|
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 ... |
117-661 |
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: 876.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 117 QPYEWISYKQ----------------------------------WVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAEL 162
Cdd:cd05927 1 GPYEWISYKEvaeradnigsalrslggkpapasfvgiysinrpeWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 163 SVIFADKpekaklllegvenkltpclkiivimdsydndlvergqkcGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICF 242
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 243 TSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDL 322
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 323 KVLQPTIFPVVPRLLNRMFDRIFG--QANTSVKRWLLDFASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMIT 400
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 401 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAA--KGEGEVCVK 478
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 479 GANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 558
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 559 SLQAFLIAIVVPDVEILPSWA-QKRGFQGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLL 637
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1958682904 638 TPTLKAKRPELRNYFRSQIDELYS 661
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
87-663 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 659.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 87 YDDVRTMYDGFQRGIQVSNDGPCLGSRKPNQ----PYEWISY--------------------------------KQWVTI 130
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYgeagtartaigsglvqhgipkgacvglyfinrPEWLIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 131 EQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFAdKPEKAKLLLEGVENklTPCLKIIVIMDSYDNDLVERGQKCGV 210
Cdd:PLN02736 120 DHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGTGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 211 EIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLPLA 290
Cdd:PLN02736 197 EIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLPLA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 291 HMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--VKRWLLDFASKRKEAEL 368
Cdd:PLN02736 273 HIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLFNAAYNAKKQAL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 369 RSGivRNNS-LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSL--PGDWTAG 445
Cdd:PLN02736 353 ENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 446 HVGAPMPCNYIKLVDVEDMNYQAAKG---EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 522
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 523 KKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEELCRNKDINKAI 601
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 602 LEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTI 663
Cdd:PLN02736 589 LADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
87-661 |
5.13e-164 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 483.45 E-value: 5.13e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 87 YDDVRTMYDGFQRGIQVSNDGPCLgSRKPNQPYEWISYKQ--------------------------------WVTIEQGC 134
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEfaervralaagllalgvkpgdrvailsdnrpeWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 135 FTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEGVENklTPCLKIIVIMDsydndlvERGQKCGVEIIG 214
Cdd:COG1022 86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 215 LKALEDLGRvNRTKPKPPE-------PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCsgfiKATESAFIASPEDVLISFL 287
Cdd:COG1022 157 LDELLALGR-EVADPAELEarraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNA----RALLERLPLGPGDRTLSFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 288 PLAHMFETVVECVMLCHGAKIGFfQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--VKRWLLDFA---SK 362
Cdd:COG1022 232 PLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 363 RKEAELRSGivRNNSLW--------DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGC 434
Cdd:COG1022 311 RYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 435 CLSLPGDWTAGHVGAPMPCNYIKLVDvedmnyqaakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPN 514
Cdd:COG1022 388 TVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 515 GTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEELCR 593
Cdd:COG1022 457 GFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQ 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 594 NKDINKAILEDMVKLgkNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYS 661
Cdd:COG1022 536 DPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
127-648 |
1.11e-154 |
|
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: 454.36 E-value: 1.11e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 127 WVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEkaklllegvenkltpclkiivimdsydndlvergq 206
Cdd:cd05907 43 WTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVEDPD----------------------------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 207 kcgveiiglkaledlgrvnrtkpkppepeDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISF 286
Cdd:cd05907 88 -----------------------------DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 287 LPLAHMFETV-VECVMLCHGAKIGFFQgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLDFASkrke 365
Cdd:cd05907 135 LPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 366 aelrsgivrnnslwdklifhkiqsslGGKVRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAG 445
Cdd:cd05907 210 --------------------------GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 446 HVGAPMPCNYIKLVDvedmnyqaakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKH 525
Cdd:cd05907 263 TVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 526 IFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQAFLIAIVVPDVEILPSWAQKRG-FQGSFEELCRNKDINKAILED 604
Cdd:cd05907 332 LIITSGGKNISPEPIENALKASPLISQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAA 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1958682904 605 MVKLgkNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPEL 648
Cdd:cd05907 411 VEAA--NARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
88-664 |
2.45e-145 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 437.92 E-value: 2.45e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 88 DDVRTMYDGFQRGIQVSNDGPCLGSR-----KPNQpYEWISYKQ--------------------------------WVTI 130
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEvydiviklgnslrsvgvkdeakcgiyganspeWIIS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 131 EQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKpEKAKLLLEGVENKlTPCLKIIVIMDSYDNDLVERGQKCGV 210
Cdd:PLN02614 121 MEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETFGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 211 EIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIA-SPEDVLISFLPL 289
Cdd:PLN02614 199 VIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVYLSYLPL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 290 AHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQANTS----VKRWLLDFASKRKE 365
Cdd:PLN02614 279 AHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGL--QKKLSdggfLKKFVFDSAFSYKF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 366 AELRSGI--VRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDW- 442
Cdd:PLN02614 357 GNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELd 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 443 TAGHVGAPMPCNYIKLVDVEDMNYQA--AKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKII 520
Cdd:PLN02614 437 MLGTVGPPVPNVDIRLESVPEMEYDAlaSTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKII 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 521 DRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQGSFEELCRNKDINKA 600
Cdd:PLN02614 516 DRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEF 595
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958682904 601 ILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTIK 664
Cdd:PLN02614 596 ILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
105-664 |
3.04e-145 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 437.35 E-value: 3.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 105 NDGPCLGSRKPNQPyewisykQWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLleGVENKL 184
Cdd:PLN02861 100 NPGDRCGIYGSNCP-------EWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKC 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 185 TPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPkPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDC 264
Cdd:PLN02861 171 SSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 265 ---SGFIKATESAfiASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLlnrmF 341
Cdd:PLN02861 250 lstDHLLKVTDRV--ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----Y 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 342 DRIFG------QANTSVKRWLLDFASKRKEAELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFL 413
Cdd:PLN02861 324 DRIYTgimqkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 414 RAALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYIKLVDVEDMNYQAAKG--EGEVCVKGANVFKGYLKDP 490
Cdd:PLN02861 404 RVTSCSVLSQGYGLTESCGGCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQ 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 491 ARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVP 570
Cdd:PLN02861 484 DLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVP 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 571 DVEILPSWAQKRGFQGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRN 650
Cdd:PLN02861 563 DRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLK 642
|
570
....*....|....
gi 1958682904 651 YFRSQIDELYSTIK 664
Cdd:PLN02861 643 YYKDCIDQLYSEAK 656
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
118-645 |
5.04e-144 |
|
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: 428.94 E-value: 5.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 118 PYEWISYKQ--------------------------------WVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVI 165
Cdd:cd17639 2 EYKYMSYAEvwervlnfgrglvelglkpgdkvaifaetraeWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 166 FADkpekaklllegvenkltpclkiivimdsydndlvergqkcgveiiglkaledlgrvnrtkpkpPEPEDLAIICFTSG 245
Cdd:cd17639 82 FTD---------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 246 TTGNPKGAMVTHQNIMNDCSGFIKATeSAFIaSPEDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMD----- 320
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRV-PELL-GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrg 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 321 ---DLKVLQPTIFPVVPRLLNRMFDRIFGQANT--SVKRWLLDFASKRKEAELRSGIvrNNSLWDKLIFHKIQSSLGGKV 395
Cdd:cd17639 175 ckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGGRL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 396 RLMITGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGE--G 473
Cdd:cd17639 253 RYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPprG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 474 EVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQV 553
Cdd:cd17639 332 EILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNI 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 554 FVHGESLQAFLIAIVVPDVEILPSWAQKRGF-QGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSI 632
Cdd:cd17639 412 CVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTP 491
|
570
....*....|...
gi 1958682904 633 DNGLLTPTLKAKR 645
Cdd:cd17639 492 ENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
89-663 |
1.17e-140 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 425.77 E-value: 1.17e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 89 DVRTMYDGFQRGIQVSNDGPCLGSRKPNQ----PYEWISYK--------------------------------QWVTIEQ 132
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKevyeevlqigsalrasgaepgsrvgiygsncpQWIVAME 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 133 GCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFA-DKpeKAKLLLEGvENKLTPCLKIIVIMDSYDNDLVERGQKCGVE 211
Cdd:PLN02430 120 ACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIGVK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 212 IIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSG---FIKATESAFiaSPEDVLISFLP 288
Cdd:PLN02430 197 TYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSFLP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 289 LAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTSVKRWLLDFASKRKEA 366
Cdd:PLN02430 275 LAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 367 ELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTA 444
Cdd:PLN02430 355 WMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCM 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 445 -GHVGAPMPCNYIKLVDVEDMNYQAAkGE---GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKII 520
Cdd:PLN02430 435 lGTVGAPAVYNELRLEEVPEMGYDPL-GEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKII 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 521 DRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQGSFEELCRNKDINKA 600
Cdd:PLN02430 513 DRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEH 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 601 ILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYSTI 663
Cdd:PLN02430 593 ILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
118-661 |
6.61e-120 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 372.91 E-value: 6.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 118 PYEWISYKQ--------------------------------WVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVI 165
Cdd:PLN02387 103 EYEWITYGQvfervcnfasglvalghnkeervaifadtraeWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 166 FADKPEKAKLLleGVENKLTPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSG 245
Cdd:PLN02387 183 ICDSKQLKKLI--DISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 246 TTGNPKGAMVTHQNIMndcsgfikATESAFIA-----SPEDVLISFLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMD 320
Cdd:PLN02387 261 STGLPKGVMMTHGNIV--------ATVAGVMTvvpklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 321 -----------DLKVLQPTIFPVVPRLLNRMFDRIFGQANTS---VKRwLLDFASKRKEAELR------SGIVRnnSLWD 380
Cdd:PLN02387 331 tsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKgglAKK-LFDIAYKRRLAAIEgswfgaWGLEK--LLWD 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 381 KLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVD 460
Cdd:PLN02387 408 ALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVS 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 VEDMNYQAAKG---EGEVCVKGANVFKGYLKDPARTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGE 533
Cdd:PLN02387 488 WEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 534 YIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEELCRNKDINKAILEDMVKLGKNA 612
Cdd:PLN02387 568 YVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAA 647
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1958682904 613 GLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYS 661
Cdd:PLN02387 648 RLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
126-530 |
4.07e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.22 E-value: 4.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 126 QWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIVIMDSydndlverg 205
Cdd:pfam00501 58 EWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDP--------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 206 qkcGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLIS 285
Cdd:pfam00501 129 ---VLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 286 FLPLAHMFETVVEC-VMLCHGAKIGFFQGDIRL----LMDDLKVLQPTIFPVVPRLLNRMFDrifgqantsvkrwlldfa 360
Cdd:pfam00501 206 TLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------------------ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 361 SKRKEAELRSGivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPG 440
Cdd:pfam00501 268 AGAPKRALLSS-----------------------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 441 DW---TAGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTL 517
Cdd:pfam00501 325 DEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYL 404
|
410
....*....|...
gi 1958682904 518 KIIDRKKHIFKLA 530
Cdd:pfam00501 405 EIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
63-660 |
1.66e-94 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 306.52 E-value: 1.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 63 EVTGTTEGVRRsaVLEddkllLYYYDDVRTM-YD-------GFQRGIQVsndgpcLGSRKPNQP--YE---WisykQWVT 129
Cdd:PTZ00216 99 EVVKDADGKER--TME-----VTHFNETRYItYAelwerivNFGRGLAE------LGLTKGSNVaiYEetrW----EWLA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 130 IEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKpEKAKLLLEGVENKLTPCLKIIvimdsYDNDLVERGQKCG 209
Cdd:PTZ00216 162 SIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNG-KNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 210 VEIIGLKALEDLGRVNRTKPKPPEPE---DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGF-IKATESAFIASPEDVLIS 285
Cdd:PTZ00216 236 CRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCS 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 286 FLPLAHMFETVVECVMLCHGAKIGFfqGDIRLLMD-------DLKVLQPTIFPVVPRLlnrmFDRI----------FGqa 348
Cdd:PTZ00216 316 YLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG-- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 349 ntSVKRWLLDFASKRKEAELRSGivRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCqFYEGYGQT 428
Cdd:PTZ00216 388 --SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLT 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 429 ECTagCC--LSLPGDWTAGHVGAPMPCNYIKLVDVEDMNY-QAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHT 505
Cdd:PTZ00216 463 ETV--CCggIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHtDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHT 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 506 GDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQ----VFVHgeSLQAFLIAIVVPDVEILPSWAQK 581
Cdd:PTZ00216 541 GDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKE 618
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958682904 582 RGFQGSFEELCRNKDINKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELY 660
Cdd:PTZ00216 619 HGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
234-646 |
6.97e-83 |
|
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: 269.23 E-value: 6.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikateSAFI-ASPEDVLISFLPLAHMFETVVECVMLCHGAKIGFfq 312
Cdd:cd17640 87 SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSL-----SDIVpPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 313 GDIRLLMDDLKVLQPTIFPVVPRLlnrmfdrifgqantsvkrWlldfaskrkEAeLRSGI---VRNNSLWDKLIFHKIQS 389
Cdd:cd17640 160 TSIRTLKDDLKRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 slGGKVRLMITGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAA 469
Cdd:cd17640 212 --GGIFKFGISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 470 KGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEA 549
Cdd:cd17640 289 GEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 550 VAQVFVHGESlQAFLIAIVVPDVEILPSWAQKRG--FQGSFEELCRNKDINKAI-LEDMVKLGKNAGLKPFEQVKGIAVH 626
Cdd:cd17640 369 IEQIMVVGQD-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALL 447
|
410 420
....*....|....*....|
gi 1958682904 627 PELFsIDNGLLTPTLKAKRP 646
Cdd:cd17640 448 EEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
126-645 |
2.23e-75 |
|
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: 250.85 E-value: 2.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 126 QWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADK----PEKAKLLLEGVENKLTPCLKIIVIMDSYDnDL 201
Cdd:cd05932 43 EWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKlddwKAMAPGVPEGLISISLPPPSAANCQYQWD-DL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 202 VERGQkcgveiiglkALEDlgrvnrtKPkPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesaFIASPED 281
Cdd:cd05932 122 IAQHP----------PLEE-------RP-TRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEH----IGTEEND 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 282 VLISFLPLAHMFETV-VECVMLCHGAKIgFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLDFa 360
Cdd:cd05932 180 RMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQKLNLLLKI- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 361 skrkeaelrsgivrnnSLWDKLIFHKIQSSLG-GKVRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLP 439
Cdd:cd05932 258 ----------------PVVNSLVKRKVLKGLGlDQCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 440 GDWTAGHVGAPMPCNYIKLVDvedmnyqaakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKI 519
Cdd:cd05932 321 GRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 520 IDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAIVVPDVEILPSwaQKRGFQGSFEELCRnkdink 599
Cdd:cd05932 390 TGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA-PLALVVLSEEARLR--ADAFARAELEASLR------ 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958682904 600 AILEDMvklgkNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKR 645
Cdd:cd05932 461 AHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
236-570 |
2.81e-65 |
|
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: 218.31 E-value: 2.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAKI----GFF 311
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 QGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantsvkrwlldfasKRKEAELRSgivrnnslwdklifhkiqssl 391
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 392 ggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWT--AGHVGAPMPCNYIKLVDVEDmNYQAA 469
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 470 KGEGEVCVKGANVFKGYLKDPARTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEA 549
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340
....*....|....*....|....
gi 1958682904 550 VAQVFVHG---ESLQAFLIAIVVP 570
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVL 293
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
238-582 |
7.27e-65 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 220.84 E-value: 7.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 238 AIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHMFETVVECVM-LCHGAKI----GFfq 312
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllpRF-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 313 gDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqantsvkrwlldfaSKRKEAELRSgivrnnslwdklifhkiqsslg 392
Cdd:COG0318 177 -DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS---------------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 393 gkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAPMPCNYIKLVDvEDMNYQAAK 470
Cdd:COG0318 217 --LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 471 GEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 550
Cdd:COG0318 294 EVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGV 371
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958682904 551 AQVFV-------HGESLQAFLI--AIVVPDVEILPSWAQKR 582
Cdd:COG0318 372 AEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
224-645 |
1.81e-62 |
|
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: 215.00 E-value: 1.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 224 VNRTKPK---PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfIKATEsafIASPEDVLISFLPLAHMFETVVECV 300
Cdd:cd05914 75 LNHSEAKaifVSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDG-VKEVV---LLGKGDKILSILPLHHIYPLTFTLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 301 M-LCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLdfaskrkeaeLRSGIVRNNSLW 379
Cdd:cd05914 151 LpLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK----------FKLAKKINNRKI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 380 DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPmpcnyIKLV 459
Cdd:cd05914 221 RKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 460 DVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEK 539
Cdd:cd05914 295 EVRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 540 IENIYLRSEAVAQ--VFV-HGEslqafLIAIVVPDVEILPSWAQKrgfqgsfeelcrNKDINKAILEDMVKlGKNAGLKP 616
Cdd:cd05914 375 IEAKINNMPFVLEslVVVqEKK-----LVALAYIDPDFLDVKALK------------QRNIIDAIKWEVRD-KVNQKVPN 436
|
410 420
....*....|....*....|....*....
gi 1958682904 617 FEQVKGIAVHPELFSidnglLTPTLKAKR 645
Cdd:cd05914 437 YKKISKVKIVKEEFE-----KTPKGKIKR 460
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
140-660 |
4.08e-62 |
|
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: 217.22 E-value: 4.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEgVENKLtPCLKIIVImdsYDNDLVERGQKcgveIIGLKALE 219
Cdd:cd05933 59 IAVGIYTTNSPEACQYVAETSEANILVVENQKQLQKILQ-IQDKL-PHLKAIIQ---YKEPLKEKEPN----LYSWDEFM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 220 DLGRvnrtkpKPPEPEDLAII-------C----FTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLP 288
Cdd:cd05933 130 ELGR------SIPDEQLDAIIssqkpnqCctliYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 289 LAHMFETVVEcVMLC--HGAKIGFFQGDIR--LLMDDLKVLQPTIFPVVPRLLNRMFDRI--FGQANTSVKRWLLDFAsK 362
Cdd:cd05933 204 LSHIAAQILD-IWLPikVGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-K 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 363 RKEAE-------LRSGIVRNNSLWDKLIFHKIQSSLG-GKVRLMITGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGC 434
Cdd:cd05933 282 GVGLEtnlklmgGESPSPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 435 CLSLPGDWTAGHVGAPMPCNYIKLVDvedmnyQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPN 514
Cdd:cd05933 361 TISNPQAYRLLSCGKALPGCKTKIHN------PDADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDED 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 515 GTLKIIDRKKHIFKLAQGEYIAPEKIEN-IYLRSEAVAQVFVHGESLQaFLIAIVVPDVEILP--------------SWA 579
Cdd:cd05933 435 GFLYITGRIKELIITAGGENVPPVPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTLKCEVNPetgepldelteeaiEFC 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 580 QKRGFQGS-FEELCRNKD--INKAILEDMVKLGKNAGLKPfEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQI 656
Cdd:cd05933 514 RKLGSQATrVSEIAGGKDpkVYEAIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEI 592
|
....
gi 1958682904 657 DELY 660
Cdd:cd05933 593 DKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
86-645 |
3.42e-61 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 214.21 E-value: 3.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 86 YYDDVRTMYDGFQR-GIQVSNDGPCLGSRKPnqpyEWIsykqWVTI-EQGCFTYSMvvvPLYDTLGTDAITYIVNKAELS 163
Cdd:cd17641 17 YADRVRAFALGLLAlGVGRGDVVAILGDNRP----EWV----WAELaAQAIGALSL---GIYQDSMAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 164 VIFADKPEKAKLLLEgVENKLTPCLKIIVI----MDSYDN-------DLVERGQKCGVEIIGLkaLEDlgRVNRTKPkpp 232
Cdd:cd17641 86 VVIAEDEEQVDKLLE-IADRIPSVRYVIYCdprgMRKYDDprlisfeDVVALGRALDRRDPGL--YER--EVAAGKG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 epEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLPLAHMFETVVECVM-LCHGAKIGFF 311
Cdd:cd17641 158 --EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 QgDIRLLMDDLKVLQPTIFPVVPRLLNRM--FDRIFGQANTSVKRWLLDF--------ASKRKEAELRSGIVRNNS-LWD 380
Cdd:cd17641 232 E-EPETMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 381 KLIFHKIQSSLG-GKVRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLV 459
Cdd:cd17641 311 ALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 460 DVedmnyqaakgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEK 539
Cdd:cd17641 390 EV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 540 IEN-----IYLRsEAVaqVFVHGeslQAFLIAIVVPDVEILPSWAQKRGFQ-GSFEELCRNKDINKAILEDMVKLgkNAG 613
Cdd:cd17641 459 IENklkfsPYIA-EAV--VLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKV--NAS 530
|
570 580 590
....*....|....*....|....*....|..
