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDPSTGHC-GAPAPCALVKLgdV 481
Cdd:PRK06334 290 TAKKQESCLPSLrfvVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITINTVNSPKHESCvGMPIRGMDVLI--V 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 PDLNY--FAKDGKGEIRIKGPCVTKGYY-KDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEYVAPE 558
Cdd:PRK06334 368 SEETKvpVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLE 446
|
....*..
gi 17556552 559 KIEQVYI 565
Cdd:PRK06334 447 ALESILM 453
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
105-594 |
3.29e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 50.29 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 105 LTYDDVHEQAKNLSmTLVHEFGLTPANTtnIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVI 184
Cdd:PRK08276 12 VTYGELEARSNRLA-HGLRALGLREGDV--VAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 185 VdSFKKAESLIKNRENMPtlkniivIDSADELKDGTAIIDtirVESLTNALNLGSRYPFTNNLPKPDdnyiICYTSGTTG 264
Cdd:PRK08276 89 V-SAALADTAAELAAELP-------AGVPLLLVVAGPVPG---FRSYEEALAAQPDTPIADETAGAD----MLYSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 265 TPKGVM--LTHSNIVANISGFLKILFAFQPsmIDATQVHISYLPLSHMmeqlthwtllgfgskigyfrgsiqgltddikt 342
Cdd:PRK08276 154 RPKGIKrpLPGLDPDEAPGMMLALLGFGMY--GGPDSVYLSPAPLYHT-------------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 343 lKPTVFpvvprllnrlydaiTSKVQQQG----FMAKlvynFAFARKLSLVKAGKVGRD----TIWDRLVfnKIQQQIGGK 414
Cdd:PRK08276 200 -APLRF--------------GMSALALGgtvvVMEK----FDAEEALALIERYRVTHSqlvpTMFVRML--KLPEEVRAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 415 VDL-----MVTGSAPisstvletCRVTL--------GTTIVEGYGQTE---CTALATFTWMGDPstGHCGAPAPCALVKL 478
Cdd:PRK08276 259 YDVsslrvAIHAAAP--------CPVEVkramidwwGPIIHEYYASSEgggVTVITSEDWLAHP--GSVGKAVLGEVRIL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 479 GDvpDLNYFAKDGKGEIRIKGPCVTKGYYKDPERTAELFDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPE 558
Cdd:PRK08276 329 DE--DGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVNIYPQ 405
|
490 500 510
....*....|....*....|....*....|....*....
gi 17556552 559 KIEQVYIRTPVVQQVYVDGDSLERW---LIAVVVPEPDV 594
Cdd:PRK08276 406 EIENLLVTHPKVADVAVFGVPDEEMgerVKAVVQPADGA 444
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
250-577 |
5.86e-06 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 49.42 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 250 PDDNYIICYTSGTTGTPKGVMLTHSNIVAN-ISGflKILFAFQPSMIdatqvhisylplshmmeqltHWTllgfgskigy 328
Cdd:cd05969 88 PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYyFTG--KYVLDLHPDDI--------------------YWC---------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 329 frgsiqglTDDIKTLKPTVFPVVPRLLNrlydAITSKVQQQGFMAKLVYnfafarklSLVKAGKVgrdTIWD------RL 402
Cdd:cd05969 136 --------TADPGWVTGTVYGIWAPWLN----GVTNVVYEGRFDAESWY--------GIIERVKV---TVWYtaptaiRM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 403 VFnKIQQQIGGKVDL-----MVTGSAPISSTVLETCRVTLGTTIVEGYGQTECTALATFTWMGDP-STGHCGAPAPCALV 476
Cdd:cd05969 193 LM-KEGDELARKYDLsslrfIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPiKPGSMGKPLPGVKA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 477 KLGDvPDLNYFAKDGKGEIRIKG--PCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLAqGEY 554
Cdd:cd05969 272 AVVD-ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHR 348
|
330 340
....*....|....*....|...