gi 1958682904 614 LKPFEQVKGIAVHPELFSIDNGLLTPTLKAKR 645
Cdd:cd17641 531 LPEAQRIRRFLLLYKELDADDGELTRTRKVRR 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
127-638 |
2.86e-60 |
|
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: 211.93 E-value: 2.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 127 WVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADkPEKAKLLLEGVENKLTPclKIIVIMDSYDNDLVER-- 204
Cdd:cd17632 106 YATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS-AEHLDLAVEAVLEGGTP--PRLVVFDHRPEVDAHRaa 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 205 ---------GQKCGVEIIGLKALEDLGrVNRTKPKPPEPED--LAIICFTSGTTGNPKGAMVTHQNIMN---DCSGFIKA 270
Cdd:cd17632 183 lesarerlaAVGIPVTTLTLIAVRGRD-LPPAPLFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLVATfwlKVSSIQDI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 271 TEsafiasPEDVLISFLPLAHMFETVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQA 348
Cdd:cd17632 262 RP------PASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRY--QA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 349 ntSVKRWLLDFA-----SKRKEAELRsgivrnnslwdklifhkiQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYE 423
Cdd:cd17632 333 --ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 424 GYGQTEctAGCCLSLpgdwtaGHVGAPMPCNYiKLVDVEDMNYQAAKG---EGEVCVKGANVFKGYLKDPARTAEALDKD 500
Cdd:cd17632 393 GYGSTE--AGAVILD------GVIVRPPVLDY-KLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDED 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 501 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPdveilpswAQ 580
Cdd:cd17632 464 GFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVP--------TQ 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 581 KRGFQGSFEELcrnkdiNKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLT 638
Cdd:cd17632 536 DALAGEDTARL------RAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
208-570 |
2.98e-57 |
|
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: 200.87 E-value: 2.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 208 CGVE-IIGLKALEDLGRVNRTKPKPPE--PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFiaSPEDVLI 284
Cdd:cd05936 95 SGAKaLIVAVSFTDLLAAGAPLGERVAltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 285 SFLPLAHMF-ETVVECVMLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantsvkrwlldfASK 362
Cdd:cd05936 173 AALPLFHVFgLTVALLLPLALGATIVLIPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 363 RKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLSLPGD 441
Cdd:cd05936 236 FKKRDFSS------------------------LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 442 WTAGHVGAPMPCNYIKLVDVEDMnyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKII 520
Cdd:cd05936 292 RKPGSIGIPLPGTEVKIVDDDGE--ELPPGEvGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIV 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682904 521 DRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFliaiVVP 570
Cdd:cd05936 369 DRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAF----VVL 420
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
140-558 |
2.11e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 194.25 E-value: 2.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADkPEKAKLLlEGVENKLTPCLKIIVIMDSYDNDLVERGQkcgveiiglkALE 219
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVD-SEFVPLL-AAILPQLPTVRTVIVEGDGPAAPLAPEVG----------EYE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 220 DLgrVNRTKPKPPEPE----DLAIICFTSGTTGNPKGAMVTHQNI-MNdcsgfIKATESAFIASPEDVLISFLPLAHMFE 294
Cdd:PRK06187 150 EL--LAAASDTFDFPDidenDAAAMLYTSGTTGHPKGVVLSHRNLfLH-----SLAVCAWLKLSRDDVYLVIVPMFHVHA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 295 TVVECVMLCHGAKI---GFFqgDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgQANTSVKRWLldfaskrkeaelrsg 371
Cdd:PRK06187 223 WGLPYLALMAGAKQvipRRF--DPENLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF--------------- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 372 ivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCL----SLPGDWT-AG 445
Cdd:PRK06187 281 -----------------SSL----RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLppedQLPGQWTkRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 446 HVGAPMPCNYIKLVDvEDMNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRK 523
Cdd:PRK06187 340 SAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRI 417
|
410 420 430
....*....|....*....|....*....|....*
gi 1958682904 524 KHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHGE 558
Cdd:PRK06187 418 KDVIISG-GENIYPRELEDALYGHPAVAEVAVIGV 451
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
133-557 |
8.31e-52 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 186.26 E-value: 8.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 133 GCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLleGVENKLTPCLKIIVIMDsydndlveRGQKCGVEI 212
Cdd:cd05911 54 GCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKVK--EAAKELGPKDKIIVLDD--------KPDGVLSIE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 213 IGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFiaSPEDVLISFLPLAHM 292
Cdd:cd05911 124 DLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGND--GSNDVILGFLPLYHI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 293 FETVVECVMLCHGAK-IGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfaskrkeaelRSG 371
Cdd:cd05911 202 YGLFTTLASLLNGATvIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALA---------------------------KSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 372 IVRNNSLwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLSLPGDWTAGHVGAP 450
Cdd:cd05911 255 LLDKYDL----------SSL----RVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 451 MPcNY-IKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 529
Cdd:cd05911 321 LP-NVeAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
410 420
....*....|....*....|....*...
gi 1958682904 530 aQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:cd05911 400 -KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
63-582 |
1.16e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 181.26 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 63 EVTGTTEGVRRSAVLEDDKLLlYYYDDVRTMYDGF-QRGIQVSNDGPCLGSRK--------PNQPYewisykqWVTIEQG 133
Cdd:PRK07656 3 EWMTLPELLARAARRFGDKEA-YVFGDQRLTYAELnARVRRAAAALAALGIGKgdrvaiwaPNSPH-------WVIAALG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 134 CFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFAdkpekAKLLLeGVENKLT---PCLKIIVIMDSYDNDLVERGQKCGV 210
Cdd:PRK07656 75 ALKAGAVVVPLNTRYTADEAAYILARGDAKALFV-----LGLFL-GVDYSATtrlPALEHVVICETEEDDPHTEKMKTFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 211 EIIGLKALEDLGRvnrtkpkPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfikATESAFIAS--PEDVLISFLP 288
Cdd:PRK07656 149 DFLAAGDPAERAP-------EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSN------AADWAEYLGltEGDRYLAANP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 289 LAHMF---ETVVECVMlcHGAKIgffqgDIRLLMDDLKVLQ------PTIFPVVPRLLNRMFDrifgqantsvkrwlldf 359
Cdd:PRK07656 216 FFHVFgykAGVNAPLM--RGATI-----LPLPVFDPDEVFRlieterITVLPGPPTMYNSLLQ----------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 360 ASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLSL 438
Cdd:PRK07656 272 HPDRSAEDLSS------------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 439 PGD---WTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNG 515
Cdd:PRK07656 328 LDDdrkTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 516 TLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFliaiVVP------DVEILPSWAQKR 582
Cdd:PRK07656 407 YLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
199-661 |
1.38e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 164.51 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 199 NDLVERGQKCGVEIIglkALEDLGRVNRT--KPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMN------DCSGFIKA 270
Cdd:PTZ00342 269 KDLKEKAKKLGISII---LFDDMTKNKTTnyKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNtvvplcKHSIFKKY 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 271 tesafiaSPEDVLiSFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN- 349
Cdd:PTZ00342 346 -------NPKTHL-SYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINn 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 350 -TSVKRWLLdfaskRKEAELRSGivRNNSLWDKL---IFH---KIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFY 422
Cdd:PTZ00342 418 lPPLKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYY 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 423 EGYGQTECTAGCCLSLPGDWTAGHVGAPM-PCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDG 501
Cdd:PTZ00342 491 QGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDG 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 502 WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAIVVPDVEILPSWAQK 581
Cdd:PTZ00342 571 YFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKD 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 582 RGF---QGSFEELCRNK----DINKAILEDMVK-----LGKNAGLKPFEQVKGIAVHPELFSIDNgLLTPTLKAKRPEL- 648
Cdd:PTZ00342 651 DNMlesTGINEKNYLEKltdeTINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVf 729
|
490
....*....|....*
gi 1958682904 649 --RNYFRSQIDELYS 661
Cdd:PTZ00342 730 kdYAFFIDQVKKIYK 744
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
235-571 |
2.45e-42 |
|
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: 158.93 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIkateSAFIASPEDVLISFLPLAHMFETVVECVM-LCHGAKI----G 309
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvilrK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 310 FfqgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqantsvkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqS 389
Cdd:cd17631 174 F---DPETVLDLIERHRVTSFFLVPTMIQALLQH-----------------PRFATTDL--------------------S 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 SLggkvRLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYIKLVDvEDMNYQ 467
Cdd:cd17631 214 SL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 468 AAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRS 547
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEH 365
|
330 340 350
....*....|....*....|....*....|.
gi 1958682904 548 EAVAQVFV-------HGESlqafLIAIVVPD 571
Cdd:cd17631 366 PAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
236-582 |
2.34e-41 |
|
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: 156.30 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHMFETVV----------ECVMLchg 305
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWR----WTEDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 306 akiGFF---QGDIRLLMDDLkvlqpTIFPVVPRllnrMFDRIFGQANTSVKrwllDFASKRKEAElrsgivrnnslwdkl 382
Cdd:cd05941 163 ---PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 383 ifhkiqsslgGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPCNYIKLVD 460
Cdd:cd05941 212 ----------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 VEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 539
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 540 IENIYLRSEAVAQVFVHGESLQAF---LIAIVVP-------DVEILPSWAQKR 582
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
172-555 |
1.61e-40 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 155.09 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 172 KAKLLL---EGVEnKLTPCLKIIVIMDSYDNDLvergqkcgveiiglkALEDLGRVNRTKPKPPEPE----DLAIICFTS 244
Cdd:cd05904 104 GAKLAFttaELAE-KLASLALPVVLLDSAEFDS---------------LSFSDLLFEADEAEPPVVVikqdDVAALLYSS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 245 GTTGNPKGAMVTHQNIMNDCSGFIKATESAFiaSPEDVLISFLPLAHMFE-TVVECVMLCHGAKI----GFfqgDIRLLM 319
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIAMVAQFVAGEGSNS--DSEDVFLCVLPMFHIYGlSSFALGLLRLGATVvvmpRF---DLEELL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 320 DDLKVLQPTIFPVVPRLLNRMfdrifgqantsVKrwlldfaskrkeaelrSGIVRNNSLwdklifhkiqSSLggkvRLMI 399
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLAL-----------VK----------------SPIVDKYDL----------SSL----RQIM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 400 TGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAG---CCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEV 475
Cdd:cd05904 282 SGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGEL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 476 CVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 555
Cdd:cd05904 362 WIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEILDAAV 440
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
234-565 |
3.75e-38 |
|
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: 144.73 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVEcVMLC--HGAKIGFf 311
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN--GYFIGERLGL--TEQDRLCIPVPLFHCFGSVLG-VLACltHGATMVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 qgdIRLLMDDLKVLQ-------------PTIFPvvpRLLNRMFDRIFgqantsvkrwllDFASkrkeaeLRSGIvrnnsl 378
Cdd:cd05917 75 ---PSPSFDPLAVLEaiekekctalhgvPTMFI---AELEHPDFDKF------------DLSS------LRTGI------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 379 wdklifhkiqsslggkvrlmiTGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLSLPGDWT---AGHVGAPMPCN 454
Cdd:cd05917 125 ---------------------MAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 455 YIKLVDVEDmNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 533
Cdd:cd05917 184 EAKIVDPEG-GIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGE 261
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958682904 534 YIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLI 565
Cdd:cd05917 262 NIYPREIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIR 300
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
147-543 |
1.35e-37 |
|
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: 146.32 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 147 TLGTDAITYIVNKAELSVIFADKP--EKAKLL-------------LEGVENKLTPCLKIIVIMDSYdndlvergqkcgve 211
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK-------------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 212 IIGLKALEDLGRVNRtkpkppEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAH 291
Cdd:cd05909 130 FPPKWLLRIFGVAPV------QPDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 292 MFetvvecvmlchgakiGFFQGDIRLLMDDLKVLQ---PTIFPVVPRLLNRMFDRIFGQANTsvkrwLLDFASKRKEAEL 368
Cdd:cd05909 200 SF---------------GLTGCLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPT-----FLRGYARAAHPED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 369 RSGIvrnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHV 447
Cdd:cd05909 260 FSSL-----------------------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 448 GAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 527
Cdd:cd05909 317 GRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFA 395
|
410
....*....|....*.
gi 1958682904 528 KLAqGEYIAPEKIENI 543
Cdd:cd05909 396 KIA-GEMVSLEAIEDI 410
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
233-566 |
1.06e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 145.20 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfIKATESAFIASPEDVLISFLPLAHMFETVVECVMLCH-GAKigff 311
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-AKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIElGGQ---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 qgdirllmdDLKVLQPTIFP-VVPRLLNRMFDRIFGqANTSVKRWLldfaskrkeaelrsgivrNNSLWDKLIFhkiqSS 390
Cdd:PRK08974 279 ---------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEEFQELDF----SS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 391 LggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLSLPGdwTAGHVGAPMPCNYIKLVDvEDMNyQ 467
Cdd:PRK08974 327 L----KLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGN-E 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 468 AAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 546
Cdd:PRK08974 399 VPPGEpGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340
....*....|....*....|....*..
gi 1958682904 547 SEAVAQVF-------VHGESLQAFLIA 566
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
215-565 |
8.75e-36 |
|
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: 141.30 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 215 LKALEDLGRVNRTkPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAHMFE 294
Cdd:cd05926 130 LSNLLADKKNAKS-EGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 295 TVVECV-MLCHGAKI----GFfqgDIRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkRWLLDFASKRKEAELr 369
Cdd:cd05926 205 LVASLLsTLAAGGSVvlppRF---SASTFWPDVRDYNATWYTAVPTIH----------------QILLNRPEPNPESPP- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 370 sgivrnnslwdklifhkiqsslgGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE-CTAGCCLSLPGDW-TAGHV 447
Cdd:cd05926 265 -----------------------PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEaAHQMTSNPLPPGPrKPGSV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 448 GAPMPcNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 527
Cdd:cd05926 322 GKPVG-VEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958682904 528 KLAqGEYIAPEKIENIYLRSEAVAQ--VF-----VHGESLQAFLI 565
Cdd:cd05926 400 NRG-GEKISPLEVDGVLLSHPAVLEavAFgvpdeKYGEEVAAAVV 443
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
141-557 |
5.86e-35 |
|
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: 139.58 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 141 VVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLleGVENKLtPCLKIIVIMDSyDNDLveRGQKCgveIIGLKALED 220
Cdd:cd17642 96 VAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVL--NVQKKL-KIIKTIIILDS-KEDY--KGYQC---LYTFITQNL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 221 LGRVNRTKPKPPE---PEDLAIICFTSGTTGNPKGAMVTHQNImndCSGFIKATESAFIA--SPEDVLISFLPLAHMFET 295
Cdd:cd17642 167 PPGFNEYDFKPPSfdrDEQVALIMNSSGSTGLPKGVQLTHKNI---VARFSHARDPIFGNqiIPDTAILTVIPFHHGFGM 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 296 VVECVMLCHGAKIGF---FQGDIRL-LMDDLKV----LQPTIFPVVPrllnrmfdrifgqantsvKRWLLDfaskrkeae 367
Cdd:cd17642 244 FTTLGYLICGFRVVLmykFEEELFLrSLQDYKVqsalLVPTLFAFFA------------------KSTLVD--------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 368 lrsgivrnnsLWDKLIFHKIQSslggkvrlmitGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLSLPGDWTAGH 446
Cdd:cd17642 297 ----------KYDLSNLHEIAS-----------GGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 447 VGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 526
Cdd:cd17642 356 VGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSL 435
|
410 420 430
....*....|....*....|....*....|.
gi 1958682904 527 FKLaQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:cd17642 436 IKY-KGYQVPPAELESILLQHPKIFDAGVAG 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
236-557 |
9.86e-35 |
|
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: 136.65 E-value: 9.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesaFIASPEDVLISFLPLAHMFETVVEC-VMLCHGAKIgffqgd 314
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARR----FGLGEDDVYLTVLPLFHINAQAVSVlAALSVGATL------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 315 irllmddlkVLQPTIfpvvprllnrmfdrifgqantSVKRWLLDFAskrkeaelRSGIVRNNSLWDKLIFHKIQ----SS 390
Cdd:cd05934 152 ---------VLLPRF---------------------SASRFWSDVR--------RYGATVTNYLGAMLSYLLAQppspDD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 391 LGGKVRLmITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDveDMNYQAAK 470
Cdd:cd05934 194 RAHRLRA-AYGAPNPPELHEEFEER-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD--DDGQELPA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 471 GE-GEVCVKGAN---VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLR 546
Cdd:cd05934 270 GEpGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILR 347
|
330
....*....|.
gi 1958682904 547 SEAVAQVFVHG 557
Cdd:cd05934 348 HPAVREAAVVA 358
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
233-573 |
1.04e-34 |
|
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: 137.27 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLA---HMFETvveCVMLCHGAKI- 308
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSfdvSVWEI---FGALLAGATLv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 ---GFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVkrwlldfaskrkeaelrsgivrnnslwdklifh 385
Cdd:cd05930 164 vlpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL--------------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 386 kiqsslggkvRLMITGAAPVSATVLT-FLRAALGCQFYEGYGQTECTAGCCL--SLPGDWTAGHV--GAPMPCNYIKLVD 460
Cdd:cd05930 211 ----------RLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPIPNTRVYVLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 vEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 534
Cdd:cd05930 281 -ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYR 358
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958682904 535 IAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPDVE 573
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEG 400
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
221-571 |
1.55e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 138.74 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 221 LGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNI---MNDCsgfiKATESAFIASPEDVLISFLPLAHMFETVV 297
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvanMLQC----RALMGSNLNEGCEILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 298 ECVMLchgakigffqgdirLLMDDLKVLQPTifpvvPRLLNRMfdrifgqantsVKrwlldfaskrkeaELR----SGIV 373
Cdd:PRK05677 269 HCMAM--------------MLIGNHNILISN-----PRDLPAM-----------VK-------------ELGkwkfSGFV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 374 RNNSLWDKLI----FHKIQSSlggKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA 449
Cdd:PRK05677 306 GLNTLFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 450 PMPCNYIKLVDveDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 528
Cdd:PRK05677 383 PVPSTLCKVID--DDGNELPLGEvGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI- 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958682904 529 LAQGEYIAPEKIENIYLRSEAVAQVfvhgeslqaflIAIVVPD 571
Cdd:PRK05677 460 LVSGFNVYPNELEDVLAALPGVLQC-----------AAIGVPD 491
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
221-557 |
2.52e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.21 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 221 LGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIM-NDCSGfiKATESAFIASPEDVLiSFLPLAHMFE-TVVE 298
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQG--KAWVPGLGDGPERVL-AALPMFHAYGlTLCL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 299 CVMLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIfgqantsvkrwlldfaskRKEAELRsGIvrnns 377
Cdd:PRK05605 282 TLAVSIGGELVLLPApDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 378 lwdklifhkiqsSLGGkVRLMITGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMPCN 454
Cdd:PRK05605 334 ------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFPDT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 455 YIKLVDVEDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 533
Cdd:PRK05605 399 EVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGF 476
|
330 340
....*....|....*....|....
gi 1958682904 534 YIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVG 500
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
189-555 |
6.56e-34 |
|
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: 134.32 E-value: 6.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 189 KIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFI 268
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN----LL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 269 KATESAFIASPEDVLISFLPLAH------MFETvvecvmLCHGAK--------IGFFQGDIRLLMDDLKVlqpTIFPVVP 334
Cdd:TIGR01733 150 AWLARRYGLDPDDRVLQFASLSFdasveeIFGA------LLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLTP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 335 RLLNRMFDRIFGQANTsvkrwlldfaskrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGA-APVSATVLTFL 413
Cdd:TIGR01733 221 SLLALLAAALPPALAS--------------------------------------------LRLVILGGeALTPALVDRWR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 414 RAALGCQFYEGYGQTECTAGC-CLSLPGDWTAGHV----GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLK 488
Cdd:TIGR01733 257 ARGPGARLINLYGPTETTVWStATLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLN 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682904 489 DPARTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 555
Cdd:TIGR01733 336 RPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
221-650 |
1.41e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 135.77 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 221 LGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNI---MNDCSGFIKATESafIASPEDVLISFLPLAHMFETVV 297
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLvanMQQAHQWLAGTGK--LEEGCEVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 298 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfaskrkeaelrsg 371
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 372 ivrNNSLWDKLIFHKIQSSLGGkvrlmitGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAP 450
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 451 MPCNYIKLVDveDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 529
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 530 AQGEYIAPEKIENIYLRSEAVAQVfvhgeslqaflIAIVVPDveilpswaQKRGfqgsfeELCRNKDINK--AILEDMVK 607
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958682904 608 LGKNAGLKPFEQVKGIAVHPELFSIDNGlltptlKAKRPELRN 650
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
213-566 |
1.44e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 135.72 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 213 IGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMND------CSGFIKATESAFIASPEDVLISF 286
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 287 LPLAHMFETVVECVMLchgakigFFQGDIRLLMDDlkvlqptifpvvPRLLNRMFDRIfgqantsvKRWLLdfaskrkea 366
Cdd:PRK12492 265 LPLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKEL--------GKWRF--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 367 elrSGIVRNNSLWDKLIFHKIQSSLGGKvRLMIT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLSLPGDWT 443
Cdd:PRK12492 309 ---SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 444 A-GHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 522
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958682904 523 KKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLIA 566
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
235-582 |
6.92e-33 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 131.80 E-value: 6.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAH------MFETVVEcvmlchGAKI 308
Cdd:TIGR01923 111 DQIATLMFTSGTTGKPKAVPHTFRNHYAS----AVGSKENLGFTEDDNWLLSLPLYHisglsiLFRWLIE------GATL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 GFFQGDIRLLmDDLKVLQPTIFPVVPRLLNRMFDRifGQANTSVKRWLLdfaskrkeaelrsgivrnnslwdklifhkiq 388
Cdd:TIGR01923 181 RIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNENLRKILL------------------------------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 sslggkvrlmitGAAPVSATVLTFLRAaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHVGAPMPCNYIKLvDVEDMnyq 467
Cdd:TIGR01923 227 ------------GGSAIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKI-KVDNK--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 468 aaKGEGEVCVKGANVFKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 547
Cdd:TIGR01923 290 --EGHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQH 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958682904 548 EAVAQVFV-------HGESLQAFLIAIVVPDVEILPSWAQKR 582
Cdd:TIGR01923 366 PGIQEAVVvpkpdaeWGQVPVAYIVSESDISQAKLIAYLTEK 407
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
151-557 |
8.30e-33 |
|
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: 132.75 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 151 DAITYIVNKAELSVIFADkPEKAKLLlEGVENKLtPCLKIIVIMDSYDNDLVERGqkcgveiIGLKALEDLgrVNRTKPK 230
Cdd:cd12119 87 EQIAYIINHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAG-------VGVLAYEEL--LAAESPE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPE----DLAIICFTSGTTGNPKGAMVTHQNI--------MNDCSGFikatesafiaSPEDVlisFLPLAHMFE---- 294
Cdd:cd12119 155 YDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLvlhamaalLTDGLGL----------SESDV---VLPVVPMFHvnaw 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 295 -TVVECVMLchGAKI----GFFQGDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDrifgqantSVKRWLLDFASKRkeael 368
Cdd:cd12119 222 gLPYAAAMV--GAKLvlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLD--------HLEANGRDLSSLR----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 369 rsgivrnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHV 447
Cdd:cd12119 284 ---------------------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 448 ----------GAPMPCNYIKLVDvEDMNYQAAKGE--GEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNG 515
Cdd:cd12119 335 deqlalrakqGRPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958682904 516 TLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:cd12119 413 YLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
236-557 |
2.61e-31 |
|
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: 124.92 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMndcSGFIKATESAFIASPEDVLIsFLPLAHMFETVVECVM-LCHGAKI---GFF 311
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL---RAAAAWADCADLTEDDRYLI-INPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 qgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqantsvkrwlldfaSKRKEAELrsgivrnnslwdklifhkiqSSL 391
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 392 ggkvRLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCcLSLPGD---WTAGHVGAPMPCNYIKLVDvedmnyq 467
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVAT-MCRPGDdaeTVATTCGRACPGFEVRIAD------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 468 aakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 547
Cdd:cd17638 186 ----DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEH 260
|
330
....*....|
gi 1958682904 548 EAVAQVFVHG 557
Cdd:cd17638 261 PGVAQVAVIG 270
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
234-541 |
5.89e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 127.79 E-value: 5.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISFLPLAHMFEtvVECVMLCH---GAKIGF 310
Cdd:PLN02246 178 PDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAILI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 FQG-DIRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkrwlLDFAskrkeaelRSGIVRNNSLwdklifhkiqS 389
Cdd:PLN02246 256 MPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL----------S 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 SlggkVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLSL-------PGDWTAGHVGAPMPCNYIKLVDV 461
Cdd:PLN02246 299 S----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVDP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 462 EDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 541
Cdd:PLN02246 373 ETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
231-582 |
9.24e-30 |
|
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: 122.42 E-value: 9.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLA------HMFETvvecvmLCH 304
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIAfdacigEIFST------LCN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 305 GAKIgFFQGDIRLLMDDLKVLqpTIFPVVPRLLnrmfdrifgqantsvkrwlldfaSKRKEAELRSgivrnnslwdklif 384
Cdd:cd17653 171 GGTL-VLADPSDPFAHVARTV--DALMSTPSIL-----------------------STLSPQDFPN-------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 385 hkiqsslggkVRLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLS--LPGDWTagHVGAPMPCNYIKLVDvE 462
Cdd:cd17653 211 ----------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-A 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 463 DMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 536
Cdd:cd17653 276 DLQPVPEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRIN 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 537 PEKIENIYLRSEAVAQ---VFVHGEslqaFLIAIVVP---DVEILPSWAQKR 582
Cdd:cd17653 355 LEEIEEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
240-565 |
9.43e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 124.15 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 240 ICFTSGTTGNPKGAMVTHQNIMNDcsGFikatesaFIA-----SPEDVLISFLPLAHMFEtvveCVM-----LCHGAKI- 308
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNN--GY-------FIGeamklTEEDRLCIPVPLYHCFG----MVLgnlacVTHGATMv 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 ----GFfqgdirllmDDLKVLQ-------------PTIFpvVPRLLNRMFDRifgqantsvkrwlLDFASkrkeaeLRSG 371
Cdd:PRK08315 271 ypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR-------------FDLSS------LRTG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 372 IvrnnslwdklifhkiqssLGGK---VRLM-----------ITGAapvsatvltflraalgcqfyegYGQTECTAGCCLS 437
Cdd:PRK08315 321 I------------------MAGSpcpIEVMkrvidkmhmseVTIA----------------------YGMTETSPVSTQT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 438 LPGD------WTaghVGAPMPCNYIKLVDvEDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGK 510
Cdd:PRK08315 361 RTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAV 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 511 WLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV--AQVF-V----HGESLQAFLI 565
Cdd:PRK08315 437 MDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEEVCAWII 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
222-543 |
1.88e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 123.21 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 222 GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPED---VLISFLPLAHMFETVVE 298
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlNFVCALPLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 299 CVMlchGAKIGffqG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfaskrkeaelr 369
Cdd:PRK07059 271 GLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 370 sgivrNNSLWDKLIFHKIQSSLGGkvrlmitGAApVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHV 447
Cdd:PRK07059 317 -----NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSPVATCNPVDATEfsGTI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 448 GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 527
Cdd:PRK07059 383 GLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
330
....*....|....*.
gi 1958682904 528 kLAQGEYIAPEKIENI 543
Cdd:PRK07059 462 -LVSGFNVYPNEIEEV 476
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
234-595 |
2.16e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 122.96 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVeCVMLC--HGAKIgFF 311
Cdd:PRK12583 200 RDDPINIQYTSGTTGFPKGATLSHHNILNN--GYFVAESLGL--TEHDRLCVPVPLYHCFGMVL-ANLGCmtVGACL-VY 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 QGDirlLMDDLKVLQ-------------PTIFpvVPRLLNRMFDRifgqantsvkrwlLDFASkrkeaeLRSGIVrnnsl 378
Cdd:PRK12583 274 PNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS------LRTGIM----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 379 wdklifhkiqsslggkvrlmitGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLSLPGD---WTAGHVGAPMPCN 454
Cdd:PRK12583 325 ----------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVETVGRTQPHL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 455 YIKLVDVEDMNyqAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 533
Cdd:PRK12583 383 EVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGE 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958682904 534 YIAPEKIENIYLRSEAVAQVFVHGeslqafliaivVPDV---EILPSWAQKR-GFQGSFEEL---CRNK 595
Cdd:PRK12583 460 NIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEELrefCKAR 517
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
232-593 |
3.31e-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: 120.95 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 232 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsgfikATESAFIA----SPEDVLISFLPLAHMFETVvecvmlcHGAK 307
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLS--------ASIRQYAErlglGPGDVFLVASPMAHQTGFV-------YGFT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 IGFFQGDIRLLMDdlkVLQPTifpVVPRLLNRmfDRI-FGQANTSVKRWLLDfASKRKEAELRSgivrnnslwdklifhk 386
Cdd:cd05903 155 LPLLLGAPVVLQD---IWDPD---KALALMRE--HGVtFMMGATPFLTDLLN-AVEEAGEPLSR---------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 iqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEC--TAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvEDM 464
Cdd:cd05903 210 --------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 465 NYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 544
Cdd:cd05903 281 ATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLL 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 545 LRSEAVAQVFVHG---ESLQAFLIAIVVPdveilpswaqKRGFQGSFEELCR 593
Cdd:cd05903 359 LGHPGVIEAAVVAlpdERLGERACAVVVT----------KSGALLTFDELVA 400
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
232-577 |
3.36e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 121.64 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 232 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAHMfetvvecvmlcHGAKIGff 311
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD----LDALAEAWQWTADDVLVHGLPLFHV-----------HGLVLG-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 qgdirllmddlkVLQPTifpvvpRLLNRMfdrifgqantsvkRWLLDFASKRKEAELRSG-------------IVRNNSL 378
Cdd:PRK07787 188 ------------VLGPL------RIGNRF-------------VHTGRPTPEAYAQALSEGgtlyfgvptvwsrIAADPEA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 379 WDKLifhkiqsslgGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKL 458
Cdd:PRK07787 237 ARAL----------RGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDvEDMNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLA 530
Cdd:PRK07787 307 VD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIG 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958682904 531 QGEyiapekIENIYLRSEAVAQVFVHGE---SLQAFLIAIVVPDVEILPS 577
Cdd:PRK07787 386 AGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGADDVAAD 429
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
199-555 |
7.74e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 121.24 E-value: 7.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 199 NDLVERGQKCGVEIIGLKALEdlgrvnrtkpkppepEDLAIICFTSGTTGNPKGAMVTHQN-IMNDCSgfikateSAFIA 277
Cdd:PLN02330 163 KELLEAADRAGDTSDNEEILQ---------------TDLCALPFSSGTTGISKGVMLTHRNlVANLCS-------SLFSV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 278 SPEDV----LISFLPLAHMFETVVEC--VMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMfdrifgqants 351
Cdd:PLN02330 221 GPEMIgqvvTLGLIPFFHIYGITGICcaTLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNL----------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 352 VKrwlldfaskrkeaelrsgivrnNSLWDKLIFHKIqsslggKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTEC 430
Cdd:PLN02330 290 VK----------------------NPIVEEFDLSKL------KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEH 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 431 TagcCLSLP-GDWTAGH-------VGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW 502
Cdd:PLN02330 342 S---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 503 LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 555
Cdd:PLN02330 419 LHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
140-625 |
8.12e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.11 E-value: 8.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIvimdsYDNDLVERGQKcgVEII--GLKA 217
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVI-----YLEDLKAKISK--VDKLtaLLAA 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 218 ----LEDLGRVNRTKPKPpepEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAHMF 293
Cdd:PRK08633 764 rllpARLLKRLYGPTFKP---DDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSF 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 294 ETVVECVM-LCHGAKIGFFQGDirllMDDLKVLQ-------------PTIFpvvprllnRMFDRifgqaNTSVKRwlLDF 359
Cdd:PRK08633 837 GLTVTLWLpLLEGIKVVYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--LMF 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 360 ASkrkeaelrsgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLP 439
Cdd:PRK08633 898 AS---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLP 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 440 -----GDWT-----AGHVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL---DKDGWLHTG 506
Cdd:PRK08633 945 dvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTG 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 507 DIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniylrsEAVAQVFvHGESLQafLIAIVVPDveilpswaQKRGFQ- 585
Cdd:PRK08633 1025 DKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD--------EKKGEKl 1086
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 586 --------GSFEELCR---NKDINKA-------ILEDMVKLGknAGLKPFEQVKGIAV 625
Cdd:PRK08633 1087 vvlhtcgaEDVEELKRaikESGLPNLwkpsryfKVEALPLLG--SGKLDLKGLKELAL 1142
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
140-577 |
9.54e-29 |
|
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: 119.85 E-value: 9.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADkpekaklllEGVENKLTPCLkiiviMDSYDNDLVergqkcgveiIGLKALE 219
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLAD---------AGAADRLRDAL-----PASPDPGTV----------LDADGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 220 DLGRvnRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsgfikaTESAFIAS-----PEDVLISFLPLAHMFE 294
Cdd:cd05922 104 AARA--SAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLL---------ANARSIAEylgitADDRALTVLPLSYDYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 295 TVVECVMLCHGAKIgFFQGDIRL---LMDDLKVLQPTIFPVVPRLLNrMFDRifgqantsvkrwlLDFAsKRKEAELRsg 371
Cdd:cd05922 173 LSVLNTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTR-------------LGFD-PAKLPSLR-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 372 ivrnnslwdklifhkIQSSLGGKVRlmitgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCCLsLPGDWTA---GHVG 448
Cdd:cd05922 235 ---------------YLTQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMTY-LPPERILekpGSIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 449 APMPCNYIkLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 528
Cdd:cd05922 290 LAIPGGEF-EILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIK 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 529 LAqGEYIAPEKIENIyLRSEA---VAQVFVHGESLQAFLIAIVVPDVEILPS 577
Cdd:cd05922 369 LF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
231-524 |
2.71e-28 |
|
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: 119.69 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfikaTESAFIASPEDVLISFLPLAHmfetVVECVMlCHGAkigf 310
Cdd:cd05906 163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG----KIQHNGLTPQDVFLNWVPLDH----VGGLVE-LHLR---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 fqgDIRLLMDDLKVLQPTIFPVVPRLLnRMFDRiFGQANTsvkrWLLDFA-SKRKEAELRsgivRNNSLWDklifhkiQS 389
Cdd:cd05906 230 ---AVYLGCQQVHVPTEEILADPLRWL-DLIDR-YRVTIT----WAPNFAfALLNDLLEE----IEDGTWD-------LS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 SLggkvRLMITGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGC--CLSLP-GDWTAGH----VGAPMPCNYI 456
Cdd:cd05906 290 SL----RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSM 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 457 KLVDVEDmNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 524
Cdd:cd05906 366 RIVDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
235-558 |
5.70e-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: 116.68 E-value: 5.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgfikateSAfIASPE-------DVLISFLPLAH------MFETVVE-CV 300
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWW----------SA-IGSALnlgltedDNWLCALPLFHisglsiLMRSVIYgMT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 301 MLCHGAkigFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSVkrwlldfaskrkeaelrsgivrnnslwd 380
Cdd:cd05912 146 VYLVDK---FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL---------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 381 klifhkiqsslggkvRLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTE-CTAGCCLSlPGDWTA--GHVGAPMPCNYIK 457
Cdd:cd05912 192 ---------------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 458 LVDvedmNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 537
Cdd:cd05912 255 IED----DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYP 328
|
330 340
....*....|....*....|.
gi 1958682904 538 EKIENIYLRSEAVAQVFVHGE 558
Cdd:cd05912 329 AEIEEVLLSHPAIKEAGVVGI 349
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
231-524 |
3.41e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 115.74 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNI------MNDCSGFikatesafiaSPEDVLISFLPLAH---MFetVVECVM 301
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLlsnaltLVDYWRF----------TPDDVLIHALPIFHthgLF--VATNVA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 302 LCHGAKIGFFQG-DIRLLMDDLKvlQPTIFPVVP----RLL-NRMFDRifgqantsvkrwlldfaskrkEAelrsgiVRN 375
Cdd:PRK07514 220 LLAGASMIFLPKfDPDAVLALMP--RATVMMGVPtfytRLLqEPRLTR---------------------EA------AAH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 376 nslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPC 453
Cdd:PRK07514 271 -------------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE--TNMNTSNPydGERRAGTVGFPLPG 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958682904 454 NYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 524
Cdd:PRK07514 330 VSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
198-582 |
4.38e-27 |
|
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: 117.65 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 198 DNDLVERGQKCGVEIIGLKALEdLGRVNRTKPKPP-EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFI 276
Cdd:COG1020 580 QSALAARLPELGVPVLALDALA-LAAEPATNPPVPvTPDDLAYVIYTSGSTGRPKGVMVEHRALVN----LLAWMQRRYG 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 277 ASPEDVLISFLPLAhmFE-TVVECVM-LCHGAKIGFFQGDIRLLMDDLKVL----QPTIFPVVPRLLNRMFDrifgqant 350
Cdd:COG1020 655 LGPGDRVLQFASLS--FDaSVWEIFGaLLSGATLVLAPPEARRDPAALAELlarhRVTVLNLTPSLLRALLD-------- 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 351 svkrwlldfaskrkeaelrsgivrnnSLWDKLifhkiqSSLggkvRLMITG--AAPVsATVLTFLRAALGCQFYEGYGQT 428
Cdd:COG1020 725 --------------------------AAPEAL------PSL----RLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPT 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 429 ECTAGCCLSL--PGDWTAGHV--GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEA-----LDK 499
Cdd:COG1020 768 ETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpFGF 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 500 DG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQA-FLIAIVVPDVEI 574
Cdd:COG1020 847 PGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGA 925
|
....*...
gi 1958682904 575 LPSWAQKR 582
Cdd:COG1020 926 AAAAALLR 933
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
229-551 |
5.64e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 116.21 E-value: 5.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 229 PKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVEC-VMLCHGAK 307
Cdd:PRK07529 207 GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLLGL--GPGDTVFCGLPLFHVNALLVTGlAPLARGAH 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 IGFF--QG--DIRLLMDDLKVL---QPTIFPVVPRLLNRMFDRIFGQANTSvkrwlldfaskrkeaelrsgivrnnslwd 380
Cdd:PRK07529 283 VVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDIS----------------------------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 381 klifhkiqsSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYIKLV 459
Cdd:PRK07529 334 ---------SL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVV 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 460 DV-EDMNYQ--AAKGE-GEVCVKGANVFKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 535
Cdd:PRK07529 401 ILdDAGRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRGGHNI 478
|
330
....*....|....*.
gi 1958682904 536 APEKIENIYLRSEAVA 551
Cdd:PRK07529 479 DPAAIEEALLRHPAVA 494
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
231-565 |
1.74e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 114.36 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPE-DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAfiASPEDVLISFLPLAHMF-ETVVECVMLCHGAKI 308
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNC--KEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 GFF-QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantsvkrwlldfASKRKEAELRSgivrnnslwdklifhki 387
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALLN-----------------SPLLKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 388 qsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAPMPCNYIKLVDVEDMNY 466
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNfLWEKRVPGSIGVPWPDTEAMIMSLETGEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 467 QAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 546
Cdd:PRK06710 398 LPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYE 475
|
330 340
....*....|....*....|....*.
gi 1958682904 547 SEAVAQVFV-------HGESLQAFLI 565
Cdd:PRK06710 476 HEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
234-571 |
7.68e-26 |
|
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: 111.48 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNImndCSGfIKATESAFIASPED-VL----ISF-LPLAHMFETvvecvmLCHGAK 307
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRAL---STS-ALAHGRALGLTSESrVLqfasYTFdVSILEIFTT------LAAGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 IGffqgdI---RLLMDDLkvlqptifpvvPRLLNRMfdrifgQANT-----SVKRwLLDfaskrkEAELRSgivrnnslw 379
Cdd:cd05918 175 LC-----IpseEDRLNDL-----------AGFINRL------RVTWafltpSVAR-LLD------PEDVPS--------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 380 dklifhkiqsslggkVRLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCNyIKL 458
Cdd:cd05918 217 ---------------LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAT-CWV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDVEDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKK 524
Cdd:cd05918 279 VDPDNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKD 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 525 HIFKLaQGEYIAPEKIENIYLRS-----EAVAQVFVH-GESLQAFLIAIVVPD 571
Cdd:cd05918 359 TQVKI-RGQRVELGEIEHHLRQSlpgakEVVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
202-570 |
1.02e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 111.62 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 202 VERGQKCGVEIIGLKALEDLGRVN----------RTKPKPPEPE----DLAIICFTSGTTGNPKGAMVTHQNImndcsgf 267
Cdd:PRK06188 121 VERALALLARVPSLKHVLTLGPVPdgvdllaaaaKFGPAPLVAAalppDIAGLAYTGGTTGKPKGVMGTHRSI------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 268 ikATESAFIAS----PEDvlISFL---PLAHMFETVVECVMLCHGAKI---GFfqgDIRLLMDDLKVLQPTIFPVVPRLL 337
Cdd:PRK06188 194 --ATMAQIQLAewewPAD--PRFLmctPLSHAGGAFFLPTLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVPTMI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 338 NRmfdrifgqantsvkrwLLDFASKRKeAELrsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAAL 417
Cdd:PRK06188 267 YA----------------LLDHPDLRT-RDL--------------------SSL----ETVYYGASPMSPVRLAEAIERF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 418 GCQFYEGYGQTECTAGCCLSLPGDWTAGHV------GAPMPCNYIKLVDvEDMNyQAAKGE-GEVCVKGANVFKGYLKDP 490
Cdd:PRK06188 306 GPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGR-EVAQGEvGEICVRGPLVMDGYWNRP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 491 ARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQaf 563
Cdd:PRK06188 384 EETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT-- 459
|
....*..
gi 1958682904 564 liAIVVP 570
Cdd:PRK06188 460 --AVVVL 464
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
133-545 |
1.10e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 111.76 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 133 GCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKA----KLLLEgVENKLtPCLKIIVimdsydndLVERGQKC 208
Cdd:PRK06087 93 ACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQtrpvDLILP-LQNQL-PQLQQIV--------GVDKLAPA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 209 GVEIIGLKALEDLGRVNrtKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsgfikATESAFIA----SPEDVLI 284
Cdd:PRK06087 163 TSSLSLSQIIADYEPLT--TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL--------ASERAYCArlnlTWQDVFM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 285 SFLPLAHmfetvvecvmlchgaKIGFFQGDIR-LLMDDLKVLQPTIFPVVP-RLLNRmfdrifgQANTsvkrWLL----- 357
Cdd:PRK06087 233 MPAPLGH---------------ATGFLHGVTApFLIGARSVLLDIFTPDAClALLEQ-------QRCT----CMLgatpf 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 358 --DFASKRKEAELRSgivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLtflRAAL--GCQFYEGYGQTECTAG 433
Cdd:PRK06087 287 iyDLLNLLEKQPADL------------------SAL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 434 CCLSL--PGDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKW 511
Cdd:PRK06087 342 AVVNLddPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRM 420
|
410 420 430
....*....|....*....|....*....|....