gi 17556552 555 VAPEKIEQVYIRTPVVQQVYVDG 577
Cdd:cd05969 349 VGPFEVESALMEHPAVAEAGVIG 371
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
247-277 |
2.81e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 47.73 E-value: 2.81e-05
10 20 30
....*....|....*....|....*....|..
gi 17556552 247 LPKPDDN-YIIcYTSGTTGTPKGVMLTHSNIV 277
Cdd:PRK10252 594 LSQPHHTaYII-FTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
467-544 |
2.96e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 47.31 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 467 CGAPAPCALVKLGD-----VPDLnyfakdGKGEIRIKGPCVTKGYYKDPERTAELfDEEGFLQTGDIGEMLpNGTIRIID 541
Cdd:PRK09192 387 CGKALPGHEIEIRNeagmpLPER------VVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYLL-DGYLYITG 458
|
...
gi 17556552 542 RKK 544
Cdd:PRK09192 459 RAK 461
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
493-594 |
4.41e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.96 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 493 GEIRIKGPCVTKGYYKDPERTAELFDEEGFLQ------TGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIR 566
Cdd:PRK10252 803 GDLYLTGIQLAQGYLGRPDLTASRFIADPFAPgermyrTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQA 881
|
90 100 110
....*....|....*....|....*....|....*....
gi 17556552 567 TPVVQQVYV-----------DGDslERWLIAVVVPEPDV 594
Cdd:PRK10252 882 LPDVEQAVThacvinqaaatGGD--ARQLVGYLVSQSGL 918
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
258-545 |
6.65e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 46.26 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 258 YTSGTTGTPKGVMLTHSNIVANIsgfLKILFAFQPSMIDATqvhISYLPLSHMMEQLThwtlLGFGSKIGYFrgsiqglt 337
Cdd:PRK07769 187 YTSGSTRIPAGVQITHLNLPTNV---LQVIDALEGQEGDRG---VSWLPFFHDMGLIT----VLLPALLGHY-------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 338 ddIKTLKPTVFPVVP-RLLNRLydAITSKVQQQGFMAklVYNFAF--ARKLSLVKAGKVGRDTiwdrlvfnkiqqqigGK 414
Cdd:PRK07769 249 --ITFMSPAAFVRRPgRWIREL--ARKPGGTGGTFSA--APNFAFehAAARGLPKDGEPPLDL---------------SN 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 415 VDLMVTGSAPISSTVLETCRVTLG------TTIVEGYGQTECTALATFTWMGD-PSTGHC---------------GAPAP 472
Cdd:PRK07769 308 VKGLLNGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATLFVSTTPMDEePTVIYVdrdelnagrfvevpaDAPNA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 473 CALVKLGDV----------PDLNYFAKDGK-GEIRIKGPCVTKGYYKDPERTAELF-----------------DEEGFLQ 524
Cdd:PRK07769 388 VAQVSAGKVgvsewavivdPETASELPDGQiGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVR 467
|
330 340
....*....|....*....|....*....