gi 1958682904 512 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYL 545
Cdd:PRK06087 421 DEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
229-543 |
7.12e-25 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 109.16 E-value: 7.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 229 PKPP-EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIAS-PEDVLISFLPLAHMFETVVECV-MLCHG 305
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPgSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 306 AKI----GFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIFGQANTSVKrwlldfaskrkeaelrsgivrnnslwdk 381
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 382 lifhkiqsslggKVRLMITGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPCNYIKL 458
Cdd:PLN02574 320 ------------SLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 538
Cdd:PLN02574 388 VDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPA 466
|
....*
gi 1958682904 539 KIENI 543
Cdd:PLN02574 467 DLEAV 471
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
151-582 |
1.56e-24 |
|
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: 107.41 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 151 DAITYIVNKAELSVIFADKPEKAKLLLEGvenkltpclkiivimdsyDNDLVERGQkcgveiIGLKALEDLGRVNRtkpk 230
Cdd:cd17655 84 ERIQYILEDSGADILLTQSHLQPPIAFIG------------------LIDLLDEDT------IYHEESENLEPVSK---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 ppePEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmfetvvecvmlchgakigf 310
Cdd:cd17655 136 ---SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS-------------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 FqgdirllmdDLKVLQptIFPvvPRLL-NRMFdrIFGQANTSVKRWLLDFASKRkeaelRSGIVRNNSLWDKLIFHkIQS 389
Cdd:cd17655 189 F---------DASVTE--IFA--SLLSgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDLTPAHLKLLDA-ADD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 SLGGKVRLMITGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYIKLVDvED 463
Cdd:cd17655 248 SEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIYQyePETDQQVSVpiGKPLGNTRIYILD-QY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 464 MNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 537
Cdd:cd17655 327 GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIEL 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958682904 538 EKIENIYLRSEAVAQ--VFVH-GESLQAFLIAIVVPDVEILPSWAQKR 582
Cdd:cd17655 406 GEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
199-557 |
2.68e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 106.81 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 199 NDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEpeDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafias 278
Cdd:PRK09088 101 DDAVAAGRTDVEDLAAFIASADALEPADTPSIPPE--RVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRV----- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 279 peDVLISFLPLAHMFETV--VECV--MLCHGAKIGFFQGdirllmddlkvLQPTifpvvpRLLNRMFDRIFGQANTsvkr 354
Cdd:PRK09088 174 --DAHSSFLCDAPMFHIIglITSVrpVLAVGGSILVSNG-----------FEPK------RTLGRLGDPALGITHY---- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 355 wlldFASKRKEAELRSGIVRNNSLWDKLIfhkiqsslggkvrLMITGAAP-VSATVLTFLraALGCQFYEGYGQTEctAG 433
Cdd:PRK09088 231 ----FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 434 CCLSLPGDWT-----AGHVGAPMPCNYIKLVDVEDMNYQAakGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGD 507
Cdd:PRK09088 290 TVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGD 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958682904 508 IGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK09088 368 IARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
232-570 |
2.94e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.45 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 232 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHMfetvvecvmlchgakIGFF 311
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG----LGADDVILMASPMAHQ---------------TGFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 QGDIRLLMDDLK-VLQPTIFPVvprllnRMFDRI------FGQANTSvkrWLLDFASKRKEAELRSgivrnnslwdklif 384
Cdd:PRK13295 255 YGLMMPVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESGRPV-------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 385 hkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLSLPGDWTAGHVGAPMPCNYIKLVDVE 462
Cdd:PRK13295 312 ----SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPDERASTTDGCPLPGVEVRVVDAD 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 463 DMNYQAAKgEGEVCVKGANVFKGYLKDPARTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 542
Cdd:PRK13295 384 GAPLPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
330 340 350
....*....|....*....|....*....|.
gi 1958682904 543 IYLRSEAVAQVFVHG---ESLQAFLIAIVVP 570
Cdd:PRK13295 460 LLYRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
210-557 |
3.45e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 106.48 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 210 VEIIGLKALEDLGRVNRtkpKPPEPEDLAIICFTSGTTGNPKGAMVTHQNImndcsgFIKATESAFIA--SPEDVLISFL 287
Cdd:PRK06839 127 ISITSLKEIEDRKIDNF---VEKNESASFIICYTSGTTGKPKGAVLTQENM------FWNALNNTFAIdlTMHDRSIVLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 288 PLAHMfetvvecvmlchgAKIGFFQgdirllmddlkvlQPTIFP----VVPRLLN-----RMFDR-----IFGQAntSVK 353
Cdd:PRK06839 198 PLFHI-------------GGIGLFA-------------FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 354 RWLLDfASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAG 433
Cdd:PRK06839 250 QALIN-CSKFETTNLQS------------------------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 434 CCLSLPGDW--TAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKW 511
Cdd:PRK06839 304 VFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARV 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958682904 512 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK06839 382 DEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
234-558 |
3.52e-24 |
|
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: 104.48 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsGFIKATESAFiaSPEDVLISFLPLAHMFETVVECVMLchgakigFFQG 313
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLF--DPDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 314 DIRLLMDDLKVLQPTIFPVVPRLLNRMfdRIfgQANTSVKRWLLDFASKRKEAELrsgivrnnslwdklifhkiqSSLgg 393
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 394 kvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYIKLVDVE-DMNYQ--AA 469
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 470 KGE-GEVCVKGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 548
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330
....*....|
gi 1958682904 549 AVAQVFVHGE 558
Cdd:cd05944 280 AVAFAGAVGQ 289
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
140-570 |
3.58e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 106.94 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADkPEKAKLLLEGVEnkLTPCLKIIVimdsydnDLVERGQKCGVeiiGLKALE 219
Cdd:PRK08316 87 VHVPVNFMLTGEELAYILDHSGARAFLVD-PALAPTAEAALA--LLPVDTLIL-------SLVLGGREAPG---GWLDFA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 220 DLGRVNRTKPKPPEP--EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPLAHmfetvv 297
Cdd:PRK08316 154 DWAEAGSVAEPDVELadDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD----MSADDIPLHALPLYH------ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 298 ecvmlChgAKIGFFqgdirlLMDDLKVLQPTIFPVVPRLlNRMFDRIFGQANTS------VkrW--LL---DFAsKRKEA 366
Cdd:PRK08316 224 -----C--AQLDVF------LGPYLYVGATNVILDAPDP-ELILRTIEAERITSffapptV--WisLLrhpDFD-TRDLS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 367 ELRSGIVrnnslwdklifhkiqsslggkvrlmitGAAPVSATVLTFLRAAL-GCQFYEGYGQTEcTAGCCLSLPGDWTAG 445
Cdd:PRK08316 287 SLRKGYY---------------------------GASIMPVEVLKELRERLpGLRFYNCYGQTE-IAPLATVLGPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 446 HVG-APMPCNYI--KLVDvEDMNyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIID 521
Cdd:PRK08316 339 RPGsAGRPVLNVetRVVD-DDGN-DVAPGEvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVD 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 522 RKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV----HGESLQAfLIAIVVP 570
Cdd:PRK08316 416 RKKDMIKTG-GENVASREVEEALYTHPAVAEVAViglpDPKWIEA-VTAVVVP 466
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
233-565 |
4.48e-24 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 105.64 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfikaTESAFIASPEDVLISFLPLAHM--FETVVECVMLCHGAKIGF 310
Cdd:cd05935 82 ELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQ----SAVWTGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 FQGDIRLLMDDLKVLQPTIFPVVPRLLNrmfdrifgqantsvkrwlldfaskrkeaelrsgivrnnslwDKLIFHKIQSS 390
Cdd:cd05935 158 ARWDRETALELIEKYKVTFWTNIPTMLV-----------------------------------------DLLATPEFKTR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 391 LGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAK 470
Cdd:cd05935 197 DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 471 GEGEVCVKGANVFKGYLKDPARTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRS 547
Cdd:cd05935 277 EVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKH 355
|
330 340
....*....|....*....|....*
gi 1958682904 548 EAVAQVFV-------HGESLQAFLI 565
Cdd:cd05935 356 PAI*EVCVisvpderVGEEVKAFIV 380
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
140-582 |
5.19e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.40 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAklLLEGVENKLTPCLKIIVIMDSYDNDLVergqkcgveiiglkALE 219
Cdd:PRK07786 93 IAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRDIVPLLSTVVVAGGSSDDSVL--------------GYE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 220 DLgrVNRTKPKPPE---PEDL-AIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafIASPEDVLISFLPLAHM--F 293
Cdd:PRK07786 157 DL--LAEAGPAHAPvdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHIagI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 294 ETVVECVMLchGAKIgffqgdirllmddlkVLQPTifpvvprllnRMFDRifGQantsvkrwLLDFAskrkEAELRSGIV 373
Cdd:PRK07786 232 GSMLPGLLL--GAPT---------------VIYPL----------GAFDP--GQ--------LLDVL----EAEKVTGIF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 374 RNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAP 450
Cdd:PRK07786 271 LVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 451 MPCNYIKLVDvEDMNyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 529
Cdd:PRK07786 351 IPTVAARVVD-ENMN-DVPVGEvGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-I 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 530 AQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAF---LIAIVVPD-------VEILPSWAQKR 582
Cdd:PRK07786 427 SGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
236-577 |
1.07e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 102.41 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfikaTESAFIASPEDVLISFLPLAHM--FETVVECVMLchGAKIGFFQG 313
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 314 DiRLLMDDLKVLQPTIFPVVPRLLNRMFDRifGQANTSVKRwlldfaskrkeaelrsgivrnnslwdklifhkiqsslgg 393
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 394 kVRLMITGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvedmnyqaakgEG 473
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 474 EVCVKGANVFKGYLKdpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 553
Cdd:cd17630 180 EIWVGGASLAMGYLR--GQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340
....*....|....*....|....*..
gi 1958682904 554 FVHG---ESLQAFLIAIVVPDVEILPS 577
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
233-573 |
1.11e-23 |
|
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: 104.64 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETvveCVM-----LCHGAk 307
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDL---SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 igffqgdirllmddlkvlqpTIFPVvPRLLNRMFDRIF-GQANTSVKRWlldfaskrkeaelrsgiVRNNSLWDKLIFHK 386
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVW-----------------VSTPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 --IQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL------------SLPgdwtaghVGAPMP 452
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYievtpevldgydRLP-------IGYAKP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 453 CNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKL 529
Cdd:cd05945 280 GAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958682904 530 aQGEYIAPEKIENIYLRSEAVAQVFV----HGESLQAfLIAIVVPDVE 573
Cdd:cd05945 359 -NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPG 404
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
231-574 |
1.59e-23 |
|
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: 104.59 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgfiKATESAFIA-SPEDVLISFLPL---AHMFETVVEcvmLCHGA 306
Cdd:cd12117 132 PVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR------LVKNTNYVTlGPDDRVLQTSPLafdASTFEIWGA---LLNGA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 307 KIgffqgdirllmddlkVLQPtifpvvprllnrmfdrifgqantsvKRWLLDFAskrkeaELRSGIVRN--NSLWdkLI- 383
Cdd:cd12117 203 RL---------------VLAP-------------------------KGTLLDPD------ALGALIAEEgvTVLW--LTa 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 384 --FHKI----QSSLGGkVRLMITGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCCLSLPGDWTAGHV--GAPMP 452
Cdd:cd12117 235 alFNQLadedPECFAG-LRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 453 CNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHI 526
Cdd:cd12117 314 NTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQ 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958682904 527 FKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPDVEI 574
Cdd:cd12117 393 VKI-RGFRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
234-511 |
1.70e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 105.35 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNImndCSG--FIKATeSAFIASPEDVLISFLPLAHMFETVVEC-VMLCHGAKI-- 308
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRML---CANqqMLAQT-FPFLAEEPPVLVDWLPWNHTFGGNHNLgIVLYNGGTLyi 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 -------GFFQGDIRllmdDLKVLQPTIFPVVPR----LLNRMfdrifgqantsvkrwlldfaskRKEAELRSgivrnns 377
Cdd:PRK08180 284 ddgkptpGGFDETLR----NLREISPTVYFNVPKgwemLVPAL----------------------ERDAALRR------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 378 lwdklifhkiqsSLGGKVRLMITGAAPVSATVLTFL----RAALGCQ--FYEGYGQTEcTAGCCLSL--PGDwTAGHVGA 449
Cdd:PRK08180 331 ------------RFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGLGMTE-TAPSATFTtgPLS-RAGNIGL 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 450 PMPCNYIKLVDVEdmnyqaakGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKW 511
Cdd:PRK08180 397 PAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
231-584 |
3.27e-23 |
|
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: 103.58 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKI 308
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 GFFQGDIRllMDDLKVLqptifpvvpRLLNRM-FDRIFgqANTSVKRWLLdfaskrkeAELRSGIVRNNSLwdklifhki 387
Cdd:cd17651 206 VLPPEEVR--TDPPALA---------AWLDEQrISRVF--LPTVALRALA--------EHGRPLGVRLAAL--------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 388 qsslggkvRLMITGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLSLPGD---WTA-GHVGAPMPCNYIKLVDv 461
Cdd:cd17651 256 --------RYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 462 EDMNyQAAKG-EGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 534
Cdd:cd17651 327 AALR-PVPPGvPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 535 IAPEKIENIYLRSEAVAQ--VFVHGE-SLQAFLIAIVVPDVEILPSWAQKRGF 584
Cdd:cd17651 405 IELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGDPEAPVDAAELRAA 457
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
140-555 |
1.17e-22 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 102.50 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFAD-------KPEKAKLLLEGVENKLTPCLKIIVImdsydndlveRGQKCGVEI 212
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITAdgglrggKVIDLKEKVDEALEELPSLEHVIVV----------GRTGADVPM 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 213 IGLKALEDL--GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATesaFIASPEDVLISFLPLA 290
Cdd:COG0365 160 EGDLDWDELlaAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV---LDLKPGDVFWCTADIG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 291 ----HMFetvveCVM--LCHGAKIGFFQGDI------RL--LMDDLKVlqpTIFPVVPRLLnRMFdrifgqantsvKRWL 356
Cdd:COG0365 237 watgHSY-----IVYgpLLNGATVVLYEGRPdfpdpgRLweLIEKYGV---TVFFTAPTAI-RAL-----------MKAG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 357 LDFASKRkeaelrsgivrnnSLwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL 436
Cdd:COG0365 297 DEPLKKY-------------DL----------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFIS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 437 SLPGDWT-AGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGAN--VFKGYLKDPARTAEAL--DKDGWLHTGDIGKW 511
Cdd:COG0365 350 NLPGLPVkPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958682904 512 LPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV 555
Cdd:COG0365 429 DEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAV 471
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
140-595 |
1.40e-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: 101.61 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADKPekakllLEGvenkltpclkiivimdsydNDLVERGQKcgveiiglkale 219
Cdd:cd12118 80 VLNALNTRLDAEEIAFILRHSEAKVLFVDRE------FEY-------------------EDLLAEGDP------------ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 220 dlgrvnRTKPKPPEPEDLAI-ICFTSGTTGNPKGAMVTHQnimndcSGFIKATESA--FIASPEDVLISFLPLAHmfetv 296
Cdd:cd12118 123 ------DFEWIPPADEWDPIaLNYTSGTTGRPKGVVYHHR------GAYLNALANIleWEMKQHPVYLWTLPMFH----- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 297 veCVMLCHGAKIGFFQG--------DIRLLMDDLKVLQPTIFPVVPRLLNRMfdrifgqANTSvkrwlldfaskrkeael 368
Cdd:cd12118 186 --CNGWCFPWTVAAVGGtnvclrkvDAKAIYDLIEKHKVTHFCGAPTVLNML-------ANAP----------------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 369 rsgivrnnslwdklifHKIQSSLGGKVRLMITGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCL------SLP 439
Cdd:cd12118 240 ----------------PSDARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAwkpewdELP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 440 GDWTAgHVGAPMPCNYIKL--VDVED---MNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWL 512
Cdd:cd12118 301 TEERA-RLKARQGVRYVGLeeVDVLDpetMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 513 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVH-------GESLQAFliaivvpdVEIlpswaqKRGFQ 585
Cdd:cd12118 379 PDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVarpdekwGEVPCAF--------VEL------KEGAK 443
|
490
....*....|...
gi 1958682904 586 GSFEEL---CRNK 595
Cdd:cd12118 444 VTEEEIiafCREH 456
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
219-574 |
4.69e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 100.04 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 219 EDLGRVNRTKPKPPEPEDL---AIICFTSGTTGNPKGAMVTHQNimndcsGFIKATESAFIA--SPEDVLISFLPLAHM- 292
Cdd:PRK03640 122 AELMNGPKEEAEIQEEFDLdevATIMYTSGTTGKPKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHIs 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 293 -FETVVECVMlcHGAKI----GFFQGDI-RLLMDDlKVlqpTIFPVVPRLLNRMFDRIfGQANTsvkrwlldfaskrkea 366
Cdd:PRK03640 196 gLSILMRSVI--YGMRVvlveKFDAEKInKLLQTG-GV---TIISVVSTMLQRLLERL-GEGTY---------------- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 367 elrsgivrNNSLwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLSLPGDWTA-- 444
Cdd:PRK03640 253 --------PSSF-----------------RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtk 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 445 -GHVGAPM-PCNyIKLVDveDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDR 522
Cdd:PRK03640 306 lGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDR 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958682904 523 KKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQ---AFLIAIVVPDVEI 574
Cdd:PRK03640 382 RSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDkwgQVPVAFVVKSGEV 435
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
233-584 |
7.40e-22 |
|
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: 99.05 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATesaFIASPEDVLIsFLPLAhmFETVVE--CVMLCHGAKIgf 310
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY---GITSSDRVLQ-FASIA--FDVAAEeiYVTLLSGATL-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 fqgdirllmddlkVLQPtifpvvprllNRMFdrifgqantsvkRWLLDFASKRKEAELRsgiVRN--NSLWDKLIFHKIQ 388
Cdd:cd17644 176 -------------VLRP----------EEMR------------SSLEDFVQYIQQWQLT---VLSlpPAYWHLLVLELLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 SSLGG--KVRLMITGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLSLPGDWTAGH-----VGAPMPC------ 453
Cdd:cd17644 218 STIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANtqvyil 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 454 -NYIKLVDVEDMnyqaakgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKK 524
Cdd:cd17644 298 dENLQPVPVGVP--------GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRID 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 525 HIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPDVEILPSWAQKRGF 584
Cdd:cd17644 370 NQVKI-RGFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
233-571 |
8.05e-22 |
|
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: 98.92 E-value: 8.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAHMFeTVVEcvM---LCHGAKIG 309
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANV----LALFAATQRWFGFNEDDVWTLFHSYAFDF-SVWE--IwgaLLHGGRLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 310 FFQGDIRLLMDDLkvlqptifpvvPRLLNRMFDRIFGQANTSVKRWLldfaskrkEAELRsgivrnnslwdkliFHKIQS 389
Cdd:cd17643 164 VVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 SLggkvRLMITGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL------SLPGDwTAGHVGAPMPCNYIKLVD 460
Cdd:cd17643 211 AL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaaDLPAA-AASPIGRPLPGLRVYVLD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 vEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 533
Cdd:cd17643 286 -ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGF 363
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958682904 534 YIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPD 571
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVAD 404
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
236-573 |
1.16e-21 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 96.57 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMndCSGFikATESAFIASPEDVLISFLPLAHMFETVVECVMLCHGAK---IGFFQ 312
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 313 GDIRL-LMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantsvkrwlldfasKRKEAELRSgiVRNnslwdklifhkiqssl 391
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 392 ggkvrlmITGA-APvsATVLTFLrAALGCQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYIKLVDVEDMnyQAAK 470
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDNDR--PVPA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 471 GE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYLRS 547
Cdd:cd17637 186 GEtGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEH 263
|
330 340
....*....|....*....|....*.
gi 1958682904 548 EAVAQVFVHGeslqafliaivVPDVE 573
Cdd:cd17637 264 PAIAEVCVIG-----------VPDPK 278
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
217-566 |
1.25e-21 |
|
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: 99.06 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 217 ALEDLGRVNRTKPKP-PEPEDLAIICFTSGTTGNPKGAMVTHqnimND--CSgfikATESAFIA--SPEDVLISFLPLAH 291
Cdd:COG1021 165 SLDALLAAPADLSEPrPDPDDVAFFQLSGGTTGLPKLIPRTH----DDylYS----VRASAEICglDADTVYLAALPAAH 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 292 MFETVVECVM--LCHGAKIgffqgdirllmddlkVLQP-----TIFP-----------VVPRLLNRMfdrifgqantsvk 353
Cdd:COG1021 237 NFPLSSPGVLgvLYAGGTV---------------VLAPdpspdTAFPlierervtvtaLVPPLALLW------------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 354 rwlLDFASKRKeAELrsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG 433
Cdd:COG1021 289 ---LDAAERSR-YDL--------------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---G 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 434 --CCLSL--PGDWTAGHVGAPM-PCNYIKLVDVEDMnyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGD 507
Cdd:COG1021 338 lvNYTRLddPEEVILTTQGRPIsPDDEVRIVDEDGN--PVPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGD 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682904 508 IGKWLPNGTLKIIDRKK-HIFKlaQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLIA 566
Cdd:COG1021 416 LVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENLLLAHPAVHDAAVvampdeyLGERSCAFVVP 480
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
233-584 |
1.34e-21 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 98.31 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKatESAFIASPEDVL----ISFLPLAHMFetvveCVMLCHGAKI 308
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR--EYELDSFPVRLLqmasFSFDVFAGDF-----ARSLLNGGTL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 GFFQGDIRL----LMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkRWLLDFASKRKE--AELRSGIVRNNSLWDKL 382
Cdd:cd17650 164 VICPDEVKLdpaaLYDLILKSRITLMESTPALI----------------RPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 383 iFHKIQSSLGGKVRLmITGAAPVSATVLTflraalgcQFYEGYGQTECTAGcclSLPgdwtaghVGAPMPCNYIKLVDvE 462
Cdd:cd17650 228 -FKTLAARFGQGMRI-INSYGVTEATIDS--------TYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-E 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 463 DMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 536
Cdd:cd17650 287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIE 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958682904 537 PEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPDVEilPSWAQKRGF 584
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELRAF 414
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
235-649 |
3.55e-21 |
|
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: 96.64 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDV-------------LISFL-PLAHMFetvveCV 300
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPL----GHIPTAAYWLGLRPDDIhwniadpgwakgaWSSFFgPWLLGA-----TV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 301 MLCHGAKIgffqgDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqanTSVKRWLldfaskrkeAELRSGIVRnnslwd 380
Cdd:cd05972 152 FVYEGPRF-----DAERILELLERYGVTSFCGPP---------------TAYRMLI---------KQDLSSYKF------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 381 klifhkiqsslgGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVD 460
Cdd:cd05972 197 ------------SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 vEDMNYQAAKGEGEVCVKGANV--FKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPE 538
Cdd:cd05972 265 -DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 539 KIENIYLRSEAVAQVFV-------HGESLQAFLIAivvpdveilpswaqKRGFQGSfEELcrnkdinkaiLEDMVKLGKN 611
Cdd:cd05972 342 EVESALLEHPAVAEAAVvgspdpvRGEVVKAFVVL--------------TSGYEPS-EEL----------AEELQGHVKK 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958682904 612 AgLKPFEQVKGIAVHPELfsidngLLTPTLKAKRPELR 649
Cdd:cd05972 397 V-LAPYKYPREIEFVEEL------PKTISGKIRRVELR 427
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
233-585 |
4.28e-21 |
|
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: 96.35 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVLISFLPlahmfetvvecvmlchgAKIGFFQ 312
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLL----GHLPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 313 GdirlLMDdlkVLQPTIFPVVPRLLNRM--FDRifGQANTSVKRWLLDFASKRKEAeLRsgIVRnnslwdkliFHKIQSS 390
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 391 LGG-KVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLSLpGDWTAGHVGAPMPCNYIKLVDVEDMNyQ 467
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLviGNCSAL-FPIKPGSMGKPIPGHRVAIVDDNGTP-L 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 468 AAKGEGEVCVK--GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYL 545
Cdd:cd05971 282 PPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLL 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958682904 546 RSEAVAQVFV-------HGESLQAFliaiVVPDVEILPSWAQKRGFQ 585
Cdd:cd05971 360 KHPAVLMAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
141-638 |
5.12e-21 |
|
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: 97.12 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 141 VVPLYDTLGTD--AITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPclkIIVIMdsydNDLVERGQkcgVEIIGLKAL 218
Cdd:cd05921 80 VSPAYSLMSQDlaKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTP---LVVSR----NAVAGRGA---ISFAELAAT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 219 EDLGRVNRTKPKPpEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfiKATESAFIASPEDVLISFLPLAHMFetvve 298
Cdd:cd05921 150 PPTAAVDAAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAM--LEQTYPFFGEEPPVLVDWLPWNHTF----- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 299 cvmlchGAKIGF-----------------FQGDIRLLMDDLKVLQPTIFPVVPrllnrmfdrifgqantsvKRWLLDFAS 361
Cdd:cd05921 222 ------GGNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVP------------------AGWEMLVAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 362 KRKEAELRSGIVRNnslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRAaLGCQ-------FYEGYGQTEcTAGC 434
Cdd:cd05921 278 LEKDEALRRRFFKR-------------------LKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATE-TAPT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 435 CLSLPGDWT-AGHVGAPMPCNYIKLVDVEdmnyqaakGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL- 512
Cdd:cd05921 337 ATFTHWPTErSGLIGLPAPGTELKLVPSG--------GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAd 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 513 ---PNGTLKIIDRKKHIFKLAQGEYIA--PekieniyLRSEAVAQ-------VFVHGESlQAFLIAIVVPDveILPSWAQ 580
Cdd:cd05921 409 pddPAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAAcaplvhdAVVAGED-RAEVGALVFPD--LLACRRL 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 581 KRGFQGSFEELCRNKDInKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLT 638
Cdd:cd05921 479 VGLQEASDAEVLRHAKV-RAAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEIT 535
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
236-577 |
6.70e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.88 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAHMFETVVECV-MLCHGAKI-----G 309
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANI----ASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLaTLASGGAVllparG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 310 FFQGdiRLLMDDLKVLQPTIFPVVPRLLNRMFDRifgqANTSvkrwlldfASKRKEAELRsgIVRNNSlwdklifhkiqs 389
Cdd:PRK05852 253 RFSA--HTFWDDIKAVGATWYTAVPTIHQILLER----AATE--------PSGRKPAALR--FIRSCS------------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 slggkvrlmitgaAPVSATVLTFLRAALGCQFYEGYGQTECT---------AGCCLSLPGDWT--AGHVGAPMpcnyIKL 458
Cdd:PRK05852 305 -------------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqieGIGQTENPVVSTglVGRSTGAQ----IRI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDVEDMNYQAAKgEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPE 538
Cdd:PRK05852 368 VGSDGLPLPAGA-VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPE 444
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958682904 539 KIENIYLRSEAVAQVFVHGESLQAF---LIAIVVPDVEILPS 577
Cdd:PRK05852 445 RVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
142-582 |
6.87e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 96.21 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 142 VPLYDTLGTDAITYIVNKAELSVIfadkpekaklllegvenkLTpclkiivimdsyDNDLVERGQKCGVEIigLKALEDL 221
Cdd:cd12116 65 VPLDPDYPADRLRYILEDAEPALV------------------LT------------DDALPDRLPAGLPVL--LLALAAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 222 GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFE-TVVECV 300
Cdd:cd12116 113 AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 301 M-LCHGAKIGFFQGDI----RLLMDDLKVLQPTIFpvvprllnrmfdrifgQANTSVKRWLLDfASKRKEAELRsgivrn 375
Cdd:cd12116 187 LpLLAGARVVIAPRETqrdpEALARLIEAHSITVM----------------QATPATWRMLLD-AGWQGRAGLT------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 376 nslwdklifhkiqsslggkvrlMITGAAPVSATVLTFLrAALGCQFYEGYGQTECT--AGCCLSLPGDwTAGHVGAPMPC 453
Cdd:cd12116 244 ----------------------ALCGGEALPPDLAARL-LSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 454 NYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHI 526
Cdd:cd12116 300 TQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQ 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 527 FKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAIVVPDVEILPSWAQKR 582
Cdd:cd12116 379 VKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
160-543 |
9.53e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 97.34 E-value: 9.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 160 AELSVIFADKP--EKAKL--LLEGVENKLtpclKIIVIMDsydndlVERGQKCGVEIIGLKAledlGRVNRTKPKPPEPE 235
Cdd:PRK06814 728 AQVKTVLTSRAfiEKARLgpLIEALEFGI----RIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPD 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMNDCsgfikATESAFI-ASPEDVLISFLPLAHMFetvvecvmlchgakiGFFQGD 314
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLANR-----AQVAARIdFSPEDKVFNALPVFHSF---------------GLTGGL 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 315 IRLLMDDLKVL---QPTIFPVVPRLlnrmfdrIFGQANT---SVKRWLLDFASKRKEAELRSgivrnnslwdklifhkiq 388
Cdd:PRK06814 854 VLPLLSGVKVFlypSPLHYRIIPEL-------IYDTNATilfGTDTFLNGYARYAHPYDFRS------------------ 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 sslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMNyqa 468
Cdd:PRK06814 909 ------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID--- 979
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682904 469 aKGeGEVCVKGANVFKGYLK-DPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 543
Cdd:PRK06814 980 -EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
231-565 |
1.26e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 95.90 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMndCSGFIKATESAFIASpeDVLISFLPLAHM-FETVVECVMLCHGAKIG 309
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCALRDD--DVYLTVMPAFHIdCQCTAAMAAFSAGATFV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 310 F--------FQGDIRLLmddlkvlQPTIFPVVPRLLNRMfdrifgqantsvkrwLLDFASKRKeaelrsgivRNNSLWDK 381
Cdd:PRK08008 245 LlekysaraFWGQVCKY-------RATITECIPMMIRTL---------------MVQPPSAND---------RQHCLREV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 382 LIFhkiqsslggkvrLMITgaapvSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSLPGD---WTAghVGAPMPCNYIKL 458
Cdd:PRK08008 294 MFY------------LNLS-----DQEKDAFEER-FGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDVEdmNYQAAKGE-GEVCVKGA---NVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 534
Cdd:PRK08008 354 RDDH--NRPLPAGEiGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GEN 430
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958682904 535 IAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLI 565
Cdd:PRK08008 431 VSCVELENIIATHPKIQDIVVVGikdsirdEAIKAFVV 468
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
234-663 |
4.44e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.48 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHqnimndcSGFIkaTES-AFIA----SPEDVLISFLPLAHM--FETVVECVML--CH 304
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISH-------SALI--VQSlAKIAivgyGEDDVYLHTAPLCHIggLSSALAMLMVgaCH 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 305 GAKIGFfqgDIRLLMDDLKVLQPTIFPVVPRLL------NRMfdRIFGQANTSVKRwLLDFAskrkeaelrsGIVRNNSL 378
Cdd:PLN02860 242 VLLPKF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRK-ILNGG----------GSLSSRLL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 379 WD-KLIF--HKIQSSLGgkvrlmITGAApvsaTVLTFLRaaLGCQFYEGYGQTECTAGCCLSLPGDWTAGH-VGAPMPCN 454
Cdd:PLN02860 306 PDaKKLFpnAKLFSAYG------MTEAC----SSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAPHV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 455 YIKL-VDVEDMnyqaakgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGE 533
Cdd:PLN02860 374 ELKIgLDESSR-------VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 534 YIAPEKIENIYLRSEAVAQVFVHGeSLQAFLIAIVVPDVEILPSW--------AQKRGFQGSFEEL---CRNKdinkail 602
Cdd:PLN02860 446 NVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK------- 517
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958682904 603 edmvklgknaGLKPFEQVKGIAVHPELFSidnglLTPTLKAKRPELRNYFRSQIDELYSTI 663
Cdd:PLN02860 518 ----------NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
233-566 |
9.13e-20 |
|
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: 92.52 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikATEsAFIASPEDVLISflpLAHMFETVvecvMLCHGAKIGFFQ 312
Cdd:cd05919 89 SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAM--ARE-ALGLTPGDRVFS---SAKMFFGY----GLGNSLWFPLAV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 313 GDIRLLMDD----------LKVLQPTIFPVVPRLLNRMFDrifgQANTSvkrwlldfaskrkEAELRSgivrnnslwdkl 382
Cdd:cd05919 159 GASAVLNPGwptaervlatLARFRPTVLYGVPTFYANLLD----SCAGS-------------PDALRS------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 383 ifhkiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvE 462
Cdd:cd05919 210 ------------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-E 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 463 DMNYQAAKGEGEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 542
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNP-EKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVES 354
|
330 340 350
....*....|....*....|....*....|.
gi 1958682904 543 IYLRSEAVAQVFV------HGES-LQAFLIA 566
Cdd:cd05919 355 LIIQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
90-661 |
1.16e-19 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 94.15 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 90 VRTMYDGFQRGIQVSNDGPCLGSRKPNQPYEWISY--------------------------------KQWVTIEQGCFTY 137
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYgtvdararelgsgllalgvrpgdvigvdceasRNIVILEVACALY 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 138 SMVVVPLYDTLGTdaITYIVNKAELSVIFADKPEKAKLLlegvenkltPC----LKIIVIMDS-YDNDLVERGQKCGVEI 212
Cdd:PTZ00297 506 GFTTLPLVGKGST--MRTLIDEHKIKVVFADRNSVAAIL---------TCrsrkLETVVYTHSfYDEDDHAVARDLNITL 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 213 IGLKALEDLGRVNRTKPKPPEPED----LAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIkATESAFIASPEDVLISFLP 288
Cdd:PTZ00297 575 IPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVHFTP 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 289 LAHMFETVVECVMLCHGAKIGffQGDIRLLMDDLKVLQPTIFPVVPRL-------LNRMFDRifgqaNTSVKRWLLDfas 361
Cdd:PTZ00297 654 FAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLfstsrlqLSRANER-----YSAVYSWLFE--- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 362 krKEAELRSGIV----RNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSaTVLTFLRAALGCQ-------FYegygqTEC 430
Cdd:PTZ00297 724 --RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEES-TSFSLLEHISVCYvpclrevFF-----LPS 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 431 TAGCCLSlpgdwtaghvGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGanvfkgylkDPARTAEAldkdgwlhtgdIGK 510
Cdd:PTZ00297 796 EGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------AAQ 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 511 WLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAIVVPDVEILP-SWAQKRGF----- 584
Cdd:PTZ00297 846 WKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMgeggg 924
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 585 ---QGSFEELCRNKdiNKAILEDMVKLGKNAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYS 661
Cdd:PTZ00297 925 parQLGWTELVAYA--SSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
200-557 |
1.41e-19 |
|
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: 92.19 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 200 DLVERGQKCGV-----------------EIIGLKALEDLGRVNRT----KPKPPEPEDLAIICFTSGTTGNPKGAMVTHQ 258
Cdd:cd05923 94 ELIERGEMTAAviavdaqvmdaifqsgvRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYTSGTTGLPKGAVIPQR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 259 NIMNDCSgFIkATESAFIASPEDVLISFLPLAHMfetvvecvmlchgakIGFFQgdirLLMDDLkVLQPTIFPVvprlln 338
Cdd:cd05923 174 AAESRVL-FM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALDGTYVVV------ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 339 RMFDRIFgqantsvkrwlldfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGK-VRLMITGAAPVSATVLTFLRAAL 417
Cdd:cd05923 226 EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTFAGATMPDAVLERVNQHL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 418 GCQFYEGYGQTEctAGCCLSLPgDWTAGHVGAPMPCNYIKLVDV-EDMNYQAAKG-EGEVCVK--GANVFKGYLKDPART 493
Cdd:cd05923 292 PGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaADAAFTGYLNQPEAT 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958682904 494 AEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:cd05923 369 AKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
209-572 |
2.67e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.30 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 209 GVEIIGLKALEDL--GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISF 286
Cdd:PRK12467 628 GLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMV 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 287 LPLAHMFETVVECVMLCHGAKIgffqgdirLLMDDLKVLQPTIFpvvprllnrmFDRIFGQANTsvkrwLLDFASkrkea 366
Cdd:PRK12467 704 STFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF----------AALMADQGVT-----VLKIVP----- 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 367 elrsgivrnnSLWDKLIFHKIQSSLGGKVRLMITGAA-PVSATVLTFlRAALGCQFYEGYGQTECTAGC----CLSLPGD 441
Cdd:PRK12467 756 ----------SHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-ALGPGARLINHYGPTETTVGVstyeLSDEERD 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 442 WTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPN 514
Cdd:PRK12467 825 FGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRAD 903
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 515 GTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV--HGESLQAFLIAIVVPDV 572
Cdd:PRK12467 904 GVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
228-649 |
3.16e-19 |
|
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: 91.28 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 228 KPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATesaFIASPEDVLISFLPLAHMFEtvvecvmLCHGAK 307
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYG-------LGNSLT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 IGFFQGDIRLLM----------DDLKVLQPTIFPVVPRLLNRMfdrifgqanTSVKRWlldfaskrkeaelrsgivrnns 377
Cdd:cd05959 226 FPLSVGATTVLMperptpaavfKRIRRYRPTVFFGVPTLYAAM---------LAAPNL---------------------- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 378 lwdklifhkiQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIK 457
Cdd:cd05959 275 ----------PSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 458 LVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 537
Cdd:cd05959 345 LRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSP 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 538 EKIENIYLRSEAVAQVFVHGESLQAFLI---AIVVPdveilpswaqKRGFQGSfeelcrnkdinkAILEDMVKLGKNAGL 614
Cdd:cd05959 422 FEVESALVQHPAVLEAAVVGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRL 479
|
410 420 430
....*....|....*....|....*....|....*
gi 1958682904 615 KPFEQVKGIAVHPELFSidngllTPTLKAKRPELR 649
Cdd:cd05959 480 APYKYPRWIVFVDELPK------TATGKIQRFKLR 508
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
140-557 |
3.96e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.38 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADkPEKAKLLLEGVENklTPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALE 219
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 220 DlGRvNRTKPKPPEPEDLAI-ICFTSGTTGNPKGAMVTHQNIMNDCSGfIKATESAFIASPEdvliSFL---PLAHmfet 295
Cdd:PRK05620 167 D-GR-STVYDWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLS-LRTTDSLAVTHGE----SFLccvPIYH---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 296 vvecvMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRmfdrifgQANTSvkrwlldfaskrkeaelrsgivrn 375
Cdd:PRK05620 236 -----VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPR-------VAHGV------------------------ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 376 NSLWDKLIFHKIQS-----SLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA- 449
Cdd:PRK05620 280 PTLWIQLMVHYLKNppermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWa 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 450 --------PMPCNYIKLVDVEDMNyQAAKGEGEVCVKGANVFKGYLKDPART----------------AEALDKDGWLHT 505
Cdd:PRK05620 356 yrvsqgrfPASLEYRIVNDGQVME-STDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRT 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 506 GDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
235-543 |
4.06e-19 |
|
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: 89.24 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAfiaSPEDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGD 314
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNW---VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 315 IRL--LMDDLKVLQPTIFPVVPRLLNRMfdrifgqantsvkrwLLDFASKRKEAElrsgivrnnslwdklifhkiqsslg 392
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 393 gKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYIKLVDVEDMNYQAAkG 471
Cdd:cd17635 118 -SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 472 EGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 543
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
152-555 |
4.69e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 91.16 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 152 AITYIVNKAELSVIFADkPEKAKLLLEGVEnkLTPCLKIIVImdsyDNDLVERGqkcGVEIIGLKALEDLgrVNRTKP-- 229
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVI----DVDDPEYP---GGRFIGALDYEAF--LASGDPdf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 230 --KPPEPEDLAI-ICFTSGTTGNPKGaMVTHQN--IMNDCSGFIkatesAFIASPEDVLISFLPLAHmfetvveCVMLCH 304
Cdd:PRK08162 174 awTLPADEWDAIaLNYTSGTTGNPKG-VVYHHRgaYLNALSNIL-----AWGMPKHPVYLWTLPMFH-------CNGWCF 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 305 --------GAKIGFFQGDIRLLMDDLKVLQPTIF---PVVPRLLnrmfdrifgqANTsvkrwlldfaskrkEAELRSGIv 373
Cdd:PRK08162 241 pwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 374 rnnslwdklifhkiqsslGGKVRLMITGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLSLPGdWTA------- 444
Cdd:PRK08162 296 ------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlpldera 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 445 ---GHVGAPMPC-NYIKLVDVEDMNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLK 518
Cdd:PRK08162 355 qlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIK 433
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958682904 519 IIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV 555
Cdd:PRK08162 434 IKDRSKDII-ISGGENISSIEVEDVLYRHPAVLVAAV 469
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
135-557 |
5.02e-19 |
|
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: 91.02 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 135 FTYSM--------VVVPLYDTLGTDAITYIVNKAELSVIFADKpekAKLLLEGVENKLTPC---LKIIVIMDSYDNDLVE 203
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIEKAAPECpskPKLVWVGDPVPEGWID 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 204 RGQKCgveiigLKALEDLGRvnRTKPKPPEPEDLAIICFTSGTTGNPKgaMVTHQNIMndcsgfikatesafiaspedvl 283
Cdd:cd05970 162 FRKLI------KNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTY---------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 284 isflPLAHMFETvvecvMLCHGAKigffQGDIRLLMDDLKVLQPtifpvvprllnrMFDRIFGQANTSVKRWLLDFASKR 363
Cdd:cd05970 210 ----PLGHIVTA-----KYWQNVR----EGGLHLTVADTGWGKA------------VWGKIYGQWIAGAAVFVYDYDKFD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 364 KEAELRSgIVRNN--------SLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCC 435
Cdd:cd05970 265 PKALLEK-LSKYGvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 436 LSLPG-DWTAGHVGAPMPCNYIKLVDVEDMNYQAAKgEGEVCVKGAN-----VFKGYLKDPARTAEALdKDGWLHTGDIG 509
Cdd:cd05970 343 ATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958682904 510 KWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:cd05970 421 WMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
209-571 |
5.74e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 92.33 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 209 GVEIIGLKALEDLGRVNRTKPKPP-EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFL 287
Cdd:PRK12316 2119 GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFM 2194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 288 PLAhmFETVVECVM--LCHGAkigffqgdiRLLMDDLKVLQPtifpvvprllNRMFDRIFGQANTsvkrwLLDFASkrke 365
Cdd:PRK12316 2195 SFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDP----------EQLYDEMERHGVT-----ILDFPP---- 2244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 366 aelrsgivrnnSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRAALGCQF-YEGYGQTECTA-----GCCLSLP 439
Cdd:PRK12316 2245 -----------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYlFNGYGPTEAVVtpllwKCRPQDP 2313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 440 GDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWL 512
Cdd:PRK12316 2314 CGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYR 2392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 513 PNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAfLIAIVVPD 571
Cdd:PRK12316 2393 ADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
233-580 |
7.23e-19 |
|
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: 89.73 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAkigf 310
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPL----AAHCQATAERYGLTPGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 fqgdiRLLMDDLKVLQPtifpvvPRLLNRMFDR----IFGQANTSVKRWLLDFASKrkeaelrsgivrnnslwdklifhk 386
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT------------------------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 iQSSLGGKVRLMITGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLSLPGDWTAGH---VGAPMPCNYIKLV 459
Cdd:cd17649 207 -GDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 460 DvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 532
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958682904 533 EYIAPEKIENIYLRSEAVAQVFVHGES--LQAFLIAIVVP-DVEILPSWAQ 580
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELRA 411
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
217-541 |
1.77e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.28 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 217 ALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPE-DVLISFLPLAH-Mfe 294
Cdd:PRK07768 134 TVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE----FDVEtDVMVSWLPLFHdM-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 295 tvvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTIFPVVPRLLNRMFDRIFGqANTSVKRWLLDFASKRkeaeLRSGIVR 374
Cdd:PRK07768 208 -----------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELISKYRG-TMTAAPNFAYALLARR----LRRQAKP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 375 NNslWDklifhkiQSSLggkvRLMITGAAPVS-ATVLTFLRA---------ALGCqfyeGYGQTECTAGCCLSLPGD--- 441
Cdd:PRK07768 271 GA--FD-------LSSL----RFALNGAEPIDpADVEDLLDAgarfglrpeAILP----AYGMAEATLAVSFSPCGAglv 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 442 -----------------WTAGHV------GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLkDPARTAEALD 498
Cdd:PRK07768 334 vdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQD 411
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958682904 499 KDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 541
Cdd:PRK07768 412 ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
231-557 |
5.72e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 87.79 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesAFIASPEDVLISFLPlahMFETVVEcvmlchgakigf 310
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV---AVVGGEDSVFLSFLP---EFWIAGE------------ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 fqgdirllmdDLKVLQPTIF--PVVprLLNRmfdrifgqantsvkrwlldfaskrkeaelrsgivrnnslWDKLIF---- 384
Cdd:PRK06178 267 ----------NFGLLFPLFSgaTLV--LLAR---------------------------------------WDAVAFmaav 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 385 --HKIQSSLG---GKVRLMITGAapVSATVLTFL--------------------RAALGCQFYEG-YGQTEcTAGCclsl 438
Cdd:PRK06178 296 erYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALTGSVLAEAaWGMTE-THTC---- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 439 pGDWTAG-------------HVGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHT 505
Cdd:PRK06178 369 -DTFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHT 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 506 GDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK06178 447 GDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVVG 497
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
231-552 |
5.86e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 88.23 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGfIKAtesafIA--SPEDVLISFLPLAHMFE-TVVECVMLCHGAK 307
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ-IKT-----IAdfTPNDRFMSALPLFHSFGlTVGLFTPLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 IGFFQgdirllmddlkvlQPTIFPVVPRLLnrmFDR----IFGqanTSVkrWLLDFAskrkeaelrsgivRNNSLWDkli 383
Cdd:PRK08043 435 VFLYP-------------SPLHYRIVPELV---YDRnctvLFG---TST--FLGNYA-------------RFANPYD--- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 384 FHKiqsslggkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVED 463
Cdd:PRK08043 478 FAR--------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPG 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 464 MnyqaAKGeGEVCVKGANVFKGYLK--DP-------ARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 534
Cdd:PRK08043 550 I----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEM 623
|
330
....*....|....*...