gi 17556552 525 TGDIG-----EMLPNGTIR---IIDRKKH 545
Cdd:PRK07769 468 TGDYGvyfdgELYITGRVKdlvIIDGRNH 496
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
106-273 |
2.03e-04 |
|
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: 44.49 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 106 TYDDVHEQAKNLSMTLVhefGLTPANTTNIGIYARNSPQWLVSAVACVEQSMVVVPLYDTLGAEAATFIISQAEISVVIV 185
Cdd:cd17634 86 SYRELHREVCRFAGTLL---DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 186 -DSFKKAESLIKNRENM--------PTLKNIIVIDSADELKDGT--------AIIDTIRVESLTNALNlgsrypftnnlp 248
Cdd:cd17634 163 aDGGVRAGRSVPLKKNVddalnpnvTSVEHVIVLKRTGSDIDWQegrdlwwrDLIAKASPEHQPEAMN------------ 230
|
170 180
....*....|....*....|....*
gi 17556552 249 kPDDNYIICYTSGTTGTPKGVMLTH 273
Cdd:cd17634 231 -AEDPLFILYTSGTTGKPKGVLHTT 254
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
254-570 |
3.12e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 43.96 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 254 YIIcYTSGTTGTPKGVMLTH-SNIVAnisgflkiLFAFQPSMI--DATQVHISYLPLSHMMEQLTHWTLLGFGSKIGYFR 330
Cdd:PTZ00237 258 YIL-YTSGTTGNSKAVVRSNgPHLVG--------LKYYWRSIIekDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 331 GSI---QGLTDDI-KTL---KPTVFPVVPRLLNRLYdaitsKVQQQGFMAKLVYNfafarkLSLVKagkvgrdTIWdrlv 403
Cdd:PTZ00237 329 GGIiknKHIEDDLwNTIekhKVTHTLTLPKTIRYLI-----KTDPEATIIRSKYD------LSNLK-------EIW---- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 404 fnkiqqqiggkvdlmvTGSAPISSTVLETCRVTLGTTIVEGYGQTE--CTALATFTWMGDPSTGhCGAPAPcaLVKlgdv 481
Cdd:PTZ00237 387 ----------------CGGEVIEESIPEYIENKLKIKSSRGYGQTEigITYLYCYGHINIPYNA-TGVPSI--FIK---- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 482 PDLnyFAKDGK-------GEIRIK---GPCVTKGYYKDPERTAELFDE-EGFLQTGDIGEMLPNGTIRIIDRKKHIFKLA 550
Cdd:PTZ00237 444 PSI--LSEDGKelnvneiGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKIS 521
|
330 340
....*....|....*....|
gi 17556552 551 qGEYVAPEKIEQVYIRTPVV 570
Cdd:PTZ00237 522 -GNKVQLNTIETSILKHPLV 540
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
438-593 |
3.25e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 43.86 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 438 GTTIVEGYGQTECTALATFtwmgDPST--GHCGAPAP------------CALVKL---GDVpdLNyfAKDGKGEI-RIKG 499
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVR----EPGTppGSIGRGAPgvaiynpetlteCAVARFdahGAL--LN--ADEAIGELvNTAG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 500 PCVTKGYYKDPERTAELFdEEGFLQTGDIGEMLPNGTIRIIDRKKHIFKLaQGEYVAPEKIEQVYIRTPVVQQVYV---- 575
Cdd:PRK13388 360 AGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVyavp 437
|
170
....*....|....*...
gi 17556552 576 DGDSLERWLIAVVVPEPD 593
Cdd:PRK13388 438 DERVGDQVMAALVLRDGA 455
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
228-327 |
4.52e-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: 43.43 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 228 VESLTNALNLGSRYPFTNNLP---KPDDNYIICYTSGTTGTPKGVMLTHSNIVAnISGFLkilfafqpSMIDATQVHISY 304
Cdd:cd05938 118 VISLLDKVDAASDEPVPASLRahvTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL--------SLCGVTADDVIY 188
|
90 100
....*....|....*....|....*
gi 17556552 305 --LPLSHMMEqlthwTLLGFGSKIG 327
Cdd:cd05938 189 itLPLYHSSG-----FLLGIGGCIE 208
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
489-583 |
3.18e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 40.53 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 489 KDGKGEIRIKGPCVTKGYYKDPERTAELfDEEGFLQTGDIGEMLPNGTIRIIDRKKHIFkLAQGEYVAPEKIEQVYIRTP 568
Cdd:PRK07638 330 KGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHP 407
|
90
....*....|....*
gi 17556552 569 VVQQVYVDGDSLERW 583
Cdd:PRK07638 408 AVDEIVVIGVPDSYW 422
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
198-273 |
8.76e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 39.39 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17556552 198 RENMPTLKNIIVIDSADELKDGTAIIDTIRVESLTNALNLGS----RYPFtnnlpkpDDNYIICYTSGTTGTPK------ 267
Cdd:PRK03584 213 RAALPSLEHVVVVPYLGPAAAAAALPGALLWEDFLAPAEAAElefePVPF-------DHPLWILYSSGTTGLPKcivhgh 285
|
....*..
gi 17556552 268 -GVMLTH 273
Cdd:PRK03584 286 gGILLEH 292
|
|
| |