gi 1958682904 535 IAPEKIENIYLRSEAVAQ 552
Cdd:PRK08043 624 VSLEMVEQLALGVSPDKQ 641
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
229-571 |
1.28e-17 |
|
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: 86.17 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 229 PKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDcsgfIKATESAFIASPEDVLISFLPLAH------MFETvvecvmL 302
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT----ILDINRRFAVGPDDRVLALSSLSFdlsvydIFGA------L 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 303 CHGAKIGFFQGDIR----LLMDDLKVLQPTIFPVVPRLLNrMfdrifgqantsvkrwLLDfaskrkeaELRSGIVRNNSL 378
Cdd:cd12114 190 SAGATLVLPDEARRrdpaHWAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 379 wdKLIFHK---IQSSLGGKVRLMITGAAPVSatvltflraaLGcqfyegyGQTEctaGCCLS-------LPGDWTAGHVG 448
Cdd:cd12114 246 --RLVLLSgdwIPLDLPARLRALAPDARLIS----------LG-------GATE---ASIWSiyhpideVPPDWRSIPYG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 449 APMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKK 524
Cdd:cd12114 304 RPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRD 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958682904 525 HIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAIVVPD 571
Cdd:cd12114 383 GQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
140-570 |
1.57e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.23 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADKpEKAKLLLEGVE----NKLTPCLKIIVImdsYDNDLVERgqkcgveiIGL 215
Cdd:PLN03102 90 VLNPINTRLDATSIAAILRHAKPKILFVDR-SFEPLAREVLHllssEDSNLNLPVIFI---HEIDFPKR--------PSS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 216 KALEDLGRVNRTKPKPP---------EPEDLAIICFTSGTTGNPKGAMVTHQnimndcsGFIKATESAFIASPEDVLISF 286
Cdd:PLN03102 158 EELDYECLIQRGEPTPSlvarmfriqDEHDPISLNYTSGTTADPKGVVISHR-------GAYLSTLSAIIGWEMGTCPVY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 287 LPLAHMFEtvvecvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTIFPVVprllnRMFDRIFGQANTSVKRWLLdfaskr 363
Cdd:PLN03102 231 LWTLPMFH--------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI-----EMHNVTHMCCVPTVFNILL------ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 364 keaelrsgivRNNSLwdklifhkIQSSLGGKVRLMITGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCL------- 436
Cdd:PLN03102 290 ----------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFcewqdew 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 437 -SLPGDWTAgHVGAPMPCNYIKLVDVEDMNYQA-------AKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDI 508
Cdd:PLN03102 350 nRLPENQQM-ELKARQGVSILGLADVDVKNKETqesvprdGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDV 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 509 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIylrseavaqVFVHGESLQAFLIAIVVP 570
Cdd:PLN03102 428 GVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
231-573 |
1.60e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 86.17 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPE----PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLPLAHMfeTVVECVMlcHGA 306
Cdd:PRK08314 182 PPPhtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNS----TPESVVLAVLPLFHV--TGMVHSM--NAP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 307 kigFFQGDIRLLMddlkvlqptifP-----VVPRLLNRMfdRIFGQANTSVKrwLLDF-ASKR-KEAELRsgivrnnSLW 379
Cdd:PRK08314 254 ---IYAGATVVLM-----------PrwdreAAARLIERY--RVTHWTNIPTM--VVDFlASPGlAERDLS-------SLR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 380 dklifhkiqsSLGGkvrlmitGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG-----------CCLSLPGDWTAGHV- 447
Cdd:PRK08314 309 ----------YIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpklQCLGIPTFGVDARVi 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 448 ----GAPMPCNyiklvdvedmnyqaakGEGEVCVKGANVFKGYLKDPARTAEA---LDKDGWLHTGDIGKWLPNGTLKII 520
Cdd:PRK08314 372 dpetLEELPPG----------------EVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFIT 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 521 DRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFliaiVVPDVE 573
Cdd:PRK08314 436 DRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
231-571 |
3.08e-17 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 85.02 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikatESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKI 308
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWM----QDEYPLGPGDRVLQKTPLS--FDVSVWELFwpLVAGARL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 GFFQGD-------IRLLMDDLKVlqpTIFPVVPRLLnrmfdRIFGQantsvkrwlldfaskrkeaELRSGivRNNSLwdk 381
Cdd:cd17646 208 VVARPGghrdpayLAALIREHGV---TTCHFVPSML-----RVFLA-------------------EPAAG--SCASL--- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 382 lifhkiqsslggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEC----TAGCClslPGDWTAGHV--GAPMPCNY 455
Cdd:cd17646 256 --------------RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidvTHWPV---RGPAETPSVpiGRPVPNTR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 456 IKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKL 529
Cdd:cd17646 319 LYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958682904 530 aQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAIVVPD 571
Cdd:cd17646 398 -RGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
229-571 |
3.14e-17 |
|
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: 85.37 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 229 PKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCsgfiKATESAFIASPEDVLISFLPLAH-M------FETVV---E 298
Cdd:cd05931 143 PPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANV----RQIRRAYGLDPGDVVVSWLPLYHdMgligglLTPLYsggP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 299 CVMLchgAKIGFFQGDIRLLmddlkvlqptifpvvpRLLNRmfdrifGQANTSVKRwllDFA----SKRKEAELRSGIvr 374
Cdd:cd05931 219 SVLM---SPAAFLRRPLRWL----------------RLISR------YRATISAAP---NFAydlcVRRVRDEDLEGL-- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 375 nnslwDkLifhkiqsslgGKVRLMITGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLSL 438
Cdd:cd05931 269 -----D-L----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 439 PGDWTAGHV----------------GAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAE------A 496
Cdd:cd05931 333 DRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaA 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682904 497 LDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENiylrseAVAQvfVHGESLQAFLIAIVVPD 571
Cdd:cd05931 413 TDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEA------TAEE--AHPALRPGCVAAFSVPD 477
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
236-566 |
7.26e-17 |
|
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: 83.92 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHqnimNDCSGFIKATESAFIASPEDVLISFLPLAHMFetVVEC-----VMLChGAKIGF 310
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 FQ----GDIRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantsVKRWLlDFASKRKEAElrsgivrnnslwdklifhk 386
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPAL---------------VSLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 iqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYIKLVDv 461
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 462 EDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 541
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 1958682904 542 NIYLRSEAVAQVFV-------HGESLQAFLIA 566
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
233-581 |
1.01e-16 |
|
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: 82.99 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikatESAFIASPED-----VLISFLPLA-HMFETvvecvmLCHGA 306
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH----RPYFGVTPADkslvyASFSFDASAwEIFPH------LTAGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 307 KIGFFQGDIRLLMDDLkvlqptifpvvprllnrmfDRIFGQANTSVKRWLLDFASKRKEAElrsgivrNNSLwdklifhk 386
Cdd:cd17645 172 ALHVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL-------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 iqsslggkvRLMITGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLSLPGDWTAGH--VGAPMPCNYIKLVDvEDM 464
Cdd:cd17645 218 ---------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANipIGKPIDNTRVYILD-EAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 465 NYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 538
Cdd:cd17645 281 QLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPG 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958682904 539 KIENIYLRSEAVAQVFV-------HGESLQAFLIAIVVPDVEILPSWAQK 581
Cdd:cd17645 360 EIEPFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
233-584 |
5.84e-16 |
|
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: 80.76 E-value: 5.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVV-ECVM-LCHGAkigf 310
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLAN----LAAAQIAAFDVGPGSRVLQFASPS--FDASVwELLMaLLAGA---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 fqgdiRLLMDDLKVLQPtifpvvprllnrmfdrifGQAntsvkrwLLDFaskrkeaelrsgivrnnsLWDKLIFHKIQS- 389
Cdd:cd17652 161 -----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPp 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 ---------SLGGKVRLMITGAAPVSATVLtflRAALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYIKLV 459
Cdd:cd17652 193 aalaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 460 DveDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 531
Cdd:cd17652 270 D--ARLRPVPPGVpGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-R 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682904 532 GEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAIVVPDVEILPSWAQKRGF 584
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELRAH 402
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
234-550 |
9.98e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 80.22 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESafiaSPEDVLISFLPLAHMFETVVecvmlCHGAKIgfFQG 313
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTHDMGLIA-----FHLAPL--IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 314 DIRLLMddlkvlqPT-IFPVVPRLlnrmfdrifgqantsvkrWLLDfASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLG 392
Cdd:cd05908 174 MNQYLM-------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 393 GKVRLMITGAAPVSATVLTFLRAALGC------QFYEGYGQTECTAGCCL----------SLPGDWTAGHVGAPM----- 451
Cdd:cd05908 228 SSIRMILNGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLpkaqspfktiTLGRRHVTHGEPEPEvdkkd 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 452 -----------PCNYIKLVDVEDMNYQAAKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKI 519
Cdd:cd05908 308 secltfvevgkPIDETDIRICDEDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVI 386
|
330 340 350
....*....|....*....|....*....|.
gi 1958682904 520 IDRKKHIFkLAQGEYIAPEKIENIYLRSEAV 550
Cdd:cd05908 387 TGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
234-593 |
1.23e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.54 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAkigff 311
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLYhpLINGA----- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 qgdiRLLMDDLKVLQPTifpvvpRLLNRMfdrifGQANTSVkrwlLDFASkrkeaelrsgivrnnSLWDKLIFHKIQSSL 391
Cdd:PRK12316 4762 ----SVVIRDDSLWDPE------RLYAEI-----HEHRVTV----LVFPP---------------VYLQQLAEHAERDGE 4807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 392 GGKVRLMITG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLSLPGDWTAG----HVGAPMPCNYIKLVDVEdM 464
Cdd:PRK12316 4808 PPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDGQ-L 4885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 465 NYQAAKGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 537
Cdd:PRK12316 4886 NPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIEL 4964
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958682904 538 EKIENIYLRSEAVAQVFVHGE--SLQAFLIAIVVP-DVEILPSWAQKRGFQGSFEELCR 593
Cdd:PRK12316 4965 GEIEARLREHPAVREAVVIAQegAVGKQLVGYVVPqDPALADADEAQAELRDELKAALR 5023
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
424-580 |
1.35e-15 |
|
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: 78.50 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 424 GYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDVEDMnyQAAKGE-GEVCVKGANVFKGYLKDPARTAEALdKDGW 502
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGR--EVPDGEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 503 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVhgeslqafliaIVVPDveilPSWAQ 580
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAV-----------IGVPD----PRWAQ 280
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
140-557 |
3.91e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 78.39 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAelsvifadkpeKAKLLLEGVENKLTPCLKI-IVIMDSYDNDLVERGQKCGVEIiglkal 218
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDA-----------GAKLLLVDEEFDAIVALETpKIVIDAAAQADSRRLAQGGLEI------ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 219 edlgrvnrTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIkateSAFIASPEDVLISFLPLAHmfetVVE 298
Cdd:PRK06145 141 --------PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHV----IALGLTASERLLVVGPLYH----VGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 299 C-----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLNRMF-----DRIfgqaNTSVKRWLLDFASKRKEAE 367
Cdd:PRK06145 205 FdlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVLtvpdrDRF----DLDSLAWCIGGGEKTPESR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 368 LRSgivrnnslwdklifhkiqsslggkvrlmitgaapvsatvltFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTA--G 445
Cdd:PRK06145 281 IRD-----------------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 446 HVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKH 525
Cdd:PRK06145 320 STGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKD 397
|
410 420 430
....*....|....*....|....*....|..
gi 1958682904 526 IFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK06145 398 MI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
232-583 |
1.32e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 78.28 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 232 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKIG 309
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALVN----RLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 310 FFQGDIRL----LMDDLKVLQPTIFPVVPRLLNRmfdriFGQANTSVKRWLldfaskrkeaelrsgivrnnslwdklifh 385
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ-----LLQMDEQVEHPL----------------------------- 1834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 386 kiqsslggKVRLMITG--AAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLSLPGDWTAGHVGAPMPCNYIK 457
Cdd:PRK12467 1835 --------SLRRVVCGgeALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTY 1904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 458 LVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLa 530
Cdd:PRK12467 1905 ILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI- 1982
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958682904 531 QGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAFLIAIVVPDVEILPSWAQKRG 583
Cdd:PRK12467 1983 RGFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
234-638 |
1.47e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.01 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPED---VLISFLPLAHMFetvvecvmlchGAKIGF 310
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMC----ANIAMQEQLRPREPDPpppVSLDWMPWNHTM-----------GGNANF 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 fQGDIR----LLMDDLKVLqPTIFPVVPRLLNRMFDRIFGqaNTSVKRWLLDFASKRKEAELRSgivrnnslwdkliFHK 386
Cdd:PRK12582 284 -NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYG--NVPAGYAMLAEAMEKDDALRRS-------------FFK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 iqsslggKVRLMITGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGccLSLPGDWTA---GHVGAPMPCNYIK 457
Cdd:PRK12582 347 -------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP--TTTGTHWDTervGLIGLPLPGVELK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 458 LVDVEDmNYqaakgegEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGE 533
Cdd:PRK12582 417 LAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGT 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 534 YIAPEKieniyLRSEAVA-------QVFVHGESlQAFLIAIVVPDVEILPSWAQKRGfqGSFEELCRNKDINKAILEDMV 606
Cdd:PRK12582 489 WVSVGT-----LRPDAVAacspvihDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHPAVLAILREGLS 560
|
410 420 430
....*....|....*....|....*....|..
gi 1958682904 607 KLGKNAGlKPFEQVKGIAVHPELFSIDNGLLT 638
Cdd:PRK12582 561 AHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
233-571 |
1.63e-14 |
|
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: 76.20 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFiaSPED---VL----ISF-LPLAHMFETvvecvmLCH 304
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAA----FLQWAAAAF--SAEElagVLastsICFdLSVFELFGP------LAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 305 GAKIgffqgdirLLMDDlkVLQPTIFPVVPR--LLNRMfdrifgqanTSVKRWLLDfaskrkeaelrsgivrnnslwdkl 382
Cdd:cd12115 171 GGKV--------VLADN--VLALPDLPAAAEvtLINTV---------PSAAAELLR------------------------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 383 ifhkiQSSLGGKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLSLPGDWTAGHVGAPMPCNYIKLV 459
Cdd:cd12115 208 -----HDALPASVRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 460 DvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 533
Cdd:cd12115 283 D-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGF 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958682904 534 YIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAIVVPD 571
Cdd:cd12115 361 RIELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
387-555 |
1.84e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 76.07 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 IQSSLGG---KVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSlPGD-WTAGHVGAPMPCNYIKLVDVE 462
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 463 DmnyqAAKGEGEVCV-----KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 537
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1958682904 538 EKIENIYLRSEAVAQVFV 555
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
182-585 |
2.55e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 75.68 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 182 NKLTPCLKIIVIMDSYDNDLVergqkcgveiIGLKALeDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQnim 261
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTF----------SALTSL-HLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQ--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 262 ndcsgfikatesAFIASPEDVL--ISF---------LPLAHmfetvvecV--------MLCHGAKIGFfqGDIRLLMDDL 322
Cdd:PRK09029 159 ------------AHLASAEGVLslMPFtaqdswllsLPLFH--------VsgqgivwrWLYAGATLVV--RDKQPLEQAL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 323 kvLQPTIFPVVPRLLNRMFDRifGQANTSVKRWLLdfaskrkeaelrsgivrnnslwdklifhkiqsslGGKvrlMItga 402
Cdd:PRK09029 217 --AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL----------------------------------GGA---AI--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 403 apvsATVLTFLRAALGCQFYEGYGQTECTAGCCL----SLPGdwtaghVGAPMPCNYIKLVDvedmnyqaakgeGEVCVK 478
Cdd:PRK09029 253 ----PVELTEQAEQQGIRCWCGYGLTEMASTVCAkradGLAG------VGSPLPGREVKLVD------------GEIWLR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 479 GANVFKGYLKDPARTAeALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVhge 558
Cdd:PRK09029 311 GASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV--- 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958682904 559 slqafliaIVVPDVE------------------ILPSWAQKR--GFQ 585
Cdd:PRK09029 385 --------VPVADAEfgqrpvavvesdseaavvNLAEWLQDKlaRFQ 423
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
242-578 |
2.72e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 75.85 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 242 FTSGTTGNPKGAMVTHQN----IMNDCSGFIKATesafiaSPEDVLISFLPLAHMfETVVECVMLCHGAKigffqgDIRL 317
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQmafvITNHLADLMPGT------TEQDASLVVAPLSHG-AGIHQLCQVARGAA------TVLL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 318 LMDDLKVlqPTIFPVVPRL-LNRMFdrifgQANTSVKRWLLDFASKRKEaelrsgivrnnslwdklifhkiQSSLggkvR 396
Cdd:PRK07470 237 PSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----------------------HSSL----R 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 397 LMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGCCLSLP------GDWTAGHVGapmPCNY------IKLVDvEDM 464
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNITVLPpalhdaEDGPDARIG---TCGFertgmeVQIQD-DEG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 465 NYQAAKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 544
Cdd:PRK07470 359 RELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKL 436
|
330 340 350
....*....|....*....|....*....|....
gi 1958682904 545 LRSEAVAQVFVHGeslqafliaivVPDveilPSW 578
Cdd:PRK07470 437 LTHPAVSEVAVLG-----------VPD----PVW 455
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
395-564 |
3.49e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 75.65 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 395 VRLMITGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG----CCL-----SLPGDwTAGHVGAPMPCNYIKL-----VD 460
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWkpewdSLPPE-EQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 VEDMNYQAAKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 538
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190
....*....|....*....|....*....|...
gi 1958682904 539 KIENIYLRSEAVAQVFV-------HGESLQAFL 564
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
231-571 |
7.53e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 74.78 E-value: 7.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 231 PPEPEDLAIICFT-SGTTGNPK------GAMVTHQNIMNDCSGFikatesafiaSPEDVLISFLPL--AHMFETVVecvm 301
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPFcgVFGFSTLL---- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 302 lchgakiGFFQGDIRLLMDDLkvlqptiF--PVVPRLL-----------NRMFDRIFGQANTSVkrwllDFASKRkeael 368
Cdd:PRK06164 242 -------GALAGGAPLVCEPV-------FdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 369 rsgivrnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTA-GCCLSLPGDWTAGHV 447
Cdd:PRK06164 298 ---------------------------LFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQAlVALQPATDPVSVRIE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 448 --GAPM-PCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 524
Cdd:PRK06164 350 ggGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMG 429
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958682904 525 HIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHGESL--QAFLIAIVVPD 571
Cdd:PRK06164 430 DSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPT 477
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
233-543 |
1.46e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 73.70 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMND---CSGFIKATEsafiaspEDVLISFLPLAHMFetvvecvmlchgakiG 309
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANqraCLKFFSPKE-------DDVMMSFLPPFHAY---------------G 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 310 FFQGDIRLLMDDLkvlqPTIF---PVVPRLLNRMFDR----IFGqaNTSVkrwLLDF---ASKRKEAELRS-------GI 372
Cdd:PRK06334 239 FNSCTLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLG--STPV---FFDYilkTAKKQESCLPSlrfvvigGD 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 373 VRNNSLWDKlifhkiqsslggkvrlmitgaapvsaTVLTFLRAALgcqfYEGYGQTECTAgcCLSLPGDWTAGH---VGA 449
Cdd:PRK06334 310 AFKDSLYQE--------------------------ALKTFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGM 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 450 PMPCNYIKLVDvEDMNYQAAKGE-GEVCVKGANVFKGYL-KDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 527
Cdd:PRK06334 358 PIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFV 436
|
330
....*....|....*.
gi 1958682904 528 KLAqGEYIAPEKIENI 543
Cdd:PRK06334 437 KIG-AEMVSLEALESI 451
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
133-555 |
1.56e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 73.64 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 133 GCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADkpekAKLL--LEGVENKLTPcLKIIVIMDSYDNDLVERGqkcgV 210
Cdd:PRK06155 90 GCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAG----W 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 211 EIIGLKALEDlgrvnRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNImndcsgFIKATESAFI--ASPEDVLISFLP 288
Cdd:PRK06155 161 STAPLPPLDA-----PAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQF------YWWGRNSAEDleIGADDVLYTTLP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 289 LAHMfetvvecvmlchGAKIGFFQGdirLLMDDLKVLQPTiFPVvprllNRMFDRIfgQANTSVKRWLLD-----FASKR 363
Cdd:PRK06155 230 LFHT------------NALNAFFQA---LLAGATYVLEPR-FSA-----SGFWPAV--RRHGATVTYLLGamvsiLLSQP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 364 KEAELRSgivrnnslwdklifHKIQSSLGGKVrlmitgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDwT 443
Cdd:PRK06155 287 ARESDRA--------------HRVRVALGPGV----------PAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-R 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 444 AGHVGAPMPCNYIKLVDVEDMNYQAakGE-GEVCVKGANVF---KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKI 519
Cdd:PRK06155 342 PGSMGRLAPGFEARVVDEHDQELPD--GEpGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRF 418
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958682904 520 IDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFV 555
Cdd:PRK06155 419 VDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAV 453
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
191-574 |
3.21e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 72.41 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 191 IVIMDSYDNDLVErGQKCGVEIIGLKALE-----DLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcS 265
Cdd:PRK07867 104 LVLTESAHAELLD-GLDPGVRVINVDSPAwadelAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS--A 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 266 GFIKATEsaFIASPEDVLISFLPLAHMFETVVE-CVMLCHGAKI---------GFfqgdirllMDDLKVLQPTIFPVVPR 335
Cdd:PRK07867 181 GVMLAQR--FGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 336 LLNrmfdrifgqantsvkrWLLDFASKRKEAElrsgivrnNSLwdklifhkiqsslggkvRLMI-TGAAPVSatVLTFlR 414
Cdd:PRK07867 251 PLS----------------YVLATPERPDDAD--------NPL-----------------RIVYgNEGAPGD--IARF-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 415 AALGCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAPMPCnyIKLVDVE--------------DMNYQAAKGEgEVCVKGA 480
Cdd:PRK07867 287 RRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 481 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGesl 560
Cdd:PRK07867 362 GGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA--- 436
|
410
....*....|....
gi 1958682904 561 qafliaivVPDVEI 574
Cdd:PRK07867 437 --------VPDPVV 442
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
233-576 |
8.02e-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: 70.89 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIkatESAFIASPEDVLISFLPlAHMFETVVE--CVMLCHGAKIGF 310
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS---ERYFGRDNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 FQGDIRL-------LMDDLKVlqpTIFPVVPRLLNRM-FDRIfgqanTSVKRWLL---DFASKRkeaelrsgivrnnslw 379
Cdd:cd17648 168 PPDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV---------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 380 dkliFHKIQSSLGGkvrLMITGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIklv 459
Cdd:cd17648 224 ----FEKLRSRFAG---LIINAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 460 dvedmnyqaakgeGEVCVKGANVFKGYLKDPARTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKH 525
Cdd:cd17648 288 -------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDF 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958682904 526 IFKLaQGEYIAPEKIENIYLRSEAVAQVFV--------HGESLQAFLIAIVVPDVEILP 576
Cdd:cd17648 355 QVKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
90-557 |
8.14e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 71.32 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 90 VRTMY-DGFQRGIQVSN----DGPCLGSRKPNqpyewISYKQWVTIEQ--GCFTYSMVVVPLYDTLGTDAITYIVNKAEL 162
Cdd:PRK06018 38 VRTTYaQIHDRALKVSQaldrDGIKLGDRVAT-----IAWNTWRHLEAwyGIMGIGAICHTVNPRLFPEQIAWIINHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 163 SVIFADK---PekaklLLEGVENKLtPCLKIIVImdsydndLVERGQKCGVEIIGLKALEDL--GRVNRTKPKPPEPEDL 237
Cdd:PRK06018 113 RVVITDLtfvP-----ILEKIADKL-PSVERYVV-------LTDAAHMPQTTLKNAVAYEEWiaEADGDFAWKTFDENTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 238 AIICFTSGTTGNPKGAMVTHQ-NIMNdcsGFIKATESAFIASPEDVLISFLPLAH-------MFETVVECVMLCHGAKIG 309
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHRsNVLH---ALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAPSMGTKLVMPGAKLD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 310 ffQGDIRLLMDDLKVlqpTIFPVVPRLlnrmfdrifgqantsvkrWLLDFASKRKEAElrsgivrnnslwdKLIFHKiqs 389
Cdd:PRK06018 257 --GASVYELLDTEKV---TFTAGVPTV------------------WLMLLQYMEKEGL-------------KLPHLK--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 390 slggkvRLMITGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLS--------LPGDWTAGHV---GAPMPCNYIKL 458
Cdd:PRK06018 298 ------MVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAalkppfskLPGDARLDVLqkqGYPPFGVEMKI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDvEDMNYQAAKGE--GEVCVKGANVFKGYLKDparTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIA 536
Cdd:PRK06018 370 TD-DAGKELPWDGKtfGRLKVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWIS 444
|
490 500
....*....|....*....|.
gi 1958682904 537 PEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK06018 445 SIDLENLAVGHPKVAEAAVIG 465
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
389-570 |
9.96e-13 |
|
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: 70.87 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 SSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSlPGDWTA--GHVGAPMPCNyIKLVDvEDMNY 466
Cdd:cd05929 244 SSL----KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGK-VHILD-EDGNE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 467 QAAKGEGEVCVKGANVFKgYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 546
Cdd:cd05929 317 VPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA 394
|
170 180
....*....|....*....|....*..
gi 1958682904 547 SEAVAQVFVHG---ESLQAFLIAIVVP 570
Cdd:cd05929 395 HPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
212-542 |
1.20e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 70.70 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 212 IIGLKALEDLGRVNRTKPKPP---EPEDLAIICFTSGTTGNPKGAMVTHQNimndcsgF---IKATESAF-IASPEDVLI 284
Cdd:PRK09274 148 LWGGTTLATLLRDGAAAPFPMadlAPDDMAAILFTSGSTGTPKGVVYTHGM-------FeaqIEALREDYgIEPGEIDLP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 285 SFlPLAHMFE------TVVECvmlchgakigffqgdirllMDDLKVLQptifpVVPRllnRMFDRIFGQANTSVkrwlld 358
Cdd:PRK09274 221 TF-PLFALFGpalgmtSVIPD-------------------MDPTRPAT-----VDPA---KLFAAIERYGVTNL------ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 359 FASKrkeaelrsgivrnnSLWDKLIFHKIQS--SLGGkVRLMITGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC---- 430
Cdd:PRK09274 267 FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpis 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 431 --TAGCCLSLPGDWT---AGH-VGAPMPCNYIKLVDVEDmNYQA--------AKGE-GEVCVKGANVFKGYLKDPARTAE 495
Cdd:PRK09274 332 siESREILFATRAATdngAGIcVGRPVDGVEVRIIAISD-APIPewddalrlATGEiGEIVVAGPMVTRSYYNRPEATRL 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958682904 496 A--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEY--IAPEKIEN 542
Cdd:PRK09274 411 AkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCERIFN 463
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
236-557 |
2.71e-12 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 69.30 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 236 DLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikatESAFIASPEDVLISFLPLAHMFE-TVVECVMLCHGAKIGF---F 311
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF----AGSGGALPSDVLYTCLPLYHSTAlIVGWSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 QGdiRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkRWLLdfASKRKEAELRsgivrnnslwdklifHKIQSSL 391
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 392 GGKVRLMITGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGcCLSLPG-DWTAGHVGAPMPCNY-IKLV--DVEDMN- 465
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSG-FINFFGkPGAIGRNPSLLRKVApLALVkyDLESGEp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 466 --------YQAAKGEGEVCVKGAN---VFKGYLkDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 528
Cdd:cd05940 272 irdaegrcIKVPRGEPGLLISRINplePFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFR 350
|
330 340
....*....|....*....|....*....
gi 1958682904 529 LaQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:cd05940 351 W-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
233-574 |
3.05e-12 |
|
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: 69.43 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgfikatesafiaspedvlisflPLAHMFEtvvecvmlchgaKIGFFQ 312
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQLEHKNMVN-------------------------LLHFERE------------KTNINF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 313 GDirllmddlKVLQPTIFPvvprlLNRMFDRIFGQANTSVKRWLLDFASKRKEAELRSGIVRNN--------SLWdKLIF 384
Cdd:cd17656 169 SD--------KVLQFATCS-----FDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNievvflpvAFL-KFIF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 385 HKIQ--SSLGGKVRLMITGAAP--VSATVLTFLRAAlGCQFYEGYG--QTECTAGCCLSLPGDWTA-GHVGAPMPCNYIK 457
Cdd:cd17656 235 SEREfiNRFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 458 LVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQ 531
Cdd:cd17656 314 ILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-R 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958682904 532 GEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAIVVPDVEI 574
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQEL 437
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
235-577 |
3.44e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 69.04 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFikaTESAFIASPEDVLISFLPLAHMFET-VVECVMLCHGAKIGFFQG 313
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 314 DI-RLLMDDLKVLQPTIFPVVPRLLNRMFdrifgqantsvkrwlldfASKRKEAELRSGivrnnslwdklifhkiqsslg 392
Cdd:cd05958 174 ATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS--------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 393 gkVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDveDMNYQAAKGE 472
Cdd:cd05958 215 --LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDGT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 473 -GEVCVKGANVFKgYLKDPARTAEAldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVA 551
Cdd:cd05958 291 iGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVA 366
|
330 340
....*....|....*....|....*....
gi 1958682904 552 QVFVHGESLQAFLI---AIVVPDVEILPS 577
Cdd:cd05958 367 ECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-552 |
5.04e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 68.64 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 232 PEPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFLPLAHMFetvvecvmlchGAKIGff 311
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTF----AAQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 qgdirllmddLKVLQPTIFPVVPrllnrmfdrifGQANtsvKRWLLDFASKRKEaelrSGIVRNNSLWDKLIFHKIQSSL 391
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 392 G-GKVRLMITGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LSLPGDWTAGH----VGAPMPCNYIKL 458
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDVEDMNYQAAKGE--------GEVCVKGANVFKGYLKDPARTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 526
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*.
gi 1958682904 527 FKLAQGEYIApEKIENIYLRSEAVAQ 552
Cdd:cd05910 357 VITTGGTLYT-EPVERVFNTHPGVRR 381
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
399-565 |
7.21e-12 |
|
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: 68.26 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 399 ITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVDvEDMNYQAAKGEGEVCV- 477
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIr 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 478 ----KGANVFKGYLKDPARTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 553
Cdd:cd05928 376 vkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 1958682904 554 FV-------HGESLQAFLI 565
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
389-573 |
1.28e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 67.24 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 SSLggkvRLMITGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMPCNyIKLVDvED 463
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 464 MNYQAAKGEGEVCVK-GANVFKgYLKDPARTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIE 541
Cdd:PRK08276 332 GNELPPGEIGTVYFEmDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIE 408
|
170 180 190
....*....|....*....|....*....|..
gi 1958682904 542 NIYLRSEAVAQVFVHGeslqafliaivVPDVE 573
Cdd:PRK08276 409 NLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
396-571 |
2.33e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 66.55 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 396 RLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE----------------CTAGCCLSlPGD--WTAGHVGAPMPcnyik 457
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnytrlddsderifTTQGRPMS-PDDevWVADADGNPLP----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 458 lvdvedmnyqaaKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----G 532
Cdd:PRK10946 377 ------------QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgG 439
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958682904 533 EYIAPEKIENIYLRSEAVaqvfvhgesLQAFLIAIvvPD 571
Cdd:PRK10946 440 EKIAAEEIENLLLRHPAV---------IHAALVSM--ED 467
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
151-551 |
3.37e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 66.27 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 151 DAITYIVNKAELSVIFAD---KPekaklLLEGVENKLtPCLKIIVIMDSYDndlvergqKCGVEIIGLKALEDL-GRVNR 226
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMTDAA--------HLPAGSTPLLCYETLvGAQDG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 227 TKPKPPEPEDLAI-ICFTSGTTGNPKGAMVTHQNIMndCSGFIKATESAFIASPEDVLisfLPLAHMFEtvVECVMLCH- 304
Cdd:PRK07008 167 DYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPYs 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 305 ----GAKIgFFQG------DIRLLMDDLKVLQPTIFPVV-PRLLNRMfdrifgqantsvkrwlldfaskrKEAELRSGIV 373
Cdd:PRK07008 240 apltGAKL-VLPGpdldgkSLYELIEAERVTFSAGVPTVwLGLLNHM-----------------------REAGLRFSTL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 374 RnnslwdklifhkiqsslggkvRLMITGAAPVSATVLTFlRAALGCQFYEGYGQTE-------CT-AGCCLSLPGD---- 441
Cdd:PRK07008 296 R---------------------RTVIGGSACPPAMIRTF-EDEYGVEVIHAWGMTEmsplgtlCKlKWKHSQLPLDeqrk 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 442 --WTAGHV--GAPMpcnyiKLVDvEDMNYQAAKGE--GEVCVKGANVFKGYLKdpaRTAEALDkDGWLHTGDIGKWLPNG 515
Cdd:PRK07008 354 llEKQGRViyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADG 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958682904 516 TLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVA 551
Cdd:PRK07008 424 FMQITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA 458
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
217-565 |
1.38e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.02 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 217 ALEDL---GRVNRTKPKPPEP-EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafIASPEDVLISFLPLAH- 291
Cdd:PRK05851 130 TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG---LDAATDVGCSWLPLYHd 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 292 MFETVVECVMLChGAKIGffqgdirllmddlkvLQPTifpvvprllnrmfdrifGQANTSVKRWLlDFASkrkeaELRSG 371
Cdd:PRK05851 207 MGLAFLLTAALA-GAPLW---------------LAPT-----------------TAFSASPFRWL-SWLS-----DSRAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 372 IVRNNSLWDKLI---FHKIQSSLGGKVRLMITGAAPVSATVLT-FLRAALGCQFYEG-----YGQTECTAGCCLSLPG-- 440
Cdd:PRK05851 248 LTAAPNFAYNLIgkyARRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAESTCAVTVPVPGig 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 441 ---------DWTAGH----VGAPMPCNYIKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPArtaeaLDKDGWLHTGD 507
Cdd:PRK05851 328 lrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGD 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958682904 508 IGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY-----LRSEAVAQVFVHGESLQAFLI 565
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAaqvrgVREGAVVAVGTGEGSARPGLV 463
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
235-565 |
2.33e-10 |
|
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: 63.31 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVlisFLPLAH------MFETVVECVMLCHGAKI 308
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALA----AFGAYLRDAVDLRPEDS---FWNAADpgwaygLYYAITGPLALGHPTIL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 ---GFFQGDIRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkrwlldfASKRKEAELRsgivrnnslwdklifh 385
Cdd:cd05973 161 legGFSVESTWRVIERLGVTNLAGSPTAYRLL----------------------MAAGAEVPAR---------------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 386 kiqssLGGKVRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCC--LSLPGDWTAGHVGAPMPCNYIKLVDveD 463
Cdd:cd05973 203 -----PKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLD--D 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 464 MNYQAAKGE-GEVCVKGANV----FKGYLKDPARTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPE 538
Cdd:cd05973 276 DGDELGPGEpGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPF 350
|
330 340 350
....*....|....*....|....*....|....
gi 1958682904 539 KIENIYLRSEAVAQVFV-------HGESLQAFLI 565
Cdd:cd05973 351 DVESALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
389-557 |
2.70e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.17 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 SSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpcnYIKLVDVEDMNY 466
Cdd:PRK13391 275 SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAM---FGDLHILDDDGA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 467 QAAKGE-GEVCVKGANVFKgYLKDPARTAEALDKDG-WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 544
Cdd:PRK13391 347 ELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLL 424
|
170
....*....|...
gi 1958682904 545 LRSEAVAQVFVHG 557
Cdd:PRK13391 425 ITHPKVADAAVFG 437
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
226-553 |
9.80e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.56 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 226 RTKPKPPEPEDLAIIcFTSGTTGNPKGAMVTHQN-------IMNDCSGFIKATESAFIASPedvlisfLPLAHM--FETV 296
Cdd:PRK05857 161 AGNADQGSEDPLAMI-FTSGTTGEPKAVLLANRTffavpdiLQKEGLNWVTWVVGETTYSP-------LPATHIggLWWI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 297 VECVMlcHGAKI---GFFQGDIRLLMDDLKVLQPTIfpvVPRLLNRMFdrifgqantsvkrwlldfaskrkeAELRSGIV 373
Cdd:PRK05857 233 LTCLM--HGGLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 374 RNNSLwdklifhkiqsslggkvRLMITGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCclsLPGD------WTAG 445
Cdd:PRK05857 284 TVPSL-----------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALC---LPTDdgsivkIEAG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 446 HVGAPMPCNYIKLVDVEDMNYQAAKGE-----GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKII 520
Cdd:PRK05857 343 AVGRPYPGVDVYLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIK 421
|
330 340 350
....*....|....*....|....*....|...
gi 1958682904 521 DRKKHIFkLAQGEYIAPEKIENIylrSEAVAQV 553
Cdd:PRK05857 422 GRSSEMI-ICGGVNIAPDEVDRI---AEGVSGV 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
234-573 |
3.59e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.56 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCsgfiKATESAFIASPEDVLISFLPLAhmFETVVECVM--LCHGAKIGFF 311
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHL----CWIAEAYELDANDRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 QGDIR---LLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLldfaskrkeaelrsgivrnnslwdklifhkiq 388
Cdd:PRK12467 3310 DNDLWdpeELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYV-------------------------------- 3357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 ssLGGKvrlmitgAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCL-SLPGDWTAGHVGAPM--PCNYIKLVdVEDMN 465
Cdd:PRK12467 3358 --FGGE-------AVPPAAFEQVK-RKLKPRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIgrPVAGRSIY-VLDGQ 3426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 466 YQ-AAKGE-GEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 536
Cdd:PRK12467 3427 LNpVPVGVaGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIE 3505
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958682904 537 PEKIENIYLRSEAVAQVFVHGESLQA--FLIAIVVPDVE 573
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADP 3544
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-541 |
3.68e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.57 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 233 EPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCS----GFikatesAFIASPEDVLISFLPLAHmfetvvecvmlchgaKI 308
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYH---------------DM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 309 GFFQGdirllmddlkVLQPtIFPVVPRLLnrMFDRIFgqaNTSVKRWLL-------------DFA----SKR-KEAELRS 370
Cdd:PRK05691 223 GLIGG----------LLQP-IFSGVPCVL--MSPAYF---LERPLRWLEaiseyggtisggpDFAyrlcSERvSESALER 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 371 givRNNSLWdklifhkiqsslggkvRLMITGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT---AGC------- 434
Cdd:PRK05691 287 ---LDLSRW----------------RVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgip 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 435 CLSLPGDWTAGHVGAP------MPCNY------IKLVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEA-LDKDG 501
Cdd:PRK05691 348 ALELDAEALARNRAEPgtgsvlMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDG 427
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958682904 502 --WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 541
Cdd:PRK05691 428 rtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
240-571 |
4.10e-09 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 58.57 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 240 ICFTSGTTGNPKGAMVTHQNIMndcsGFIKATESAFIASPEDVLISFLPLAH-MFETVVECVMLCHGAKIGFFQGDIRLL 318
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 319 MDDLKVLQPTIFPVVPRLLnrmfdrifgqantsvkrwlldfaskrkEAELRSGIvrnnslwdklIFHKIQSSLGGkvrlm 398
Cdd:cd17633 81 IRKINQYNATVIYLVPTML---------------------------QALARTLE----------PESKIKSIFSS----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 399 itGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCnyiklVDVEDMNyQAAKGEGEVCVK 478
Cdd:cd17633 119 --GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN-ADGGEIGKIFVK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 479 GANVFKGYLKdpartAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGE 558
Cdd:cd17633 191 SEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
330
....*....|....*.
gi 1958682904 559 SLQAF---LIAIVVPD 571
Cdd:cd17633 265 PDARFgeiAVALYSGD 280
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
209-573 |
4.63e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 209 GVEIIGLKA-LEDLGRVNrtKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNImndcSGFIKATESAFIASPEDVLISFL 287
Cdd:PRK12316 3171 GVQVLDLDRgDENYAEAN--PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL----SNHLCWMQQAYGLGVGDRVLQFT 3244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 288 PLAHMFETVVECVMLCHGAKIgffqgdirllmddlkVLQPTIFPVVPRLLNRMFDRIFGQANTSVKRWLLDFASKRKEAE 367
Cdd:PRK12316 3245 TFSFDVFVEELFWPLMSGARV---------------VLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHR 3309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 368 LRSgivrnnslwdklifhkiqsslggkVRLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLSLPGDWTAGH- 446
Cdd:PRK12316 3310 CTS------------------------LKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAv 3363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 447 -VGAPMPCNYIKLVDVeDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKI 519
Cdd:PRK12316 3364 pIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEY 3442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958682904 520 IDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAIVVPDVE 573
Cdd:PRK12316 3443 IGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
450-605 |
7.34e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 58.75 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 450 PMPCNYIK-----LVDVEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL-DKDGW--LHTGDIGKwLPNGTLKIID 521
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLLFYQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 522 RKKHIFKLAqGEYIAPEKIENiYLR-----SEAVAQVFVHGESLQAfLIAIVVPDveilpswaqkrgfQGSFEelcRNKD 596
Cdd:PRK04813 396 RIDFQIKLN-GYRIELEEIEQ-NLRqssyvESAVVVPYNKDHKVQY-LIAYVVPK-------------EEDFE---REFE 456
|
....*....
gi 1958682904 597 INKAILEDM 605
Cdd:PRK04813 457 LTKAIKKEL 465
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
218-573 |
8.76e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 58.40 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 218 LEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFI-----KATESAFIASPedvlisflplahM 292
Cdd:PRK07788 190 LDDLIAGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPAP------------M 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 293 FetvvecvmlcHG-----AKIGFFQG---------DIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantsvkrwLLD 358
Cdd:PRK07788 258 F----------HAtgwahLTLAMALGstvvlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGP 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 359 FASKRKEAelrsgivrnnslwdklifhkiqSSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCCLSL 438
Cdd:PRK07788 315 EVLAKYDT----------------------SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIAT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 439 PGDWTA--GHVGAPMPCNYIKLVDvEDMNyQAAKGE-GEVCVKGANVFKGYL--KDPARtaealdKDGWLHTGDIGKWLP 513
Cdd:PRK07788 368 PEDLAEapGTVGRPPKGVTVKILD-ENGN-EVPRGVvGRIFVGNGFPFEGYTdgRDKQI------IDGLLSSGDVGYFDE 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 514 NGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliaivVPDVE 573
Cdd:PRK07788 440 DGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
235-566 |
1.52e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 235 EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSgFIKATesaFIASPEDVLISFLPLAhmFE-TVVECVM-LCHGAKIGFF- 311
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQ-WMQAT---YALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 312 ---QGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSVkrwlldfaskrkeaelrsgivrnnslwdklifhkiq 388
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSL------------------------------------ 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 sslggkvRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTE----CTAGCCLSLPGDWTAghVGAPMPCNYIKLVDVEd 463
Cdd:PRK05691 1391 -------RRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLDAE- 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 464 MNYQAAKGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 536
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 1958682904 537 PEKIENIYLRSEAVAQ--VFVHGESLQAFLIA 566
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
219-571 |
1.79e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 57.34 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 219 EDLGRVNRTKP-KPPEPEDLAIICFTSGTTGNPKGAMVTHQNImndcsGFIKATESA-FIASPEDVLISFLPLAHMfetv 296
Cdd:PRK13388 133 ELVAAAGALTPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRL-----AFAGRALTErFGLTRDDVCYVSMPLFHS---- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 297 vECVM------LCHGAKI---------GFfqgdirllMDDLKVLQPTIFPVVPRLLNrmfdrifgqantsvkrWLLDFAS 361
Cdd:PRK13388 204 -NAVMagwapaVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLA----------------YILATPE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 362 KRKEAE--LRSGivrnnslwdklifhkiqssLGgkvrlmiTGAAPVSATvlTFLRAaLGCQFYEGYGQTEctAGCCLSLP 439
Cdd:PRK13388 259 RPDDADnpLRVA-------------------FG-------NEASPRDIA--EFSRR-FGCQVEDGYGSSE--GAVIVVRE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 440 GDWTAGHVGAPMPCnyIKLVDVEDM---------------NYQAAKGEgEVCVKGANVFKGYLKDPARTAEALdKDGWLH 504
Cdd:PRK13388 308 PGTPPGSIGRGAPG--VAIYNPETLtecavarfdahgallNADEAIGE-LVNTAGAGFFEGYYNNPEATAERM-RHGMYW 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682904 505 TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliaivVPD 571
Cdd:PRK13388 384 SGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPD 438
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
389-571 |
2.97e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 56.63 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 389 SSLggkvRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTE------CTAGCCLSLPGDwtaghVGAPMPCNYIKLVDvE 462
Cdd:PRK12406 271 SSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsgavtfATSEDALSHPGT-----VGKAAPGAELRFVD-E 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 463 DMNY--QAAKGEGEVCVKGANVFKgYLKDPARTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 540
Cdd:PRK12406 341 DGRPlpQGEIGEIYSRIAGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEI 417
|
170 180 190
....*....|....*....|....*....|....
gi 1958682904 541 ENIYLRSEAVAQVFVHG---ESLQAFLIAIVVPD 571
Cdd:PRK12406 418 EAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
448-541 |
4.48e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.17 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 448 GAPMPCNYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPArTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIF 527
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI 464
|
90
....*....|....
gi 1958682904 528 kLAQGEYIAPEKIE 541
Cdd:PRK09192 465 -IINGRNIWPQDIE 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
234-582 |
4.75e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMN------------DCSGFIKATESAFIASpedVLISFLPLAHmfetvvecvm 301
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNrlcwmqqayglgVGDTVLQKTPFSFDVS---VWEFFWPLMS---------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 302 lchGAkigffqgdiRLLmddlkvlqptifpVVPRLLNRMFDRIFGQANTSVKRwLLDFASKRKEAELRSGivrnnslwdk 381
Cdd:PRK12316 721 ---GA---------RLV-------------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE---------- 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 382 lifhKIQSSLggKVRLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLSLPGDWTAGHV--GAPMPCNYIKL 458
Cdd:PRK12316 765 ----DVASCT--SLRRIVCSGEALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYI 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 459 VDVeDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 532
Cdd:PRK12316 839 LDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RG 916
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682904 533 EYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAIVVPD------VEILPSWAQKR 582
Cdd:PRK12316 917 LRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
217-308 |
6.49e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 55.65 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 217 ALEDLGRVNRTKPKPPEP-------EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATEsafiASPEDVLISFLPL 289
Cdd:PRK08279 174 GYEDLAAAAAGAPTTNPAsrsgvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPL 249
|
90 100
....*....|....*....|
gi 1958682904 290 AH-MFETVVECVMLCHGAKI 308
Cdd:PRK08279 250 YHnTGGTVAWSSVLAAGATL 269
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
242-557 |
1.12e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 54.79 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 242 FTSGTTGNPKGAMVTHQNIMN--DCsgfikaTESAFIASPED-VLISflplahmfETVVECVMLcHGAKIGFFQGDIRLL 318
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHsfDC------NVHDFHMKREDsVLIA--------GTLVHSLFL-YGAISTLYVGQTVHL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 319 MddlkvlqPTIFPvvprllNRMFDRIfGQANTSVkrwlLDFASKRKEAELRSGIVRNNSLwdklifhKIQSSlGGKvrlm 398
Cdd:PRK07638 215 M-------RKFIP------NQVLDKL-ETENISV----MYTVPTMLESLYKENRVIENKM-------KIISS-GAK---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 399 iTGAAPVSATVLTFLRAalgcQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYIKLVDVEDMNYQAAKGE-GEVCV 477
Cdd:PRK07638 265 -WEAEAKEKIKNIFPYA----KLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEiGTVYV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 478 KGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:PRK07638 339 KSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
232-523 |
1.18e-07 |
|
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: 54.79 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 232 PEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdcsgFIKATESAFIASPEDVLIsFLPLAHMFETVVECVM-LCHGAKIgf 310
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKCILP----NIQHFRSLFNITSEDILF-LTSPLTFDPSVVEIFLsLSSGATL-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 311 fqgdirllmddlkVLQPTIFPVVPRLLNRMFDRIFG----QANTSVKRwllDFASKRKEAELRSGIvrnnslwdklifhk 386
Cdd:cd17654 188 -------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT-------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 iqSSLggKVrLMITGAAPVSATVLTFLRAA-LGCQFYEGYGQTECtagCCLSL----PGDWTAGHVGAPMPCNYIKLVDV 461
Cdd:cd17654 238 --SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEV---SCWALaykvPEEDSPVQLGSPLLGTVIEVRDQ 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 462 EdmnyqAAKGEGEVCVKGANVfKGYLKDPARTAEALdkdgWLHTGDIGKwLPNGTLKIIDRK 523
Cdd:cd17654 310 N-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRK 360
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-566 |
3.16e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSG---FIKATESAFIA--SPEDVLIS---FLPlAHMFETVVECV--MLC 303
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSkvpYLALSEADVIAqtASQSFDISvwqFLA-APLFGARVEIVpnAIA 3946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 304 HgakigffqgDIRLLMDDLKVLQPTIFPVVPRLLNRMF--DRifgQANTSVkRWLL--------DFASKRKEAELRSGIV 373
Cdd:PRK05691 3947 H---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLptgeamppELARQWLQRYPQIGLV 4013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 374 rnNSLwdklifhkiqsslggkvrlmitGAAPVSATVlTFLRAALgcqfyegygqtECTAGCCLSlpgdwtaghVGAPMPC 453
Cdd:PRK05691 4014 --NAY----------------------GPAECSDDV-AFFRVDL-----------ASTRGSYLP---------IGSPTDN 4048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 454 NYIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHI 526
Cdd:PRK05691 4049 NRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958682904 527 -----FKLAQGEyIAPEKIENIYLRSEAVA-QVFVHGESLQAFLIA 566
Cdd:PRK05691 4128 vkirgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLVP 4172
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-581 |
8.84e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 51.61 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 232 PEPEDLAIICfTSGTTGNPKGAMVTHQNImndcsgFIKATESAFIASPEDVLISFLPLAHMFETVVECVMLC---HGAK- 307
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDI------FRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPplmHGTGs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 ----IGFFQGDiRLLMDDLKVLQPTIFPVVPR-LLNRMFdrIFGQAntsVKRWLLDfaskrkeaELRSGivRNNSLwdkl 382
Cdd:cd05924 74 wtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPYDL---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 383 ifhkiqSSLggkvRLMITGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMPcnyiKLVD 460
Cdd:cd05924 134 ------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP----DTVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 VEDMNYQAAKGEGEVCV--KGANVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 535
Cdd:cd05924 200 LDDDGRVVPPGSGGVGWiaRRGHIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKV 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958682904 536 APEKIENIYLRSEAVAQVFVHGeslqafliaivVPDveilPSWAQK 581
Cdd:cd05924 279 FPEEVEEALKSHPAVYDVLVVG-----------RPD----ERWGQE 309
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
231-262 |
1.25e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.97 E-value: 1.25e-06
10 20 30
....*....|....*....|....*....|..
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMN 262
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 625
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
212-571 |
1.51e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.48 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 212 IIGLKALeDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDC----SGFIKATESafIASPEDVLISFL 287
Cdd:PRK05850 138 VIEVDLL-DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGG--VPPPDTTVVSWL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 288 PLAH-MFETVVECV-MLChgakigffqGDIRLLMDDLKVLQPtifpvvP----RLLNRmfdriFGQANTSVKRWLLDFAS 361
Cdd:PRK05850 215 PFYHdMGLVLGVCApILG---------GCPAVLTSPVAFLQR------ParwmQLLAS-----NPHAFSAAPNFAFELAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 362 KRKEAELRSGIvrnnslwdklifhkiqsSLGGkVRLMITGAAPV-SATVLTFLR--AALGcqFYE-----GYGQTECTAG 433
Cdd:PRK05850 275 RKTSDDDMAGL-----------------DLGG-VLGIISGSERVhPATLKRFADrfAPFN--LREtairpSYGLAEATVY 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 434 CCLSLPGD-----------WTAGHVgapMPC---------NY-------IKLVDVEDMNYQAAKGEGEVCVKGANVFKGY 486
Cdd:PRK05850 335 VATREPGQppesvrfdyekLSAGHA---KRCetgggtplvSYgsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGY 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 487 LKDPART-----AEALDK-----DG-WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIeniylrsEAVAQVFV 555
Cdd:PRK05850 412 WQKPEETertfgATLVDPspgtpEGpWLRTGDLG-FISEGELFIVGRIKDLL-IVDGRNHYPDDI-------EATIQEIT 482
|
410
....*....|....*.
gi 1958682904 556 HGEslqafLIAIVVPD 571
Cdd:PRK05850 483 GGR-----VAAISVPD 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
231-292 |
4.26e-06 |
|
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: 49.98 E-value: 4.26e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682904 231 PPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNdCSGFIkateSAFIASPEDVLISFLPLAHM 292
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
222-564 |
8.68e-06 |
|
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: 48.97 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 222 GRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQnimndcSGFIKATE----SAFIASPEDVLISFLPLAHmfetvv 297
Cdd:cd05915 140 ALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHR------ALVLHSLAaslvDGTALSEKDVVLPVVPMFH------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 298 eCVMLCHGAKIGFFQGDI---------RLLMDDLKVLQPTIFPVVPRLLNrmfdrIFGQANTSVKRwlldfaskrkeael 368
Cdd:cd05915 208 -VNAWCLPYAATLVGAKQvlpgprldpASLVELFDGEGVTFTAGVPTVWL-----ALADYLESTGH-------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 369 rsgivrnnslwdklifhkiqsSLGGKVRLMITGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLSLPgDWT--- 443
Cdd:cd05915 268 ---------------------RLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEsls 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 444 ---AGHVGAPMPCN-YIKLVDVEDMNYQAAKGEGE----VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNG 515
Cdd:cd05915 324 eeeKLTLKAKTGLPiPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEG 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682904 516 TLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFL 564
Cdd:cd05915 404 YVEIKDRLKDLIKSG-GEWISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
418-568 |
1.01e-05 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 48.87 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 418 GCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYIKLVdVEDMNYQAAKGEGEVCVKGANVFKGYLKDPArtaEAL 497
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPV 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682904 498 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLIAIV 568
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
395-574 |
1.15e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 48.47 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 395 VRLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpCNYIKLVDvEDMNYQAAKGE 472
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSV-LGDLHICD-DDGNELPAGRI 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 473 GEVCVKGANVFKGYLKDPARTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV 550
Cdd:PRK13390 349 GTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAV 427
|
170 180
....*....|....*....|....
gi 1958682904 551 AQVFVHGeslqafliaivVPDVEI 574
Cdd:PRK13390 428 HDVAVIG-----------VPDPEM 440
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
140-257 |
3.48e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 46.81 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 140 VVVPLYDTLGTDAITYIVNKAELSVIFADKpekaKLLLEGVENKLtPCLKIIVIMDsydnDLVERGQKCgveiIGLKAL- 218
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVLITTP----ALLERKPADDL-PSLKHVLLVG----EDVEEGPGT----LDFNALm 190
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958682904 219 ----EDLgrvnrtKPKPPEPEDLAIICFTSGTTGNPKG------AMVTH 257
Cdd:PRK04319 191 eqasDEF------DIEWTDREDGAILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-555 |
4.84e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.09 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 234 PEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKAtesaFIASPEDvlisflplahmfetvveCVMlcHGAKIGFFQG 313
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIER----FGMRADD-----------------CEL--HFYSINFDAA 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 314 DIRLLmddlkvlqptifpvVPRLLN-RMFDRIFGQantsvkrWlldfaskrkEAELRSGIVRNNSLwDKLIFHKIQSS-- 390
Cdd:PRK05691 2389 SERLL--------------VPLLCGaRVVLRAQGQ-------W---------GAEEICQLIREQQV-SILGFTPSYGSql 2437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 391 ---LGGK-----VRLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTE-------CTAGccLSLPGDWTAGHVGAPMPCN 454
Cdd:PRK05691 2438 aqwLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGAR 2515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 455 YIKLVDvEDMNYQAAKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIF 527
Cdd:PRK05691 2516 VAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQV 2594
|
330 340
....*....|....*....|....*...
gi 1958682904 528 KLaQGEYIAPEKIENIYLRSEAVAQVFV 555
Cdd:PRK05691 2595 KI-RGFRIELGEIESRLLEHPAVREAVV 2621
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
226-557 |
6.05e-05 |
|
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: 46.03 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 226 RTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHqnimndcSGF-IKATES---AFIASPEDVLISFLPLAHMF--ETVVEC 299
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT-------GGYlVYAATTmkyVFDYGPGDIYWCTADVGWVTghSYLLYG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 300 VMLChGAKIGFFQGdirllmddlKVLQPTifpvvPRLLNRMFDR----IFGQANTSVKrwlldfaSKRKEAelrsgivrn 375
Cdd:cd17634 296 PLAC-GATTLLYEG---------VPNWPT-----PARMWQVVDKhgvnILYTAPTAIR-------ALMAAG--------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 376 nslwDKLIFHKIQSSLggkvRLMITGAAPVSATVLTFLRAALG---CQFYEGYGQTECTAGCCLSLPG--DWTAGHVGAP 450
Cdd:cd17634 345 ----DDAIEGTDRSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRP 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 451 MPCNYIKLVDVEDmNYQAAKGEGEVCVKGA--NVFKGYLKDPARTAEALDK--DGWLHTGDIGKWLPNGTLKIIDRKKHI 526
Cdd:cd17634 417 VFGVQPAVVDNEG-HPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDV 495
|
330 340 350
....*....|....*....|....*....|.
gi 1958682904 527 FKLAqGEYIAPEKIENIYLRSEAVAQVFVHG 557
Cdd:cd17634 496 INVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
230-584 |
1.05e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 230 KPPEP--EDLAIICFTSGTTGNPKGAMVTHQNIMNDCSgfikATEsAFIASPEDVLISfLPLAHmfetvvecvmlchgak 307
Cdd:PRK07824 28 RVGEPidDDVALVVATSGTTGTPKGAMLTAAALTASAD----ATH-DRLGGPGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 308 IGFFQGDIRLLmddLKVLQPTIFPVvprllNRMFDrifgqantsvkrwLLDFAskRKEAELRSGiVRNNSLWD-KLIfhK 386
Cdd:PRK07824 86 IAGLQVLVRSV---IAGSEPVELDV-----SAGFD-------------PTALP--RAVAELGGG-RRYTSLVPmQLA--K 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 387 IQSSLGGKVRL-----MITGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLslpgdwtagHVGAPMPCNYIKLVD 460
Cdd:PRK07824 140 ALDDPAATAALaeldaVLVGGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 461 vedmnyqaakgeGEVCVKGANVFKGY--LKDPARTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPE 538
Cdd:PRK07824 208 ------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQ 269
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958682904 539 KIENIYLRSEAVAQVFVHG---ESLQAFLIAIVVPDVEILPSWAQKRGF 584
Cdd:PRK07824 270 VVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALRAH 318
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
227-579 |
5.63e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports 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 FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 42.80 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 227 TKPKPPEPEDL---AIICF--TSGTTGNPKGAMVTHQNIMNDCSGFIKatesAFIASPEDVLISFLPLAHMFETVVeCV- 300
Cdd:cd05939 91 SSTEPPSQDDVnfrDKLFYiyTSGTTGLPKAAVIVHSRYYRIAAGAYY----AFGMRPEDVVYDCLPLYHSAGGIM-GVg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 301 -MLCHGAKIgffqgDIRL------LMDDLKVLQPTIfpvvprllnrmfdrifGQANTSVKRWLLdfASKRKEAELRsgiv 373
Cdd:cd05939 166 qALLHGSTV-----VIRKkfsasnFWDDCVKYNCTI----------------VQYIGEICRYLL--AQPPSEEEQK---- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 374 rnnslwdklifHKIQSSLGGKVRLMITgaapvSATVLTFLRAALGcqfyEGYGQTECTAgcclSLpGDWTaGHVGApmpC 453
Cdd:cd05939 219 -----------HNVRLAVGNGLRPQIW-----EQFVRRFGIPQIG----EFYGATEGNS----SL-VNID-NHVGA---C 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 454 NY----------IKLVDVEDMNYQAAKGEGEVCVK------GANV-----------FKGYLKDPArTAEALDKDGWLH-- 504
Cdd:cd05939 270 GFnsrilpsvypIRLIKVDEDTGELIRDSDGLCIPcqpgepGLLVgkiiqndplrrFDGYVNEGA-TNKKIARDVFKKgd 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682904 505 ----TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGESL-----QAFLIAIVVP----D 571
Cdd:cd05939 349 saflSGDVLVMDELGYLYFKDRTGDTFRW-KGENVSTTEVEGILSNVLGLEDVVVYGVEVpgvegRAGMAAIVDPerkvD 427
|
410
....*....|....*.
gi 1958682904 572 VEI--------LPSWA 579
Cdd:cd05939 428 LDRfsavlaksLPPYA 443
|
|
| |
